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Fries, E
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Publications (10 of 17) Show all publications
Wicher, K. B. & Fries, E. (2010). Evolutionary aspects of hemoglobin scavengers. Antioxidants and Redox Signaling, 12(2), 249-259.
Open this publication in new window or tab >>Evolutionary aspects of hemoglobin scavengers
2010 (English)In: Antioxidants and Redox Signaling, ISSN 1523-0864, E-ISSN 1557-7716, Vol. 12, no 2, 249-259 p.Article, review/survey (Refereed) Published
Abstract [en]

With the evolution of fish, systems appeared for the disposal of the hemoglobin (Hb) that was inevitably released from erythrocytes. Thus, a plasma protein that bound free Hb with great affinity, haptoglobin (Hp), evolved from a protease of the innate immune system. In parallel, other proteins appeared (for example, hemopexin and alpha(1)-microglobulin), which bound and mediated the removal of free heme groups. Remarkably, Hp later disappeared in some vertebrate lineages, suggesting that it could also be disadvantageous. In the avian lineage, a soluble protein evolved, possibly from a scavenger receptor, which in some birds seems to have replaced Hp. Among mammals, multimeric forms of Hp appeared independently at two discrete times, suggesting that this form of the protein confers an advantage on the bearer, possibly by improving resistance to infection.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-138203 (URN)10.1089/ars.2009.2760 (DOI)000273181600007 ()19650711 (PubMedID)
Available from: 2010-12-16 Created: 2010-12-16 Last updated: 2017-12-11Bibliographically approved
Wicher, K. B. & Fries, E. (2007). Convergent evolution of human and bovine haptoglobin: partial duplication of the genes. Journal of Molecular Evolution, 65(4), 373-379.
Open this publication in new window or tab >>Convergent evolution of human and bovine haptoglobin: partial duplication of the genes
2007 (English)In: Journal of Molecular Evolution, ISSN 0022-2844, E-ISSN 1432-1432, Vol. 65, no 4, 373-379 p.Article in journal (Refereed) Published
Abstract [en]

Haptoglobin (Hp) is a hemoglobin-binding plasma protein consisting of two types of chains, called α and β, which originate from a common polypeptide. In humans, but not in other mammals, Hp has been shown to occur in two allelic forms, Hp1 and Hp2, which differ in the length of the α-chain. The longer α-chain (in Hp2) seems to have arisen by an internal duplication of a gene segment coding for almost the entire α-chain of Hp1. In this article we show that Hp of cow (Bos taurus) contains an α-chain, the structure of which is similar to that of the human Hp2 α-chain. Furthermore, comparison of the structure of bovine Hp and human Hp2 suggests that the bovine gene arose by a duplication of the gene segment homologous to that duplicated in human Hp2. However, a phylogenetic analysis indicates that the two genes were formed independently. The evolutionary pressure that has led to the fixation of the Hps with a longer α-chain is not known.

Keyword
Bos Taurus, Convergent evolution, Haptoglobin, Hemoglobin, Human, Partial gene duplication
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-15856 (URN)10.1007/s00239-007-9002-3 (DOI)000250626400002 ()17922076 (PubMedID)
Available from: 2008-03-11 Created: 2008-03-11 Last updated: 2017-12-08Bibliographically approved
Asgeirsson, D., Venturoli, D., Fries, E., Rippe, B. & Rippe, C. (2007). Glomerular sieving of three neutral polysaccharides, polyethylene oxide and bikunin in rat. Effects of molecular size and conformation. Acta Physiologica, 191(3), 237-246.
Open this publication in new window or tab >>Glomerular sieving of three neutral polysaccharides, polyethylene oxide and bikunin in rat. Effects of molecular size and conformation
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2007 (English)In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 191, no 3, 237-246 p.Article in journal (Refereed) Published
Abstract [en]

Aim: Polysaccharides and many other non-protein polymers generally have a more open, flexible and asymmetrical structure compared with globular proteins. For a given molecular weight (MW), the Stokes–Einstein radius (ae) of the following polymers increases in the order: Ficoll < dextran ≤ pullulan < polyethylene oxide (PEO). We have tested the hypothesis that such an increase in 'molecular extension' will increase the molecule's glomerular permeability. Thus, we investigated the glomerular sieving coefficients (θ) of the mentioned polymers and of the negatively charged and extended protein bikunin.

