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  • 1.
    Apitanyasai, Kantamas
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology. Chulalongkorn Univ, Dept Biochem, Ctr Excellence Mol Biol & Genom Shrimp, Fac Sci, 254 Phayathai Rd, Bangkok 10330, Thailand..
    Noonin, Chadanat
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Tassanakajon, Anchalee
    Chulalongkorn Univ, Dept Biochem, Ctr Excellence Mol Biol & Genom Shrimp, Fac Sci, 254 Phayathai Rd, Bangkok 10330, Thailand..
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Characterization of a hemocyte homeostasis-associated-like protein (HHAP) in the freshwater crayfish Pacifastacus leniusculus2016In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 58, p. 429-435Article in journal (Refereed)
    Abstract [en]

    Hemocyte homeostasis-associated-like protein (HHAP) in the freshwater crayfish Pacifastacus leniusculus has a distinct role from that of its homolog PmHHAP in the shrimp Penaeus monodon. Knockdown of PIHHAP in vitro using double-stranded RNA (dsRNA) had no effect on the cell morphology of hematopoietic tissue (HPT) cells. The total hemocyte number and caspase activity were unchanged after PIHHAP knockdown in vivo, in contrast to the results found in shrimp. Moreover, suppression of PIHHAP both in vitro and in vivo did not change the mRNA levels of some genes involved in hematopoiesis and hemocyte homeostasis. Interestingly, bacterial count and scanning electron microscope revealed that depletion of PIHHAP in intestine by RNAi resulted in higher number of bacteria in the crayfish intestine. Together, these results suggest that PIHHAP is not involved in hemocyte homeostasis in the crayfish P. leniusculus but appears to affect the bacterial number in the intestine through an unknown mechanism. Since PIHHAP has different functions from PmHHAP, we therefore named it HHAP-like protein.

  • 2.
    Aspan, A
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Huang, TS
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    CDNA CLONING OF PROPHENOLOXIDASE FROM THE FRESH-WATER CRAYFISH PACIFASTACUS-LENIUSCULUS AND ITS ACTIVATION1995In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 92, no 4, p. 939-943Article in journal (Refereed)
    Abstract [en]

    Prophenoloxidase (proPO), an enzyme that is the terminal component of the so-called proPO activating system, a defense and recognition system in crustaceans and insects, has been purified and cloned from a crayfish blood cell cDNA library. The deduced ami

  • 3. Aspan, Anna
    et al.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    The prophenoloxidase activating system in invertebrates; assays of the prophenoloxidase activating enzyme and phenoloxidase.1995In: Techniques in Fish Immunology 4, 161-171, 1995Chapter in book (Refereed)
  • 4. Avarre, JC
    et al.
    Michelis, R
    Hall, M
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    Khayat, M
    Tietz, A
    Lubzens, E
    Lipid composition during sexual development of the noble crayfish Asyacus astacus and effect of a fungal infection2002In: Invertebrate Reproduction and Development, Vol. 41, no 1-3, p. 251-259Article in journal (Refereed)
  • 5. Bachere, E
    et al.
    Fuchs, R
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Shrimp immunity and disease control2000In: AQUACULTUREArticle in journal (Refereed)
  • 6. Ballesteros, I.
    et al.
    Martin, M.P.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Telleria, M.T.
    Dieguez-Uribeondo, J.
    Lack of specificity of the molecular diagnosis method for identification of Aphanomyces astaci2007In: BFPP-CONNAISSANCE ET GESTION DU PATRIMOINE AQUATIQUE, ISSN 1297-6318, no 385, p. 17-24Article in journal (Refereed)
    Abstract [en]

    A recent PCR-test developed for identification of Aphanomyces astaci, the organism responsible for crayfish plague, provided false positives for Aphanomyces frigidophilus, Aphanomyces repetans, and some Saprolegnia spp. Real-time PCR showed that with the designed primers, A. astaci and A. frigidophilus cannot be distinguished. The results of this study show that this particular crayfish plague PCR-test ought to be improved and that molecular-based techniques need to be contrasted to histological evidences and disease history.

  • 7.
    Bangyeekhun, E
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Molecular cloning and characterization of two serine proteinase genes from the crayfish plague fungus, Aphanomyces astaci2001In: Journal of Invertebrate Pathology, ISSN 0022-2011, E-ISSN 1096-0805, Vol. 77, no 3, p. 206-216Article in journal (Refereed)
    Abstract [en]

     

