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BETA
Söderhäll, Kenneth
Alternative names
Publications (10 of 147) Show all publications
Sirikharin, R., Söderhäll, I. & Söderhäll, K. (2018). Characterization of a cold-active transglutaminase from a crayfish, Pacifastacus leniusculus. Fish and Shellfish Immunology, 80, 546-549
Open this publication in new window or tab >>Characterization of a cold-active transglutaminase from a crayfish, Pacifastacus leniusculus
2018 (English)In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 80, p. 546-549Article in journal (Refereed) Published
Abstract [en]

Transglutaminase (TGase) from signal crayfish (Pacifastacus leniusculus) and its activity at low temperatures was studied. TGase is an abundant protein in the hematopoietic (HPT) cells and this tissue was used for TGase enzyme preparation. The optimal temperature and pH for the activity of crayfish TGase were determined. We found that TGase activity at 4 degrees C showed nearly the same activity as at a temperature of 22 degrees C. TGase activity from crayfish was compared with guinea pig liver TGase activity at 4 degrees C and the crayfish TGase displayed a higher activity while guinea pig liver TGase had a very low activity at this low temperature. By comparing kinetic parameters to guinea pig liver TGase, the results showed that a high activity of crayfish TGase was due to a decreasing K-m value for pentylamine as a substrate, while it did not affect the k(cat) value (at 22 degrees C). The amino acid sequences of a krill and a crayfish TGase, which both are cold adapted, do not give any clue to why these two enzymes are cold-adapted. These results demonstrate that crayfish TGase is adapted to have significant activity at low temperatures and since crayfish are living in quite cold waters this is an interesting adaptation of this enzyme.

Keywords
Cold-adapted enzyme, Crayfish, Transglutaminase
National Category
Immunology
Identifiers
urn:nbn:se:uu:diva-363096 (URN)10.1016/j.fsi.2018.06.042 (DOI)000440958100061 ()29960064 (PubMedID)
Funder
Swedish Research Council, VR 621-2012-2418Swedish Research Council Formas, FORMAS 2011-606
Available from: 2018-10-16 Created: 2018-10-16 Last updated: 2018-10-16Bibliographically approved
Junkunlo, K., Söderhäll, K. & Söderhäll, I. (2018). Clotting protein: An extracellular matrix (ECM) protein involved in crustacean hematopoiesis. Developmental and Comparative Immunology, 78, 132-140
Open this publication in new window or tab >>Clotting protein: An extracellular matrix (ECM) protein involved in crustacean hematopoiesis
2018 (English)In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 78, p. 132-140Article in journal (Refereed) Published
Abstract [en]

Hematopoietic progenitor cells in crustaceans are organized in lobule-like structures surrounded by different types of cells and extracellular matrix (ECM) proteins in a Hematopoietic tissue (HPT). Here we show that the clotting protein (CP) is part of the ECM in HPT and is secreted during HPT cell culture. The formation of a filamentous network of CP was observed in HPT cell culture. A high amount of CP protein was detected at the surfaces of undifferentiated cells (round-shaped) compared with migrating cells (spindle shaped). Co-localization of the CP protein and TGase activity was observed on the cell surface and filamentous network between cells. A role for CP together with collagen was revealed in a 3D culture in which a collagen-I matrix was immobilized with CP or supplemented with CP. The results showed possible functions of CP, collagen, TGase and the cytokine Ast1 in the regulation of HPT progenitor cell behavior. This is the first study to provide insight into the role of CP, which probably not only participates in clot formation but also functions as an ECM component protein controlling hematopoietic stem cell behavior.

Keywords
Clotting protein, ECM, Hematopoiesis, Crustacean
National Category
Zoology
Identifiers
urn:nbn:se:uu:diva-340667 (URN)10.1016/j.dci.2017.09.017 (DOI)000413881000014 ()28943319 (PubMedID)
Funder
Swedish Research Council, 621-2012-2416
Available from: 2018-02-05 Created: 2018-02-05 Last updated: 2018-02-05Bibliographically approved
Cerenius, L. & Söderhäll, K. (2018). Crayfish immunity: Recent findings. Developmental and Comparative Immunology, 80, 94-98
Open this publication in new window or tab >>Crayfish immunity: Recent findings
2018 (English)In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 80, p. 94-98Article in journal (Refereed) Published
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.