Methods: In anaesthetized Wistar rats, glomerular sieving curves were generated for each FITC-labelled polymer from their respective concentration in urine and plasma, determined by size exclusion chromatography. The θ for bikunin was measured using a tissue uptake technique.

Results: For a molecule of ae = 55 Å (cf. IgG), θ increased in the order: Ficoll (0.00035 ± 0.000013) < dextran (0.022 ± 0.0029) < pullulan (0.033 ± 0.0024) < PEO (0.12 ± 0.0055). For ae = 36 Å (cf. albumin) the order was: Ficoll (0.076 ± 0.0061) < dextran (0.45 ± 0.037) = pullulan (0.45 ± 0.021) < PEO (0.65 ± 0.0076). θ for bikunin (0.089 ± 0.0045) was 150 times higher than that of albumin, having an equivalent ae and net negative charge.

Conclusion: From these results it is concluded that for flexible and asymmetric macromolecules, their degree of glomerular hyperpermeability is proportional to their degree of 'molecular extension'. Thus, compared with globular proteins, the polysaccharides investigated, including Ficoll, were found to be hyperpermeable across the glomerular filter in vivo.

Keyword
capillary permeability, fractional clearance, frictional ratio, Mark-Houwink-Khun-Sakurada
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-13025 (URN)10.1111/j.1748-1716.2007.01733.x (DOI)000250892700007 ()17935524 (PubMedID)
Available from: 2008-01-21 Created: 2008-01-21 Last updated: 2017-12-11Bibliographically approved
Forteza, R., Casalino-Matsuda, S. M., Monzon, M. E., Fries, E., Rugg, M. S., Milner, C. M. & Day, A. J. (2007). TSG-6 Potentiates the Antitissue Kallikrein Activity of Inter-{alpha}-inhibitor through Bikunin Release. American Journal of Respiratory Cell and Molecular Biology, 36(1), 20-31.
Open this publication in new window or tab >>TSG-6 Potentiates the Antitissue Kallikrein Activity of Inter-{alpha}-inhibitor through Bikunin Release
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2007 (English)In: American Journal of Respiratory Cell and Molecular Biology, ISSN 1044-1549, E-ISSN 1535-4989, Vol. 36, no 1, 20-31 p.Article in journal (Refereed) Published
Abstract [en]

TSG-6 (the protein product of TNF-stimulated gene-6), an inflammation-associated protein, forms covalent complexes with heavy chains (HCs) from inter-alpha-inhibitor and pre-alpha-inhibitor and associates noncovalently with their common bikunin chain, potentiating the antiplasmin activity of this serine protease inhibitor. We show that TSG-6 and TSG-6(.)HC complexes are present in bronchoalveolar lavage fluid from patients with asthma and increase after allergen challenge. Immunodetection demonstrated elevated TSG-6 in the airway tissue and secretions of smokers. Experiments conducted in vitro with purified components revealed that bikunin.HC complexes (byproducts of TSG-6.HC formation) release bikunin. Immunoprecipitation revealed that bikunin accounts for a significant proportion of tissue kallikrein inhibition in bronchoalveolar lavage after allergen challenge but not in baseline conditions, confirming that bikunin in its free state, but not when associated with HCs, is a relevant protease inhibitor in airway secretions. In primary cultures of differentiated human airway epithelial and submucosal gland cells, TSG-6 is induced by TNF-alpha and IL-1 beta, which suggests that these cells are responsible for TSG-6 release in vivo. Bikunin and HC3 (i.e., pre-alpha-inhibitor) were also induced by TNF-alpha in primary cultures. Our results suggest that TSG-6 may play an important protective role in bronchial epithelium by increasing the antiprotease screen on the airway lumen.

Keyword
Airway, Bikunin, IαI, Tissue kallikrein, TSG-6
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-22530 (URN)10.1165/rcmb.2006-0018OC (DOI)000243306400004 ()16873769 (PubMedID)
Available from: 2007-01-18 Created: 2007-01-18 Last updated: 2017-12-07Bibliographically approved
Wicher, K. B. & Fries, E. (2006). Haptoglobin, a hemoglobin-binding plasma protein, is present in bony fish and mammals but not in frog and chicken. Proceedings of the National Academy of Sciences of the United States of America, 103(11), 4168-4173.
Open this publication in new window or tab >>Haptoglobin, a hemoglobin-binding plasma protein, is present in bony fish and mammals but not in frog and chicken
2006 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 103, no 11, 4168-4173 p.Article in journal (Refereed) Published
Abstract [en]