    Two novel genes encoding the serine proteinases, subtilisin (AaSP1) and trypsin (AaSP2), from Aphanomyces astaci were identified. Based on the amino acidconsensus sequences around the catalytic triad of these serine proteinases, degenerated oligonucleotides were designed for isolation of serine proteinase genes from a genomic DNA library. The AaSP1 gene encodes a full-length protein of 515 amino acids as a large precursor of 56 kDa. After cleavage of a predicted leader sequence of 18 residues and a prepeptide of 133 amino acids, the mature enzyme of 364 amino acids is generated with a calculated molecular mass of 39 kDa and a pI of 6.0. The primary sequence of AaSP1 showed similarity to both bacterial subtilisin and fungal subtilisin-like serine proteinases. Southern blot analysis of AaSP1 revealed the presence of at least two subtilisin genes in the A. astaci genome. Northern blot analysis indicated that the size of AaSP1 transcript was 1.6 kb. The AaSP2 gene encodes a prepropeptide of 276 amino acids with a molecular mass of 29 kDa. A mature protein of 237 amino acids is probably generated after cleavage of a 17-residue signal peptide and a 21-amino-acid prepeptide with a predicted molecular mass of 25 kDa and a pI of 6.0. The primary sequence of AaSP2 showed similarity to trypsin enzymes from various organisms. Southern blot analysis revealed the presence of multiple trypsin genes in the A. astaci genome. Northern blot analysis indicated that the size of AaSP2 transcript was 1.0 kb. The regulation of AaSP2 transcription was not controlled by nitrogen catabolic repression. However, the expression of AaSP2 was found to be specifically induced by crayfish plasma, implying a role in pathogenesis toward the crayfish host.

  • 8.
    Bangyeekhun, E
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Ryynänen, H J
    Henttonen, P
    Huner, J V
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Sequence analysis of the ribosomal internal transcribed spacer DNA of the crayfish parasite Psorospermium haeckeli.2001In: Diseases of Aquatic Organisms, ISSN 0177-5103, E-ISSN 1616-1580, Vol. 46, no 3, p. 217-22Article in journal (Refereed)
    Abstract [en]

    Two morphotypes of the crayfish parasite Psorospermium haeckeli were isolated from 2 crayfish species of different geographical origin. The oval-shaped sporocysts were obtained from the epidermal and connective tissue beneath the carapace of the noble crayfish Astacus astacus fromSweden and Finland. Elongated spores were isolated from the abdominal muscle tissue of the red swamp crayfish Procambarus clarkii from USA. To compare genetic divergence of 2 morphotypes of the parasite, the ribosomal internal transcribed spacer (ITS) DNA (ITS 1 and ITS 2) and the 5.8S rRNAgene were cloned and sequenced. The analysed region is variable in length, with the ribosomal ITS sequence of the European morphotype longer than the North American one. Sequence diversity is found mainly in ITS 1 and ITS 2 regions, and there is 66% and 58% similarity between the 2 morphotypes,respectively. Thus, analysis of the ribosomal ITS DNA suggests that P. haeckeli forms obtained from Europe and North America are genetically diverse, which supports the previously reported morphological characteristics.

  • 9. Barracco, M A
    et al.
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Effect of fixed epimastigote forms of Trypanosoma cruzi on the hemocytes and the prophenoloxidase-activating system of the crayfish Pacifastacus leniusculus.1996In: Braz J Med Biol Res, ISSN 0100-879X, Vol. 29, no 10, p. 1321-7Article in journal (Refereed)
  • 10. Barracco, MA
    et al.
    Soderhall, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Effect of fixed epimastigote forms of Trypanosoma cruzi on the hemocytes and the prophenoloxidase-activating system of the crayfish Pacifastacus leniusculus1996In: BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH, ISSN 0100-879X, Vol. 29, no 10, p. 1321-1327Article in journal (Refereed)
    Abstract [en]

    The effect of the parasite Trypanosoma cruzi on the hemocytes and the prophenoloxidase (proPO)-activating system of the crayfish Pacifastacus leniusculus was studied. Incubation of the crayfish hemocyte lysate with fixed epimastigote forms of the parasite

  • 11.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Andersson, M. Gunnar
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, The Linnaeus Centre for Bioinformatics.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Aphanomyces astaci and crustaceans.2009In: Oomycete Genetics and Genomics.: Diversity, Interactions, and Research Tools. / [ed] Kurt Lamour and Sophien Kamoun, Hoboken, New Jersey: John Wiley & Sons, Inc. , 2009, p. 425-433Chapter in book (Other academic)
  • 12.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Babu, Ramesh
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Jiravanichpaisal, Pikul
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    In vitro effects on bacterial growth of phenoloxidase reaction products2010In: Journal of Invertebrate Pathology, ISSN 0022-2011, E-ISSN 1096-0805, Vol. 103, no 1, p. 21-23Article in journal (Refereed)
    Abstract [en]

    An active phenoloxidase preparation from the freshwater crayfish Pacifastacus leniusculus exhibited a strong antibacterial effect in vitro on the bacteria Aeromonas hydrophila, Escherichia coli, Streptococcus pneumoniae whereas a weaker but still significant effect against Bacillus cereus, Pseudomonas aeruginosa and Staphylococcus aureus. In most cases reduction of bacterial growth was stronger when dopamine was used as substrate as compared to L-dopa. The effect on bacteria was abolished if no substrate was available for the phenoloxidase or in the presence of the phenoloxidase inhibitor phenylthiourea.

