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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2020-11-01
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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. |
first_indexed | 2024-03-09T06:33:52Z |
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language | English |
last_indexed | 2024-03-09T06:33:52Z |
publishDate | 2020-11-01 |
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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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