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

0
0

Issued Date

2020

Resource Type

Article

File Type

application/pdf

ISSN

21678359

DOI

10.7717/peerj.10218

Other identifier(s)

2-s2.0-85095877062

Rights

Srinakharinwirot University

Rights Holder(s)

Scopus

Bibliographic Citation

PeerJ. Vol 8, (2020)

Suggested Citation

Sukonset C., Surinlert P., Thongsum O., Watthammawut A., Somrit M., Nakeim J., Weerachatyanukul W., Asuvapongpatana S. Cathepsin D in prawn reproductive system: its localization and function in actin degradation. PeerJ. Vol 8, (2020). doi:10.7717/peerj.10218 Retrieved from: https://hdl.handle.net/20.500.14740/5751

Title

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

Author(s)

Sukonset C.
 Surinlert P.
 Thongsum O.
 Watthammawut A.
 Somrit M.
 Nakeim J.
 Weerachatyanukul W.
 Asuvapongpatana S.

Abstract

Cathepsin D (CAT-D) is a well-known aspartic protease that serves a function as housekeeping 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-ArgLeu-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. Copyright 2020 Sukonset et al.

Subject(s)

Actin antibody
 Aldehyde
 Beta actin
 Cathepsin D
 F actin
 Horseradish peroxidase
 Hydrogen peroxide
 Lysosome enzyme
 Paraformaldehyde
 Pepstatin
 Phalloidin
 Phosphate buffered saline
 RNA directed DNA polymerase
 Acrosome
 Amino acid sequence
 Animal cell
 Animal model
 Animal tissue
 Article
 Cell interaction
 Confocal microscopy
 Controlled study
 Densitometry
 Ejaculation
 Enzyme activity
 Epithelium cell
 Genetic transcription
 Genital system
 Glycosylation
 Housekeeping
 Human
 Human cell
 Hydrolysis
 Immunofluorescence
 Immunohistochemistry
 In situ hybridization
 Macrobrachium rosenbergii
 Nonhuman
 Phylogeny
 Protein fingerprinting
 Protein function
 Reverse transcription polymerase chain reaction
 RNA extraction
 SH-SY5Y cell line
 Somatic cell
 Spermatocyte
 Spermatogenesis
 Spermatogonium
 Sustentacular cell
 Testis
 Vas deferens
 Western blotting

View online Resources

Research Projects

Organizational Units

Journal Issue

URI

https://hdl.handle.net/20.500.14740/5751

Collections

Scopus: Year 1983-2021

Endorsement

Review

Supplemented By

Referenced By