  • 13.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology. Jämförande fysiologi.
    Bangyeekhun, Eakaphun
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology. Jämförande fysiologi.
    Keyser, Pia
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology. jämförande fysiologi.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology. jämförande fysiologi.
    Host prophenoloxidase expression in freshwater crayfish is linked to increased resistance to the crayfish plague fungus, Aphanomyces astaci.2003In: Cell Microbiol, ISSN 1462-5814, Vol. 5, no 5, p. 353-7Article in journal (Refereed)
  • 14.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Haipeng, Liu
    State Key Laboratory of Marine Environmental Science, College of Oceanography and Environmental Science, Xiamen University, Xiamen, 361005 Fujian, China.
    Zhang, Yanjiao
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Rimphanitchayakit, Vichien
    Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
    Tassanakajon, Anchalee
    Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
    Andersson, M. Gunnar
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, The Linnaeus Centre for Bioinformatics.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    High sequence variability among hemocyte-specific Kazal-type proteinase inhibitors in decapod crustaceans2010In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 34, no 1, p. 69-75Article in journal (Refereed)
    Abstract [en]

    Crustacean hemocytes were found to produce a large number of transcripts coding for Kazal-type proteinase inhibitors (KPIs). A detailed study performed with the crayfish Pacifastacus leniusculus and the shrimp Penaeus monodon revealed the presence of at least 26 and 20 different Kazal domains from the hemocyte KPIs, respectively. Comparisons with KPIs from other taxa indicate that the sequences of these domains evolve rapidly. A few conserved positions, e.g. six invariant cysteines were present in all domain sequences whereas the position of P1 amino acid, a determinant for substrate specificity, varied highly. A study with a single crayfish animal suggested that even at the individual level considerable sequence variability among hemocyte KPIs produced exist. Expression analysis of four crayfish KPI transcripts in hematopoietic tissue cells and different hemocyte types suggest that some of these KPIs are likely to be involved in hematopoiesis or hemocyte release as they were produced in particular hemocyte types or maturation stages only.

  • 15.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Kawabata, Shun-ichiro
    Lee, Bok Luel
    Nonaka, Masaru
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Proteolytic cascades and their involvement in invertebrate immunity2010In: TIBS -Trends in Biochemical Sciences. Regular ed., ISSN 0968-0004, E-ISSN 1362-4326, Vol. 35, no 10, p. 575-583Article, review/survey (Refereed)
    Abstract [en]

    Bacteria and other potential pathogens are cleared rapidly from the body fluids of invertebrates by the immediate response of the innate immune system. Proteolytic cascades, following their initiation by pattern recognition proteins, control several such reactions, notably coagulation, melanisation, activation of the Toll receptor and complement-like reactions. However, there is considerable variation among invertebrates and these cascades, although widespread, are not present in all phyla. In recent years, significant progress has been made in identifying and characterizing these cascades in insects. Notably, recent work has identified several connections and shared principles among the different pathways, suggesting that cross-talk between them may be common.

  • 16.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Kawabata, Shun-ichiro
    Kyushu University, Fukuoka, Japan.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Biological and Immunological Aspects of Innate Defence Mechanisms Activated by (1,3)- β -Glucans and Related Polysaccharides in Invertebrates2009In: Chemistry, Biochemistry and Biology of (1-›3)-β-Glucans and Related Polysaccharides. / [ed] Antony Bacic, Geoffrey B. Fincher & Bruce A. Stone, Burlington, MA: Academic Press , 2009, p. 563-577Chapter in book (Other academic)
    Abstract [en]

    (1,3)- β -glucans are powerful stimulants of a wide variety of innate defence reactions in invertebrates. These polysaccharides exert a great influence on reactions such as induction of antimicrobial peptides, cellular defence such as encapsulation and phagocytosis, and on the melanization and coagulation cascades. In most cases, these reactions set up an effective defence against microorganisms containing (1,3)- β -glucans or (1,3;1,6)- β -glucans in their outer structures (i.e. mainly fungi and oomycetes).

     

  • 17.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Lee, Bok Luel
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    The proPO-system: pros and cons for its role in invertebrate immunity2008In: Trends in immunology, ISSN 1471-4906, E-ISSN 1471-4981, Vol. 29, no 6, p. 263-271Article, review/survey (Refereed)
    Abstract [en]

    Melanisation is an important immune response in many invertebrates. Recent evidence also strongly implies that the melanisation (prophenoloxidase activating) cascade is intimately associated with the appearance of factors stimulating cellular defence by aiding phagocytosis and encapsulation reactions. However, some controversy exists in the field, and at least in flies and mosquitoes, the successful combat of some pathogens does not seem to be dependent on phenoloxidase activity. This may be because of redundancy among separate immune mechanisms, inappropriate testing, species differences or a combination thereof. Recently, by using RNA interference against phenoloxidase or in specific host-pathogen interactions where the pathogen prevents melanin production by the host, convincing data have confirmed the importance of this cascade in invertebrate innate immunity.

