Literature DB >> 11684093

Multiple glutathione S-transferase isoforms are present on male germ cell plasma membrane.

A V Rao1, C Shaha.   

Abstract

Phase II detoxification enzymes, the glutathione S-transferases (GSTs) of 24 kDa are known to be cytosolic enzymes. This study shows that multiple GST isoforms that are 24 kDa in size are present on the extracellular side of the plasma membrane of rat male germ cells. The GST activity of male germ cell plasma membranes is several folds higher than somatic cell plasma membrane GST activity. Isoform composition of the germ cell plasma membrane and the cytosolic pool differ, GSTM5 and GSTPi being absent on the plasma membranes. The molecular masses of the common isoforms are comparable between the two pools and both pools show GST and glutathione peroxidase activity.

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Year:  2001        PMID: 11684093     DOI: 10.1016/s0014-5793(01)02958-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Genome-wide identification of AR-regulated genes translated in Sertoli cells in vivo using the RiboTag approach.

Authors:  Karel De Gendt; Guido Verhoeven; Paul S Amieux; Miles F Wilkinson
Journal:  Mol Endocrinol       Date:  2014-02-25

2.  Gene expression changes are age-dependent and lobe-specific in the brown Norway rat model of prostatic hyperplasia.

Authors:  Carlise R Bethel; Jaideep Chaudhary; Matthew D Anway; Terry R Brown
Journal:  Prostate       Date:  2009-06-01       Impact factor: 4.104

3.  Glucose availability determines silver nanoparticles toxicity in HepG2.

Authors:  Mariusz Zuberek; Dominika Wojciechowska; Damian Krzyzanowski; Sylwia Meczynska-Wielgosz; Marcin Kruszewski; Agnieszka Grzelak
Journal:  J Nanobiotechnology       Date:  2015-10-22       Impact factor: 10.435

  3 in total

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