Keywords
Lectin, Pattern recognition, Prophenoloxidase, White spot syndrome virus, Antimicrobial peptide, Complement system
National Category
Physiology
Identifiers
urn:nbn:se:uu:diva-343652 (URN)10.1016/j.dci.2017.05.010 (DOI)000423002100010 ()28502650 (PubMedID)
Available from: 2018-05-09 Created: 2018-05-09 Last updated: 2018-05-09Bibliographically approved
Guo, E., Korkut, G. G., Jaree, P., Söderhäll, I. & Söderhäll, K. (2017). A Pacifastacus leniusculus serine protease interacts with WSSV. Fish and Shellfish Immunology, 68, 211-219
Open this publication in new window or tab >>A Pacifastacus leniusculus serine protease interacts with WSSV
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2017 (English)In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 68, p. 211-219Article in journal (Refereed) Published
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.

Keywords
Hematopoietic tissue, Invertebrate, Serine protease, Virus, WSSV
National Category
Immunology
Identifiers
urn:nbn:se:uu:diva-335858 (URN)10.1016/j.fsi.2017.07.026 (DOI)000411299500022 ()28705723 (PubMedID)
Funder
Swedish Research Council, 621-2012-2418
Available from: 2018-01-24 Created: 2018-01-24 Last updated: 2018-06-26Bibliographically approved
Junkunlo, K., Söderhäll, K., Noonin, C. & Söderhäll, I. (2017). PDGF/VEGF-related receptor affects transglutaminase activity to control cell migration during crustacean hematopoiesis. Stem Cells and Development, 26(20), 1449-1459
Open this publication in new window or tab >>PDGF/VEGF-related receptor affects transglutaminase activity to control cell migration during crustacean hematopoiesis
2017 (English)In: Stem Cells and Development, ISSN 1547-3287, E-ISSN 1557-8534, Vol. 26, no 20, p. 1449-1459Article in journal (Refereed) Published
Abstract [en]

The platelet-derived growth factor (PDGF) receptor, a tyrosine kinase (TK) receptor whose ligand is PDGF, is crucial in the transduction of extracellular signals into cells and mediates numerous processes, such as cell proliferation, differentiation, survival, and migration. We demonstrate the important roles of a receptor TK related to the PDGF/VEGF family protein (PVR) in controlling hematopoietic progenitor cell migration by affecting extracellular transglutaminase (TGase) activity. Pl_PVR1, GenBank accession No. KY444650, is highly expressed in hemocytes and the hematopoietic tissue (HPT). Sunitinib malate was used to block the PVF/PVR downstream pathway in HPT cell culture. The addition of Sunitinib also caused the HPT cells to increase in size and begin spreading. An increase in extracellular TGase activity on the HPT cell membrane was observed in a dose-dependent manner after treatment with Sunitinib malate. The presence of crude Ast1 provided a combinatorial beneficial effect that enhanced the number of spreading cells after inhibition of the Pl_PVR downstream signaling cascade. In addition, an increased immunoreactivity for beta-tubulin and elongation of beta-tubulin filaments were found in Pl_PVR signaling-inhibited cells. The potential roles of PVF/PVR signaling in controlling progenitor cell activity during hematopoiesis in crayfish were investigated and discussed.

Keywords
PDGF/VEGF, hematopoiesis, Transglutaminase, Ast1, crayfish
National Category
Developmental Biology Cell Biology Immunology
Research subject
Biology with specialization in Molecular Biology
Identifiers
urn:nbn:se:uu:diva-327243 (URN)10.1089/scd.2017.0086 (DOI)000412919700001 ()28805145 (PubMedID)
Funder
Swedish Research Council, VR 2011-4797, VR 621-2012-2418
Available from: 2017-08-07 Created: 2017-08-07 Last updated: 2018-01-03Bibliographically approved
Sirikharin, R., Junkunlo, K., Söderhäll, K. & Söderhäll, I. (2017). Role of astakine1 in regulating transglutaminase activity. Developmental and Comparative Immunology, 76, 77-82
Open this publication in new window or tab >>Role of astakine1 in regulating transglutaminase activity
2017 (English)In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 76, p. 77-82Article in journal (Refereed) Published
Abstract [en]