  • 18.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Coagulation in invertebrates2011In: Journal of Innate Immunity, ISSN 1662-811X, Vol. 3, no 1, p. 3-8Article, review/survey (Refereed)
    Abstract [en]

    In most animals there is a need to quickly prevent the loss of blood or equivalent fluids through inflicted injuries. In invertebrates with an open circulatory system (and sometimes a hydroskeleton as well) these losses may otherwise soon be fatal. Also, there is a need to prevent microbes that have gained access to the body through the wound from disseminating throughout the open circulatory system. Therefore, many invertebrates possess a coagulation system to prevent such accidents from having too serious consequences. In this review we discuss recent developments in a few animals - mainly arthropods - where more detailed data are available. It is likely, however, that corresponding systems are present in most phyla, but this is still unchartered territory.

  • 19.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Commentary: variable immune molecules in invertebrates2013In: Journal of Experimental Biology, ISSN 0022-0949, E-ISSN 1477-9145, Vol. 216, no 23, p. 4313-4319Article in journal (Other academic)
    Abstract [en]

    Recently it has become evident that invertebrates may mount a highly variable immune response that is dependent on which pathogen is involved. The molecular mechanisms behind this diversity are beginning to be unravelled and in several invertebrate taxa immune proteins exhibiting a broad range of diversity have been found. In some cases, evidence has been gathered suggesting that this molecular diversity translates into the ability of an affected invertebrate to mount a defence that is specifically aimed at a particular pathogen.

  • 20.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Crayfish immunity: Recent findings2018In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 80, p. 94-98Article in journal (Refereed)
    Abstract [en]

    Freshwater crayfish is an important commodity as well as a successful model for studies on crustacean immunity. Due to the ease with which they are kept and the available methods for hemocyte separation and culture they have proven to be very useful. Here, recent progress regarding pattern recognition, immune effector production and antiviral mechanisms are discussed. Several cases of functional resemblance between vertebrate complement and the crayfish immune reactions are highlighted.

  • 21.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Crustacean immune responses and their implications for disease control2012In: Infectious disease in aquaculture: prevention and control / [ed] Austin, B., Cambridge: Woodhead Publishing Limited, 2012, p. 69-87Chapter in book (Refereed)
    Abstract [en]

    This chapter reviews recent advances in our knowledge of crustacean immunity. Emphasis is given to shrimp due to their importance in aquaculture and trade and to freshwater crayfish since they serve as model organisms for research in crustacean immunology. Crustaceans lack antibodies, interferon and some other components from the mammalian immune arsenal but can still mount an efficient defence against many potential pathogens. Crustacean innate immunity relies on a combination of efficient hemocyte and humoral reactions carried out by plasma proteins.

  • 22.
    Cerenius, Lage
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    CRUSTACEAN IMMUNITY AND COMPLEMENT - A PREMATURE COMPARISON1995In: American Zoologist, ISSN 0003-1569, E-ISSN 2162-4445, Vol. 35, no 1, p. 60-67Article in journal (Refereed)
    Abstract [en]

    The prophenoloxidase activating system constitutes a system for recognition of foreignness in several invertebrates. The system has been especially well studied in crustaceans and it will now be possible to begin structural comparisons between components

  • 23.
    Cerenius, Lage
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Isolation of pattern recognition molecules from crustaceans1995In: Techniques in Fish Immunology 4, 155-160, 1995Chapter in book (Refereed)
  • 24.
    Cerenius, Lage
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Saprolegniaceae; zoospore formation, virulence and pathogenesis in animal hosts.1996In: Biology of lower fungi, 1996, p. 97-116Chapter in book (Refereed)
  • 25.
    Cerenius, Lage
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    The prophenoloxidase-activating system in invertebrates.2004In: Immunol Rev, ISSN 0105-2896, Vol. 198, p. 116-26Article in journal (Refereed)
  • 26. Chaga, O
    et al.
    Lignell, M
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    The haemopoietic cells of the freshwater crayfish Pacifastacus leniusculus1995In: Animal Biology, Vol. 4, p. 59-70Article in journal (Refereed)
  • 27. Diao, Yupu
    et al.
    Lu, Anrui
    Yang, Bing
    Hu, Wenli
    Peng, Qing
    Ling, Qing-Zhi
    Beerntsen, Brenda T.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Ling, Erjun
    Existence of Prophenoloxidase in Wing Discs: A Source of Plasma Prophenoloxidase in the Silkworm, Bombyx mori2012In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 7, no 7, p. e41416-Article in journal (Refereed)
    Abstract [en]

