Cathepsin D in prawn reproductive system: its localization and function in actin degradation

Cathepsin D (CAT-D) is a well-known aspartic protease that serves a function as house-keeping lysosomal enzyme in all somatic cells. Its existence in reproductive tissues is highly variable, even in the somatic derived epithelial cells of reproductive tract. In Macrobrachium rosenbergii, existence o...

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Main Authors: Chompoonut Sukonset, Piyaporn Surinlert, Orawan Thongsum, Atthaboon Watthammawut, Monsicha Somrit, Jirasuda Nakeim, Wattana Weerachatyanukul, Somluk Asuvapongpatana
Format: Article
Language:English
Published: PeerJ Inc. 2020-11-01
Series:PeerJ
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Online Access:https://peerj.com/articles/10218.pdf
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author Chompoonut Sukonset
Piyaporn Surinlert
Orawan Thongsum
Atthaboon Watthammawut
Monsicha Somrit
Jirasuda Nakeim
Wattana Weerachatyanukul
Somluk Asuvapongpatana
author_facet Chompoonut Sukonset
Piyaporn Surinlert
Orawan Thongsum
Atthaboon Watthammawut
Monsicha Somrit
Jirasuda Nakeim
Wattana Weerachatyanukul
Somluk Asuvapongpatana
author_sort Chompoonut Sukonset
collection DOAJ
description Cathepsin D (CAT-D) is a well-known aspartic protease that serves a function as house-keeping lysosomal enzyme in all somatic cells. Its existence in reproductive tissues is highly variable, even in the somatic derived epithelial cells of reproductive tract. In Macrobrachium rosenbergii, existence of MrCAT-D and its translational product was detected in both somatic cells (Sertoli-like supporting cells) and developing spermatogenic cells as well as along accessory spermatic ducts. Specifically, MrCAT-D was localized onto the sperm surface rather than within the acrosomal matrix, as evident by similar staining pattern of anti-CAT-D on live and aldehyde fixed sperm. MrCAT-D in testicular extracts and sperm isolates showed active enzyme activities towards its specific fluorogenic substrate (MCA-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys (Dnp)-D-Arg-NH2). MrCAT-D also exerted its function towards hydrolyzing filamentous actin, the meshwork of which is shown to be localized at the junction between germ cells and supporting cells and spermatogonia in M. rosenbergii testicular epithelium. Together, we have localized MrCAT-D transcript and its translational product in both supporting and germ cells of testis and claimed its enzymatic function towards actin degradation, which may be related to sperm release from the epithelial cell interaction.
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spelling doaj.art-3a1378fdb40140668b494562469490432023-12-03T11:00:34ZengPeerJ Inc.PeerJ2167-83592020-11-018e1021810.7717/peerj.10218Cathepsin D in prawn reproductive system: its localization and function in actin degradationChompoonut Sukonset0Piyaporn Surinlert1Orawan Thongsum2Atthaboon Watthammawut3Monsicha Somrit4Jirasuda Nakeim5Wattana Weerachatyanukul6Somluk Asuvapongpatana7Department of Anatomy, Faculty of Science, Mahidol University, Ratchathewee, Bangkok, ThailandChulabhon International College of Medicine, Thammasat University, Prathumtani, Pratumtani, ThailandDepartment of Anatomy, Faculty of Science, Mahidol University, Ratchathewee, Bangkok, ThailandDepartment of Anatomy, Faculty of Medicine, Srinakharinwirot University, Wattana, Bangkok, ThailandDepartment of Anatomy, Faculty of Science, Mahidol University, Ratchathewee, Bangkok, ThailandDepartment of Anatomy, Faculty of Allied Health Science, Buraphar University, Mueng Chonburi, Chonburi, ThailandDepartment of Anatomy, Faculty of Science, Mahidol University, Ratchathewee, Bangkok, ThailandDepartment of Anatomy, Faculty of Science, Mahidol University, Ratchathewee, Bangkok, ThailandCathepsin D (CAT-D) is a well-known aspartic protease that serves a function as house-keeping lysosomal enzyme in all somatic cells. Its existence in reproductive tissues is highly variable, even in the somatic derived epithelial cells of reproductive tract. In Macrobrachium rosenbergii, existence of MrCAT-D and its translational product was detected in both somatic cells (Sertoli-like supporting cells) and developing spermatogenic cells as well as along accessory spermatic ducts. Specifically, MrCAT-D was localized onto the sperm surface rather than within the acrosomal matrix, as evident by similar staining pattern of anti-CAT-D on live and aldehyde fixed sperm. MrCAT-D in testicular extracts and sperm isolates showed active enzyme activities towards its specific fluorogenic substrate (MCA-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys (Dnp)-D-Arg-NH2). MrCAT-D also exerted its function towards hydrolyzing filamentous actin, the meshwork of which is shown to be localized at the junction between germ cells and supporting cells and spermatogonia in M. rosenbergii testicular epithelium. Together, we have localized MrCAT-D transcript and its translational product in both supporting and germ cells of testis and claimed its enzymatic function towards actin degradation, which may be related to sperm release from the epithelial cell interaction.https://peerj.com/articles/10218.pdfCAT-D Testis Sperm Spermatogenesis Actin meshwork
spellingShingle Chompoonut Sukonset
Piyaporn Surinlert
Orawan Thongsum
Atthaboon Watthammawut
Monsicha Somrit
Jirasuda Nakeim
Wattana Weerachatyanukul
Somluk Asuvapongpatana
Cathepsin D in prawn reproductive system: its localization and function in actin degradation
PeerJ
CAT-D
Testis
Sperm
Spermatogenesis
Actin meshwork
title Cathepsin D in prawn reproductive system: its localization and function in actin degradation
title_full Cathepsin D in prawn reproductive system: its localization and function in actin degradation
title_fullStr Cathepsin D in prawn reproductive system: its localization and function in actin degradation
title_full_unstemmed Cathepsin D in prawn reproductive system: its localization and function in actin degradation
title_short Cathepsin D in prawn reproductive system: its localization and function in actin degradation
title_sort cathepsin d in prawn reproductive system its localization and function in actin degradation
topic CAT-D
Testis
Sperm
Spermatogenesis
Actin meshwork
url https://peerj.com/articles/10218.pdf
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