Hemoglobin (Hb) released from erythrocytes may cause oxidation of lipids and proteins. Haptoglobin (Hp), which occurs in the plasma of all mammals, binds free Hb and inhibits its oxidative activity. It is not known whether this protective protein also exists in lower vertebrates. By analyzing available genomic sequences, we have found that bony fish, but not more primitive animals, have a gene coding for a protein homologous to mammalian Hp. Furthermore, we show that this protein is present in the plasma of Japanese pufferfish (Takifugu rubripes) and that it binds Hb. These results, together with a phylogenetic analysis, suggest that Hp evolved from a complement-associated protein (mannose-binding lectin-associated serine proteinase, MASP), with the emergence of fish. Surprisingly, we found that both chicken (Gallus gallus) and the Western clawed frog (Xenopus tropicalis) lack the Hp gene. In chicken plasma, however, we identified a different type of Hb-binding protein, PIT54, which has been reported to be a potent antioxidant. PIT54 is a soluble member of the family of scavenger receptor cysteine-rich proteins, and we found that its gene exists only in birds. We also show that the plasma of ostrich (Strutio camelus), a primitive bird, contains both PIT54 and Hp. Collectively, our data suggest that PIT54 has successively taken over the function of Hp during the evolution of the avian lineage and has completely replaced the latter protein in chicken.

Keyword
Amino Acid Sequence, Animals, Birds/genetics, Chickens/genetics, Chromosome Mapping, Evolution; Molecular, Fishes/genetics, Haptoglobins/*genetics, Humans, Invertebrates/genetics, Mammals/genetics, Molecular Sequence Data, Phylogeny, Sequence Homology; Amino Acid, Species Specificity, Xenopus/genetics
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-94049 (URN)10.1073/pnas.0508723103 (DOI)16537503 (PubMedID)
Available from: 2006-02-28 Created: 2006-02-28 Last updated: 2017-12-14Bibliographically approved
Suder, P., Bierczynska-Krzysik, A., Kraj, A., Brostedt, P., Mak, P., Stawikowski, M., . . . Silberring, J. (2006). Identification of bikunin as an endogenous inhibitor of dynorphin convertase in human cerebrospinal fluid. The FEBS Journal, 273(22), 5113-5120.
Open this publication in new window or tab >>Identification of bikunin as an endogenous inhibitor of dynorphin convertase in human cerebrospinal fluid
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2006 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 273, no 22, 5113-5120 p.Article in journal (Refereed) Published
Abstract [en]

Dynorphin-converting enzymes constitute a group of peptidases capable of converting dynorphins to enkephalins. Through the action of these enzymes, the dynorphin-related peptides bind to delta-opioid instead of kappa-opioid receptors, leading to a change in the biological function of the neuropeptides. In this article, we describe the identification of the protein bikunin as an endogenous, competitive inhibitor of a dynorphin-converting enzyme in human cerebrospinal fluid. This protein is present together with its target enzyme in the same body fluids. The K-M value of the convertase was found to be 9 mu M, and the K-i value of the inhibitor was 1.7 nM. The finding indicates that bikunin may play a significant role as a regulatory mechanism of neuropeptides, where one bioactive peptide is converted to a shorter sequence, which in turn, can affect the action of its longer form.

