Pactacin is a novel digestive enzyme in teleosts

Abstract Generally, animals extract nutrients from food by degradation using digestive enzymes. Trypsin and chymotrypsin, one of the major digestive enzymes in vertebrates, are pancreatic proenzymes secreted into the intestines. In this investigation, we report the identification of a digestive tele...

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Autores principales: Mari Kawaguchi, Yohei Okazawa, Aiko Imafuku, Yuko Nakano, Risa Shimizu, Reiji Ishizuka, Tianlong Jiang, Tatsuki Nagasawa, Junya Hiroi, Shigeki Yasumasu
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/7169f27bf9904798a44802b9a010d61d
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spelling oai:doaj.org-article:7169f27bf9904798a44802b9a010d61d2021-12-02T18:18:06ZPactacin is a novel digestive enzyme in teleosts10.1038/s41598-021-86565-92045-2322https://doaj.org/article/7169f27bf9904798a44802b9a010d61d2021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-86565-9https://doaj.org/toc/2045-2322Abstract Generally, animals extract nutrients from food by degradation using digestive enzymes. Trypsin and chymotrypsin, one of the major digestive enzymes in vertebrates, are pancreatic proenzymes secreted into the intestines. In this investigation, we report the identification of a digestive teleost enzyme, a pancreatic astacin that we termed pactacin. Pactacin, which belongs to the astacin metalloprotease family, emerged during the evolution of teleosts through gene duplication of astacin family enzymes containing six cysteine residues (C6astacin, or C6AST). In this study, we first cloned C6AST genes from pot-bellied seahorse (Hippocampus abdominalis) and analyzed their phylogenetic relationships using over 100 C6AST genes. Nearly all these genes belong to one of three clades: pactacin, nephrosin, and patristacin. Genes of the pactacin clade were further divided into three subclades. To compare the localization and functions of the three pactacin subclades, we studied pactacin enzymes in pot-bellied seahorse and medaka (Oryzias latipes). In situ hybridization revealed that genes of all three subclades were commonly expressed in the pancreas. Western blot analysis indicated storage of pactacin pro-enzyme form in the pancreas, and conversion to the active forms in the intestine. Finally, we partially purified the pactacin from digestive fluid, and found that pactacin is novel digestive enzyme that is specific in teleosts.Mari KawaguchiYohei OkazawaAiko ImafukuYuko NakanoRisa ShimizuReiji IshizukaTianlong JiangTatsuki NagasawaJunya HiroiShigeki YasumasuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Mari Kawaguchi
Yohei Okazawa
Aiko Imafuku
Yuko Nakano
Risa Shimizu
Reiji Ishizuka
Tianlong Jiang
Tatsuki Nagasawa
Junya Hiroi
Shigeki Yasumasu
Pactacin is a novel digestive enzyme in teleosts
description Abstract Generally, animals extract nutrients from food by degradation using digestive enzymes. Trypsin and chymotrypsin, one of the major digestive enzymes in vertebrates, are pancreatic proenzymes secreted into the intestines. In this investigation, we report the identification of a digestive teleost enzyme, a pancreatic astacin that we termed pactacin. Pactacin, which belongs to the astacin metalloprotease family, emerged during the evolution of teleosts through gene duplication of astacin family enzymes containing six cysteine residues (C6astacin, or C6AST). In this study, we first cloned C6AST genes from pot-bellied seahorse (Hippocampus abdominalis) and analyzed their phylogenetic relationships using over 100 C6AST genes. Nearly all these genes belong to one of three clades: pactacin, nephrosin, and patristacin. Genes of the pactacin clade were further divided into three subclades. To compare the localization and functions of the three pactacin subclades, we studied pactacin enzymes in pot-bellied seahorse and medaka (Oryzias latipes). In situ hybridization revealed that genes of all three subclades were commonly expressed in the pancreas. Western blot analysis indicated storage of pactacin pro-enzyme form in the pancreas, and conversion to the active forms in the intestine. Finally, we partially purified the pactacin from digestive fluid, and found that pactacin is novel digestive enzyme that is specific in teleosts.
format article
author Mari Kawaguchi
Yohei Okazawa
Aiko Imafuku
Yuko Nakano
Risa Shimizu
Reiji Ishizuka
Tianlong Jiang
Tatsuki Nagasawa
Junya Hiroi
Shigeki Yasumasu
author_facet Mari Kawaguchi
Yohei Okazawa
Aiko Imafuku
Yuko Nakano
Risa Shimizu
Reiji Ishizuka
Tianlong Jiang
Tatsuki Nagasawa
Junya Hiroi
Shigeki Yasumasu
author_sort Mari Kawaguchi
title Pactacin is a novel digestive enzyme in teleosts
title_short Pactacin is a novel digestive enzyme in teleosts
title_full Pactacin is a novel digestive enzyme in teleosts
title_fullStr Pactacin is a novel digestive enzyme in teleosts
title_full_unstemmed Pactacin is a novel digestive enzyme in teleosts
title_sort pactacin is a novel digestive enzyme in teleosts
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/7169f27bf9904798a44802b9a010d61d
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