Document Detail


Isolation and characterization of rat fetal Sertoli cells.
MedLine Citation:
PMID:  2840259     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Sertoli cells were prepared from fetal rats, aged 15, 18, and 21 days. Cultures of these cells can be prepared at a purity of 85% by a method that is widely used to prepare the same cells from postnatal rats. The fetal cells are identical in appearance to postnatal Sertoli cells. Fetal Sertoli cells round up in response to (Bu)2cAMP, but not in response to FSH. Protein synthesis in the cells is not stimulated by (Bu)2cAMP or FSH. However, incorporation of [35S]methionine into secreted proteins appearing in the incubation medium is stimulated by the cyclic nucleotide, but not by FSH. Reproducible patterns for the incorporation of [35S]methionine into cellular and secreted proteins are presented as autoradiograms of one- and two-dimensional electrophoretograms. These autoradiograms show that the response of secreted proteins to (Bu)2cAMP is a general one; most or all proteins participate in the response. No clear differences were observed in the nature of the proteins synthesized when cells from fetal rats of 15, 18, and 21 days of age were compared. Fetal Sertoli cells produced approximately 2 nmol lactate/10(6) cells.h, which is approximately one fifth of the amount produced by postnatal cells. Lactate production was increased by the addition of FSH or (Bu)2cAMP to the medium. Fetal Sertoli cells also synthesize androgen-binding protein, and this activity is not increased by either FSH or (Bu)2cAMP.
Authors:
H Ueda; C Ziomek; P F Hall
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Endocrinology     Volume:  123     ISSN:  0013-7227     ISO Abbreviation:  Endocrinology     Publication Date:  1988 Aug 
Date Detail:
Created Date:  1988-08-29     Completed Date:  1988-08-29     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0375040     Medline TA:  Endocrinology     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1014-22     Citation Subset:  AIM; IM    
Affiliation:
Worcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.
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MeSH Terms
Descriptor/Qualifier:
Androgen-Binding Protein / biosynthesis*
Animals
Bucladesine / pharmacology
Cell Separation
Cells, Cultured
Electrophoresis, Polyacrylamide Gel
Follicle Stimulating Hormone / pharmacology
Gestational Age
Isoelectric Point
Lactates / biosynthesis
Lactic Acid
Male
Methionine / metabolism
Microscopy, Electron
Molecular Weight
Rats
Sertoli Cells / cytology,  drug effects,  metabolism*
Testis / cytology,  embryology*
Grant Support
ID/Acronym/Agency:
AM-28113/AM/NIADDK NIH HHS; AM-34400/AM/NIADDK NIH HHS; FO5-TWO3811/TW/FIC NIH HHS
Chemical
Reg. No./Substance:
0/Androgen-Binding Protein; 0/Lactates; 362-74-3/Bucladesine; 50-21-5/Lactic Acid; 63-68-3/Methionine; 9002-68-0/Follicle Stimulating Hormone

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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