Transglutaminase (TGase) has been implicated in maintaining the undifferentiated stage of hematopoietic stem cells (HSC) in the crayfish Pacifastacus leniusculus. TGase activity has been reported to be regulated by astakine1, an essential crayfish cytokine for inducing new hemocyte synthesis in hematopoietic tissue (HPT). Here, the role of astakine1 in TGase activity regulation and clotting protein (CP) cross-linking was characterized. A reduction in TGase activity was observed by the addition of purified astakine1 in vitro for both endogenous crayfish TGase and a commercial purified guinea pig liver TGase. As a result, we observed that astakine1 inhibits TGase enzyme activity and acts as a non-competitive inhibitor for the TGase enzyme. Additionally, the clotting reaction was impaired in the presence of astakine1. A decrease in TGase-mediated crosslinking of ε(γ-glutamyl)-lysine bonds was also observed in the presence of astakine1. In conclusion, this study shows that astakine1 acts as an inhibitor of TGase activity and that it also affects CP cross-linking during crayfish hematopoiesis.

Place, publisher, year, edition, pages
Elsevier, 2017
Keywords
Astakine1, Clotting protein, Hematopoiesis, Transglutaminase activity
National Category
Developmental Biology Immunology Zoology
Research subject
Biology with specialization in Comparative Physiology
Identifiers
urn:nbn:se:uu:diva-327217 (URN)10.1016/j.dci.2017.05.015 (DOI)000407985100009 ()28528959 (PubMedID)
Funder
Swedish Research Council, VR 621-2012-2418
Available from: 2017-08-07 Created: 2017-08-07 Last updated: 2017-10-09Bibliographically approved
Apitanyasai, K., Noonin, C., Tassanakajon, A., Söderhäll, I. & Söderhäll, K. (2016). Characterization of a hemocyte homeostasis-associated-like protein (HHAP) in the freshwater crayfish Pacifastacus leniusculus. Fish and Shellfish Immunology, 58, 429-435
Open this publication in new window or tab >>Characterization of a hemocyte homeostasis-associated-like protein (HHAP) in the freshwater crayfish Pacifastacus leniusculus
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2016 (English)In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 58, p. 429-435Article in journal (Refereed) Published
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.

Keywords
Pacifastacus leniusculus, Hemocyte homeostasis, RNA interference, Intestine, Aeromonas hydrophila
National Category
Immunology
Identifiers
urn:nbn:se:uu:diva-309995 (URN)10.1016/j.fsi.2016.09.038 (DOI)000387523100051 ()27663854 (PubMedID)
Funder
Swedish Research Council, 2012-2418
Available from: 2016-12-12 Created: 2016-12-09 Last updated: 2017-11-29Bibliographically approved
Soonthornchai, W., Chaiyapechara, S., Jarayabhand, P., Söderhäll, K. & Jiravanichpaisal, P. (2015). Interaction of Vibrio spp. with the Inner Surface of the Digestive Tract of Penaeus monodon. PLoS ONE, 10(8), Article ID e0135783.
Open this publication in new window or tab >>Interaction of Vibrio spp. with the Inner Surface of the Digestive Tract of Penaeus monodon
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2015 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 10, no 8, article id e0135783Article in journal (Refereed) Published
Abstract [en]

Several species of Vibrio are the causative agent of gastroenteritis in humans. In aquaculture, Vibrio harveyi (Vh) and V. parahaemolyticus (Vp) have long been considered as shrimp pathogens in freshwater, brackish and marine environments. Here we show by using scanning electron microscopy (SEM) that Penaeus monodon orally inoculated with each of these two pathogens via an Artemia diet had numerous bacteria attached randomly across the stomach surface, in single and in large biofilm-like clusters 6 h post-infection. A subsequent marked proliferation in the number of V. harveyi within the biofilm-like formations resulted in the development of infections in the stomach, the upper and middle midgut, but neither in the posterior midgut nor the hindgut. SEM also revealed the induced production of peritrichous pili-like structures by the Vp attaching to the stomach lining, whilst only a single polar fibre was seen forming an apparent physical bridge between Vh and the host's epithelium. In contrast to these observations, no such adherences or linkages were seen when trials were conducted with non-pathogenic Vibrio spp. or with Micrococcus luteus, with no obvious resultant changes to the host's gut surface. In naive shrimp, the hindgut was found to be a favorable site for bacteria notably curved, short-rod shaped bacteria which probably belong to Vibrio spp. Data from the current study suggests that pathogens of P. monodon must be able to colonize the digestive tract, particularly the stomach, where chitin is present, and then they use an array of virulent factors and enzymes to infect their host resulting in disease. Oral infection is a better way of mimicking natural routes of infection; investigating the host-bacteria interactions occurring in the digestive tract may lead to new strategies for the prevention or control of bacterial infections in penaeids.