    In insects, hemocytes are considered as the only source of plasma prophenoloxidase (PPO). PPO also exists in the hemocytes of the hematopoietic organ that is connected to the wing disc of Bombyx mori. It is unknown whether there are other cells or tissues that can produce PPO and release it into the hemolymph besides circulating hemocytes. In this study, we use the silkworm as a model to explore this possibility. Through tissue staining and biochemical assays, we found that wing discs contain PPO that can be released into the culture medium in vitro. An in situ assay showed that some cells in the cavity of wing discs have PPO1 and PPO2 mRNA. We conclude that the hematopoietic organ may wrongly release hemocytes into wing discs since they are connected through many tubes as repost in previous paper. In wing discs, the infiltrating hemocytes produce and release PPO probably through cell lysis and the PPO is later transported into hemolymph. Therefore, this might be another source of plasma PPO in the silkworm: some infiltrated hemocytes sourced from the hematopoietic organ release PPO via wing discs.

  • 28. Dieguez-Uribeondo, Javier
    et al.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Dykova, I.
    Gelder, S.R.
    Hentonen, P.
    Jiravanichpaisal, Pikul
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Lom, J.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Pathogens, parasites and ectocommensals.2006In: Atlas of crayfish in Europe: Distribution and Diseases., Publications Scientifiques du Muséum National d'Histoire Naturelle Vol. 64 “Patrimoines Naturels” , 2006, p. 135-155Chapter in book (Other (popular science, discussion, etc.))
  • 29.
    Diéguez-Uribeondo, Javier
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Evolutionary Biology, Physiological Botany.
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Evolutionary Biology, Physiological Botany.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Evolutionary Biology, Physiological Botany.
    Physiological characterization of Saprolegnia parasitica isolates from brown trout1996In: Aquaculture, ISSN 0044-8486, E-ISSN 1873-5622, Vol. 140, no 3, p. 247-257Article in journal (Refereed)
    Abstract [en]

    Saprolegnia parasitica has caused large mortalities in brown trout, Salmo trutta, in Spain. Several strains of Saprolegnia parasitica have been isolated from these epizootics and characterized regarding their physiological adaptation and genetic diversity

  • 30. Diéguez-Uribeondo, Javier
    et al.
    Fregeneda-Grandes, Juan M.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Pérez-Iniesta, Elena
    Aller-Gancedo, José Miguel
    Tellería, M. Teresa
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Martin, María P.
    Re-evaluation of the enigmatic species complex Saprolegnia diclina-Saprolegnia parasitica based on morphological, physiological and molecular data2007In: Fungal Genetics and Biology, ISSN 1087-1845, E-ISSN 1096-0937, Vol. 44, no 7, p. 585-601Article in journal (Refereed)
    Abstract [en]

    The phylogenetic relationships among isolates of the Saprolegnia diclina-Saprolegnia parasitica complex were investigated based on ITS rDNA sequences, and correlated with morphological and physiological characters. The isolates studied belong to five phylogenetically separate clades. The majority of presumed parasitic isolates, mostly isolated from fish lesions, fell within a clade that comprises isolates which has been variously named as S. diclina Type 1, S. parasitica, Saprolegnia salmonis or just as unnamed Saprolegnia sp. Presence of bundles of long-hooked hairs on secondary cysts, high frequency of retracted germination, and oogonia production at 7 degrees C (when occurring) were characteristic of this clade. A single isolate identified as S. diclina Type 2 clustered in a clade along with Saprolegnia ferax isolates. The isolates identified as S. diclina s. str. (S. diclina Type 3) distributed in two clades and appeared closely related to Saprolegnia multispora and to a number of Chilean isolates identified as Saprolegnia australis. The ITS sequences of clade I were almost identical even though the isolates were of diverse geographical origins and showed physiological and morphological differences and variations in their pathogenicity. This suggest these species reproduces clonally even in apparently sexually competent isolates. Adaptation to parasitism in Saprolegnia might have occurred at spore level by the development of long-hooked hairs to facilitate host attachment and selection of a retracting germination. The use of the name S. parasitica should be assigned to isolates of clade I that contained isolates forming cysts with bundles of long-hooked hairs.