Keyword
bikunin, cerebrospinal fluid, dynorphin conversion, inhibition, opioids
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-22543 (URN)10.1111/j.1742-4658.2006.05508.x (DOI)000241674500010 ()17087727 (PubMedID)
Available from: 2007-03-03 Created: 2007-03-03 Last updated: 2017-12-07Bibliographically approved
Rugg, M. S., Willis, A. C., Mukhopadhyay, D., Hascall, V. C., Fries, E., Fülöp, C., . . . Day, A. J. (2005). Characterization of complexes formed between TSG-6 and inter-alpha-inhibitor that act as intermediates in the covalent transfer of heavy chains onto hyaluronan.. J Biol Chem, 280(27), 25674-86.
Open this publication in new window or tab >>Characterization of complexes formed between TSG-6 and inter-alpha-inhibitor that act as intermediates in the covalent transfer of heavy chains onto hyaluronan.
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2005 (English)In: J Biol Chem, ISSN 0021-9258, Vol. 280, no 27, 25674-86 p.Article in journal (Refereed) Published
Keyword
Alpha-Globulins/*metabolism, Animals, Catalysis, Cell Adhesion Molecules/genetics/*metabolism, Cell Line, Chondroitinases and Chondroitin Lyases/pharmacology, Drosophila, Humans, Hyaluronic Acid/chemistry/*metabolism, In Vitro, Magnesium/metabolism, Manganese/metabolism, Mice, Molecular Weight, Protein Binding/drug effects, Recombinant Proteins/genetics/metabolism, Research Support; Non-U.S. Gov't, Sodium Hydroxide/pharmacology
Identifiers
urn:nbn:se:uu:diva-80330 (URN)15840581 (PubMedID)
Available from: 2006-05-08 Created: 2006-05-08 Last updated: 2011-01-11
Mahoney, D. J., Mulloy, B., Forster, M. J., Blundell, C. D., Fries, E., Milner, C. M. & Day, A. J. (2005). Characterization of the interaction between tumor necrosis factor-stimulated gene-6 and heparin: implications for the inhibition of plasmin in extracellular matrix microenvironments.. J Biol Chem, 280(29), 27044-55.
Open this publication in new window or tab >>Characterization of the interaction between tumor necrosis factor-stimulated gene-6 and heparin: implications for the inhibition of plasmin in extracellular matrix microenvironments.
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2005 (English)In: J Biol Chem, ISSN 0021-9258, Vol. 280, no 29, 27044-55 p.Article in journal (Refereed) Published
Keyword
Alpha-Globulins/metabolism, Cell Adhesion Molecules/genetics/*metabolism, Extracellular Matrix/*metabolism, Heparan Sulfate Proteoglycans/metabolism, Heparin/*metabolism, Humans, Hyaluronic Acid/metabolism, Models; Molecular, Mutagenesis; Site-Directed, Plasmin/*antagonists & inhibitors, Protein Binding, Protein Structure; Tertiary
Identifiers
urn:nbn:se:uu:diva-22546 (URN)15917224 (PubMedID)
Available from: 2007-01-18 Created: 2007-01-18 Last updated: 2011-01-12
Kaczmarczyk, A., Blom, A., Alston-Smith, J., Sjoquist, M. & Fries, E. (2005). Plasma bikunin: half-life and tissue uptake. Mol Cell Biochem, 271((1-2)), 61-7.
Open this publication in new window or tab >>Plasma bikunin: half-life and tissue uptake
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2005 (English)In: Mol Cell Biochem, Vol. 271, no (1-2), 61-7 p.Article in journal (Refereed) Published
Identifiers
urn:nbn:se:uu:diva-72099 (URN)
Available from: 2006-05-05 Created: 2006-05-05 Last updated: 2011-01-11
Kaczmarczyk, A., Blom, A. M., Alston-Smith, J., Sjöquist, M. & Fries, E. (2005). Plasma bikunin: half-life and tissue uptake.. Molecular and Cellular Biochemistry, 271(1-2), 61-67.
Open this publication in new window or tab >>Plasma bikunin: half-life and tissue uptake.
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2005 (English)In: Molecular and Cellular Biochemistry, ISSN 0300-8177, E-ISSN 1573-4919, Vol. 271, no 1-2, 61-67 p.Article in journal (Refereed) Published
Abstract [en]

Bikunin is a chondroitin sulfate-containing plasma protein synthesized in the liver. In vitro, it has been shown to inhibit proteases and to have additional activities, but its biological function is still unclear. Here we have studied the dynamics of plasma bikunin in rats and mice. A half-life of 7 +/- 2 min was obtained from the time course of the decrease of the plasma level of bikunin following hepatectomy. Clearance experiments with intravenously injected radiolabeled bikunin with or without the chondroitin sulfate chain showed that the polysaccharide had little influence on the elimination rate of the protein. The uptake of bikunin by different tissues was studied using bikunin labeled with the residualizing agent 125I-tyramine cellobiose; 60 min after intravenous injection, 49% of the radioactivity was recovered in the kidneys and 6-11% in the liver, bones, skin, intestine and skeletal muscle. The uptake in the liver was analyzed by intravenous injection of radiolabeled bikunin followed by collagenase perfusion and dispersion of the liver cells. These experiments indicated that bikunin is first trapped extracellularly within the liver before being internalized by the cells.

Keyword
bikunin, chondroitin sulfate, half-life, hepatectomy, liver perfusion, tissue distribution, tyramine cellobiose
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-12863 (URN)10.1007/s11010-005-5282-3 (DOI)15881656 (PubMedID)
Available from: 2008-01-18 Created: 2008-01-18 Last updated: 2017-12-11Bibliographically approved
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