Biol Reprod Keystone Symposia Conference on Frontiers in Reproductive Biology & Regulation of Fertility.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kissinger, C.
Right arrow Articles by Griswold, M. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kissinger, C.
Right arrow Articles by Griswold, M. D.
Agricola
Right arrow Articles by Kissinger, C.
Right arrow Articles by Griswold, M. D.

Biology of Reproduction, Vol 27, 233-240, Copyright © 1982 by Society for the Study of Reproduction

ARTICLES

Analysis of Sertoli cell-secreted proteins by two-dimensional gel electrophoresis

C Kissinger, MK Skinner and MD Griswold

The [35S]methionine-labeled proteins secreted from cultured Sertoli cells were analyzed by two-dimensional gel electrophoresis and fluorography. Major polypeptides which were resolved by this procedure were designated by number and further analyzed. Many of these major polypeptides appeared as a series of spots which corresponded to charge isomers. Two of these polypeptides (5 and 6) were shown to be acidic, glycosylated and to comprise the subunits of a dimeric protein of molecular weight 70,000. Some of the polypeptides (4a and 5a) were shown to be secreted from testicular peritubular cells which contaminated the Sertoli cell cultures. However, many of the polypeptides (1,2,3,4,5,5b and 6) were specifically secreted from the Sertoli cells. The fluorogram of the secreted polypeptides obtained from cultured Sertoli cells from 20- or 60-day-old rats were similar to each other but differed from the pattern of polypeptides which were secreted from cultures of Sertoli cells from 10-day-old rats. Polypeptide 3 was identified by immunoprecipitation as testicular transferrin and the synthesis of polypeptide 3 was stimulated when the Sertoli cells were cultured in the presence of follicle-stimulating hormone (FSH), insulin, testosterone and retinol.


This article has been cited by other articles:


Home page
 Br. J. Ophthalmol.Home page
J. H. Kim, J. H. Kim, Y. S. Yu, B.-H. Min, and K.-W. Kim
The role of clusterin in retinal development and free radical damage
Br. J. Ophthalmol., November 1, 2007; 91(11): 1541 - 1546.
[Abstract] [Full Text] [PDF]

Home page
 Endocr. Rev.Home page
D. D. Mruk and C. Y. Cheng
Sertoli-Sertoli and Sertoli-Germ Cell Interactions and Their Significance in Germ Cell Movement in the Seminiferous Epithelium during Spermatogenesis
Endocr. Rev., October 1, 2004; 25(5): 747 - 806.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
J. M. Dufour and K. H. Kim
Cellular and Subcellular Localization of Six Retinoid Receptors in Rat Testis During Postnatal Development: Identification of Potential Heterodimeric Receptors
Biol Reprod, November 1, 1999; 61(5): 1300 - 1308.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1982 by the Society for the Study of Reproduction.