  • 31.
    Diéguez-Uribeondo, Javier
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Huang, TS
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Physiological adaptation of an Aphanomyces astaci strain isolated from the freshwater crayfish Procambarus clarkii 1995In: Mycological Research, ISSN 0953-7562, E-ISSN 1469-8102, Vol. 99, no 5, p. 574-578Article in journal (Refereed)
    Abstract [en]

    Physiological, epidemiological and genetical properties of an Aphanomyces astaci strain (Pc) isolated from the warm water crayfish, Procambarus clarkii, were compared to other A. astaci strains isolated from the cold water crayfish Astacus astacus,

  • 32.
    Donpudsa, Suchao
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Rimphanitchayakit, Vichien
    Tassanakajon, Anchalee
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Characterization of two crustin antimicrobial peptides from the freshwater crayfish Pacifastacus leniusculus2010In: Journal of Invertebrate Pathology, ISSN 0022-2011, E-ISSN 1096-0805, Vol. 104, no 3, p. 234-238Article in journal (Refereed)
    Abstract [en]

    The two bacteria-induced crustin genes, Plcrustin1 and Plcrustin2, previously found in the hemocyte cDNA library of Pacifastacus leniusculus, contain the open reading frames of 357 bp encoding a putative protein of 118 amino acid residues and 330 bp encoding a putative protein of 109 amino acid residues, respectively. The carboxyl-terminal part of the two crustins possesses, respectively, 7 and 8 conserved cysteine residues representation of a WAP domain that is found in carcinins and crustins in other several crustaceans. The amino acid sequences of Plcrustin1 and Plcrustin2 show that they belong to type I crustins. In order to characterize their properties and biological activities, the two recombinant crustin proteins were produced in the Escherichia coil expression system. Antimicrobial assays showed that the growth of only one Gram-positive bacterium, Micrococcus luteus M1 11, was inhibited by the recombinant Plcrustin1 and Plcrustin2 with MIC of about 0.07-0.27 mu M and 3.5-8 mu M, respectively. In addition, the study of inhibition mechanism revealed that the antimicrobial activity of the two recombinant crustin proteins was a result of bactericidal effect. However, the two crustins did not exhibit the inhibitory activities against trypsin, chymotrypsin, elastase and subtilisin A.

  • 33.
    Donpudsa, Suchao
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Rimphanitchayakit, Vichien
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Tassanakajon, Anchalee
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Proteinase inhibitory activities of two two-domain Kazal proteinase inhibitors from the freshwater crayfish Pacifastacus leniusculus and the importance of the P2 position in proteinase inhibitory activity2010In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 29, no 5, p. 716-723Article in journal (Refereed)
    Abstract [en]

    Serine proteinase inhibitors are found ubiquitously in living organisms and involved in homeostasis of processes using proteinases as well as innate immune defense. Two two-domain Kazal-type serine proteinase inhibitors (KPIs), KPI2 and KPI8, have been identified from the hemocyte cDNA library of the crayfish Pacifastacus leniusculus. Unlike other KPIs from P. leniusculus, they are found specific to the hernocytes and contain an uncommon P-2 amino acid residue, Gly. To unveil their inhibitory activities, the two KPIs and their domains were over-expressed. By testing against subtilisin, trypsin, chymotrypsin and elastase, the KPI2 was found to inhibit strongly against subtilisin and weakly against trypsin, while the KPI8 was strongly active against only trypsin. With their P-1 Set and Lys residues, the KPI2_domain2 and KPI8_domain2 were responsible for strong inhibition against subtilisin and trypsin, respectively. Mutagenesis of KPI8_domain1 at P-2 amino acid residue from Gly to Pro, mimicking the P-2 residue of KPI8_domain2, rendered the KPI8_domain1 strongly active against trypsin, indicating the important role of P-2 residue in inhibitory activities of the Kazal-type serine proteinase inhibitors. Only the KPI2 was found to inhibit against the extracellular serine proteinases from the pathogenic oomycete of the freshwater crayfish, Aphanomyces astaci.

  • 34. Gu, H F
    et al.
    Lind, M I
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Wieslander, L
    Landegren, U
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    Melefors, O
    Using PRINS for gene mapping in polytene chromosomes.1997In: Chromosome Res, ISSN 0967-3849, Vol. 5, no 7, p. 463-5Article in journal (Refereed)
  • 35.
    Guo, Enen
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Korkut, Gül Gizem
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Jaree, Phattarunda
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    A Pacifastacus leniusculus serine protease interacts with WSSV2017In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 68, p. 211-219Article in journal (Refereed)
    Abstract [en]

    Serine proteases are involved in many critical physiological processes including virus spread and replication. In the present study, we identified a new clip-domain serine protease (PIcSP) in the crayfish Pacifastacus leniusculus hemocytes, which can interact with the White Spot Syndrome Virus (WSSV) envelope protein VP28. It was characterized by a classic clip domain with six strictly conserved Cys residues, and contained the conserved His-Asp-Ser (H-D-S)motif in the catalytic domain. Furthermore, signal peptide prediction revealed that it has a 16-residue secretion signal peptide. Tissue distribution showed that it was mainly located in P. leniusculus hemocytes, and its expression was increased in hemocytes upon WSSV challenge. In vitro knock down of PIcSP decreased both the expression of VP28 and the WSSV copy number in hematopoietic stem (HPT) cells. Accordingly, these data suggest that the new serine protease may be of importance for WSSV infection into hematopoietic cells.