National Category
Biological Sciences
Identifiers
urn:nbn:se:uu:diva-262429 (URN)10.1371/journal.pone.0135783 (DOI)000359666100069 ()26285030 (PubMedID)
Available from: 2015-09-17 Created: 2015-09-15 Last updated: 2017-12-05Bibliographically approved
Kong, L., Lu, A., Guan, J., Yang, B., Li, M., Hillyer, J. F., . . . Ling, E. (2015). Thermolysin Damages Animal Life Through Degradation of Plasma Proteins Enhanced by Rapid Cleavage of Serpins and Activation of Proteases. Archives of Insect Biochemistry and Physiology, 88(1), 64-84
Open this publication in new window or tab >>Thermolysin Damages Animal Life Through Degradation of Plasma Proteins Enhanced by Rapid Cleavage of Serpins and Activation of Proteases
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2015 (English)In: Archives of Insect Biochemistry and Physiology, ISSN 0739-4462, E-ISSN 1520-6327, Vol. 88, no 1, p. 64-84Article in journal (Refereed) Published
Abstract [en]

Thermolysin, a metallopeptidase secreted by pathogenic microbes, is concluded as an important virulence factor due to cleaving purified host proteins in vitro. Using the silkworm Bombyx mori as a model system, we found that thermolysin injection into larvae induces the destruction of the coagulation response and the activation of hemolymph melanization, which results in larval death. Thermolysin triggers the rapid degradation of insect and mammalian plasma proteins at a level that is considerably greater than expected in vitro and/or in vivo. To more specifically explore the mechanism, thermolysin-induced changes to key proteins belonging to the insect melanization pathway were assessed as a window for observing plasma protein cleavage. The application of thermolysin induced the rapid cleavage of the melanization negative regulator serpin-3, but did not directly activate the melanization rate-limiting enzyme prophenoloxidase (PPO) or the terminal serine proteases responsible for PPO activation. Terminal serine proteases of melanization are activated indirectly after thermolysin exposure. We hypothesize that thermolysin induces the rapid degradation of serpins and the activation of proteases directly or indirectly, boosting uncontrolled plasma protein degradation in insects and mammalians.

Keywords
thermolysin, plasma, cleavage
National Category
Physiology Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:uu:diva-241933 (URN)10.1002/arch.21178 (DOI)000346495500007 ()
Available from: 2015-01-26 Created: 2015-01-19 Last updated: 2018-01-11Bibliographically approved
Jearaphunt, M., Noonin, C., Jiravanichpaisal, P., Nakamura, S., Tassanakajon, A., Söderhäll, I. & Söderhäll, K. (2014). Caspase-1-like regulation of the proPO-system and role of ppA and caspase-1-like cleaved peptides from proPO in innate immunity. PLoS Pathogens, 10(4), e1004059
Open this publication in new window or tab >>Caspase-1-like regulation of the proPO-system and role of ppA and caspase-1-like cleaved peptides from proPO in innate immunity
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2014 (English)In: PLoS Pathogens, ISSN 1553-7366, E-ISSN 1553-7374, Vol. 10, no 4, p. e1004059-Article in journal (Refereed) Published
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.

National Category
Immunology
Identifiers
urn:nbn:se:uu:diva-229571 (URN)10.1371/journal.ppat.1004059 (DOI)000342033600027 ()24722332 (PubMedID)
Funder
Swedish Research Council
Available from: 2014-08-11 Created: 2014-08-11 Last updated: 2017-12-05Bibliographically approved
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