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Evolution of Primary Hemostasis in Early Vertebrates

Hemostasis is a defense mechanism which protects the organism in the event of injury to stop bleeding. Recently, we established that all the known major mammalian hemostatic factors are conserved in early vertebrates. However, since their highly vascularized gills experience high blood pressure and...

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Autores principales: Kim, Seongcheol, Carrillo, Maira, Kulkarni, Vrinda, Jagadeeswaran, Pudur
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2793433/
https://www.ncbi.nlm.nih.gov/pubmed/20037653
http://dx.doi.org/10.1371/journal.pone.0008403
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author Kim, Seongcheol
Carrillo, Maira
Kulkarni, Vrinda
Jagadeeswaran, Pudur
author_facet Kim, Seongcheol
Carrillo, Maira
Kulkarni, Vrinda
Jagadeeswaran, Pudur
author_sort Kim, Seongcheol
collection PubMed
description Hemostasis is a defense mechanism which protects the organism in the event of injury to stop bleeding. Recently, we established that all the known major mammalian hemostatic factors are conserved in early vertebrates. However, since their highly vascularized gills experience high blood pressure and are exposed to the environment, even very small injuries could be fatal to fish. Since trypsins are forerunners for coagulation proteases and are expressed by many extrapancreatic cells such as endothelial cells and epithelial cells, we hypothesized that trypsin or trypsin-like proteases from gill epithelial cells may protect these animals from gill bleeding following injuries. In this paper we identified the release of three different trypsins from fish gills into water under stress or injury, which have tenfold greater serine protease activity compared to bovine trypsin. We found that these trypsins activate the thrombocytes and protect the fish from gill bleeding. We found 27 protease-activated receptors (PARs) by analyzing zebrafish genome and classified them into five groups, based on tethering peptides, and two families, PAR1 and PAR2, based on homologies. We also found a canonical member of PAR2 family, PAR2-21A which is activated more readily by trypsin, and PAR2-21A tethering peptide stops gill bleeding just as trypsin. This finding provides evidence that trypsin cleaves a PAR2 member on thrombocyte surface. In conclusion, we believe that the gills are evolutionarily selected to produce trypsin to activate PAR2 on thrombocyte surface and protect the gills from bleeding. We also speculate that trypsin may also protect the fish from bleeding from other body injuries due to quick contact with the thrombocytes. Thus, this finding provides evidence for the role of trypsins in primary hemostasis in early vertebrates.
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spelling pubmed-27934332009-12-24 Evolution of Primary Hemostasis in Early Vertebrates Kim, Seongcheol Carrillo, Maira Kulkarni, Vrinda Jagadeeswaran, Pudur PLoS One Research Article Hemostasis is a defense mechanism which protects the organism in the event of injury to stop bleeding. Recently, we established that all the known major mammalian hemostatic factors are conserved in early vertebrates. However, since their highly vascularized gills experience high blood pressure and are exposed to the environment, even very small injuries could be fatal to fish. Since trypsins are forerunners for coagulation proteases and are expressed by many extrapancreatic cells such as endothelial cells and epithelial cells, we hypothesized that trypsin or trypsin-like proteases from gill epithelial cells may protect these animals from gill bleeding following injuries. In this paper we identified the release of three different trypsins from fish gills into water under stress or injury, which have tenfold greater serine protease activity compared to bovine trypsin. We found that these trypsins activate the thrombocytes and protect the fish from gill bleeding. We found 27 protease-activated receptors (PARs) by analyzing zebrafish genome and classified them into five groups, based on tethering peptides, and two families, PAR1 and PAR2, based on homologies. We also found a canonical member of PAR2 family, PAR2-21A which is activated more readily by trypsin, and PAR2-21A tethering peptide stops gill bleeding just as trypsin. This finding provides evidence that trypsin cleaves a PAR2 member on thrombocyte surface. In conclusion, we believe that the gills are evolutionarily selected to produce trypsin to activate PAR2 on thrombocyte surface and protect the gills from bleeding. We also speculate that trypsin may also protect the fish from bleeding from other body injuries due to quick contact with the thrombocytes. Thus, this finding provides evidence for the role of trypsins in primary hemostasis in early vertebrates. Public Library of Science 2009-12-23 /pmc/articles/PMC2793433/ /pubmed/20037653 http://dx.doi.org/10.1371/journal.pone.0008403 Text en Kim et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Kim, Seongcheol
Carrillo, Maira
Kulkarni, Vrinda
Jagadeeswaran, Pudur
Evolution of Primary Hemostasis in Early Vertebrates
title Evolution of Primary Hemostasis in Early Vertebrates
title_full Evolution of Primary Hemostasis in Early Vertebrates
title_fullStr Evolution of Primary Hemostasis in Early Vertebrates
title_full_unstemmed Evolution of Primary Hemostasis in Early Vertebrates
title_short Evolution of Primary Hemostasis in Early Vertebrates
title_sort evolution of primary hemostasis in early vertebrates
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2793433/
https://www.ncbi.nlm.nih.gov/pubmed/20037653
http://dx.doi.org/10.1371/journal.pone.0008403
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