  • 36. Hall, M
    et al.
    Scott, T
    Sugumaran, M
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    Law, J H
    Proenzyme of Manduca sexta phenol oxidase: purification, activation, substrate specificity of the active enzyme, and molecular cloning.1995In: Proc Natl Acad Sci U S A, ISSN 0027-8424, Vol. 92, no 17, p. 7764-8Article in journal (Refereed)
  • 37. Hall, M
    et al.
    van Heusden, M C
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Identification of the major lipoproteins in crayfish hemolymph as proteins involved in immune recognition and clotting.1995In: Biochem Biophys Res Commun, ISSN 0006-291X, Vol. 216, no 3, p. 939-46Article in journal (Refereed)
  • 38. HALL, M
    et al.
    VANHEUSDEN, MC
    SODERHALL, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    IDENTIFICATION OF THE MAJOR LIPOPROTEINS IN CRAYFISH HEMOLYMPH AS PROTEINS INVOLVED IN IMMUNE RECOGNITION AND CLOTTING1995In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, ISSN 0006-291X, Vol. 216, no 3, p. 939-946Article in journal (Refereed)
  • 39. Hall, M
    et al.
    Wang, RG
    van, Antwerpen R
    Sottrup-Jensen, L
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    The crayfish plasma clotting protein: A vitellogenin-related protein responsible for clot formation in crustacean blood1999In: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, Vol. 96, no 5, p. 1965-1970Article in journal (Refereed)
    Abstract [en]

    Coagulation in crayfish blood is based on the transglutaminase-mediated crosslinking of a specific plasma clotting protein. Here we report the cloning of the subunit of this clotting protein from a crayfish hepatopancreas cDNA library. The ORF encodes a p

  • 40. Hernandez-Cortes, Patricia
    et al.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Garcia-Carreno, F
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Trypsin from Pacifastacus leniusculus hepatopancreas: Purification and cDNA cloning of the synthesized zymogen1999In: Biological chemistry (Print), ISSN 1431-6730, E-ISSN 1437-4315, Vol. 380, no 4, p. 499-501Article in journal (Refereed)
    Abstract [en]

    Trypsin was purified from crayfish, Pacifastacus leniusculus, hepatopancreas, and the gene that encoded this enzyme was cloned from a hepatopancreas cDNA library. Crayfish trypsin is synthesized as a zymogen according to the sequence of the putative precu

  • 41. Holmblad, T
    et al.
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Cell adhesion molecules and antioxidative enzymes in a crustacean, possible role in immunity1999In: AQUACULTURE, ISSN 0044-8486, Vol. 172, no 1-2, p. 111-123Article in journal (Refereed)
    Abstract [en]

    The question as to how the immune defence of an invertebrate animal is initiated and coordinated has largely been unanswered. This short review focuses on recent discoveries about crayfish hemolymph proteins, which may play roles in cell adhesion events l

  • 42. Holmblad, T
    et al.
    Thornqvist, PO
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Soderhall, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Johansson, MW
    Identification and cloning of an integrin beta subunit from hemocytes of the freshwater crayfish Pacifastacus leniusculus1997In: Journal of Experimental Zoology, ISSN 0022-104X, Vol. 277, no 3, p. 255-261Article in journal (Other scientific)
    Abstract [en]

    We have cloned and sequenced a beta subunit of integrin from a cDNA library of crayfish hemocytes. This beta integrin shows great similarity to beta integrin subunits from other animals; the highest is towards beta pat-3 from Caenorhabditis elegans follow

  • 43. Huang, Chih-Cheng
    et al.
    Sritunyalucksana, Kallaya
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Song, Yen-Ling
    Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase.2004In: Dev Comp Immunol, ISSN 0145-305X, Vol. 28, no 4, p. 279-94Article in journal (Refereed)
  • 44. Huang, TS
    et al.
    Law, JH
    Soderhall, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Purification and cDNA cloning of ferritin from the hepatopancreas of the freshwater crayfish Pacifastacus leniusculus1996In: EUROPEAN JOURNAL OF BIOCHEMISTRY, ISSN 0014-2956, Vol. 236, no 2, p. 450-456Article in journal (Refereed)
    Abstract [en]

    Ferritin was purified from the hepatopancreas of the freshwater crayfish Pacifastacus leniusculus after injection of iron. It has the same size as horse spleen ferritin (440 kDa) and migrates as two bands, 19 kDa and 20 kDa, respectively, in SDS/PAGE unde

  • 45. Huang, TS
    et al.
    Melefors, O
    Lind, Maria
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    An atypical Iron-Responsive Element (IRE) within crayfish ferritin mRNA and an Iron Regulatory Protein 1 (IRP1)-like protein from crayfish hepatopancreas1999In: INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, ISSN 0965-1748, Vol. 29, no 1, p. 1-9Article in journal (Refereed)
    Abstract [en]

    A putative crayfish iron-responsive element (IRE) is present in the 5'-untranslated region of the crayfish ferritin mRNA. The putative crayfish IRE is in a cap-proximal position and shares most of the structural features of the consensus IRE, but the RNA

  • 46.
    Huang, TS
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Wang, HY
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Lee, SY
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Johansson, MW
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    A cell adhesion protein from the crayfish Pacifastacus leniusculus, a serine proteinase homologue similar to Drosophila masquerade2000In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 275, no 14, p. 9996-10001Article in journal (Refereed)
    Abstract [en]

    A cDNA encoding a protein resembling masquerade, a serine proteinase homologue expressed during embryogenesis, larval, and pupal development in Drosophila melanogaster, was identified in hemocytes of the adult freshwater crayfish, Pacifastacus leniusculus. The crayfish protein is similar to Drosophila masquerade in the following aspects: (a) overall sequence of the serine proteinase domain, such as the position of three putative disulfide bridges, glycine in the place of the catalytic serine residue, and the presence of a substrate-lining pocket typical for trypsins; (b) the presence of several copies of a disulfide-knotted motif in the putative propeptide. This masquerade-like protein is cleaved into a 27-kDa fragment, which could be detected by immunoblot analysis using an affinity-purified antibody against a synthetic peptide in the C-terminal domain of the protein. The 27-kDa protein could be immunoaffinity-purified from hemocyte lysate supernatant and exhibited cell adhesion activity in vitro, indicating that the C-terminal domain of the crayfish masquerade-like protein mediates cell adhesion.

  • 47.
    Jearaphunt, Miti
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Noonin, Chadanat
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Jiravanichpaisal, Pikul
    Nakamura, Seiko
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Tassanakajon, Anchalee
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Caspase-1-like regulation of the proPO-system and role of ppA and caspase-1-like cleaved peptides from proPO in innate immunity2014In: PLoS Pathogens, ISSN 1553-7366, E-ISSN 1553-7374, Vol. 10, no 4, p. e1004059-Article in journal (Refereed)
    Abstract [en]

    Invertebrates rely on innate immunity to respond to the entry of foreign microorganisms. One of the important innate immune responses in arthropods is the activation of prophenoloxidase (proPO) by a proteolytic cascade finalized by the proPO-activating enzyme (ppA), which leads to melanization and the elimination of pathogens. Proteolytic cascades play a crucial role in innate immune reactions because they can be triggered more quickly than immune responses that require altered gene expression. Caspases are intracellular proteases involved in tightly regulated limited proteolysis of downstream processes and are also involved in inflammatory responses to infections for example by activation of interleukin 1ß. Here we show for the first time a link between caspase cleavage of proPO and release of this protein and the biological function of these fragments in response to bacterial infection in crayfish. Different fragments from the cleavage of proPO were studied to determine their roles in bacterial clearance and antimicrobial activity. These fragments include proPO-ppA, the N-terminal part of proPO cleaved by ppA, and proPO-casp1 and proPO-casp2, the fragments from the N-terminus after cleavage by caspase-1. The recombinant proteins corresponding to all three of these peptide fragments exhibited bacterial clearance activity in vivo, and proPO-ppA had antimicrobial activity, as evidenced by a drastic decrease in the number of Escherichia coli in vitro. The bacteria incubated with the proPO-ppA fragment were agglutinated and their cell morphology was altered. Our findings show an evolutionary conserved role for caspase cleavage in inflammation, and for the first time show a link between caspase induced inflammation and melanization. Further we give a more detailed understanding of how the proPO system is regulated in time and place and a role for the peptide generated by activation of proPO as well as for the peptides resulting from Caspase 1 proteolysis.

  • 48.
    Jimenez-Vega, Florinda
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Yepiz-Plascencia, Gloria
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Vargas-Albores, Francisco
    A single WAP domain-containing protein from Litopenaeus vannamei hemocytes.2004In: Biochem Biophys Res Commun, ISSN 0006-291X, Vol. 314, no 3, p. 681-7Article in journal (Refereed)
  • 49.
    Jiravanichpaisal, P
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Bangyeekhun, E
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Söderhäll, K
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Söderhäll, I
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    Experimental infection of white spot syndrome virus in freshwater crayfish Pacifastacus leniusculus.2001In: Dis Aquat Organ, ISSN 0177-5103, Vol. 47, no 2, p. 151-7Article in journal (Refereed)
  • 50.
    Jiravanichpaisal, Pikul
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Lee, Bok Luel
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Cell-mediated immunity in arthropods: Hematopoiesis, coagulation, melanization and opsonization.2006In: Immunobiology, ISSN 0171-2985, Vol. 211, no 4, p. 213-36Article in journal (Refereed)
123 1 - 50 of 146
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