Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It is well known that rat Sertoli cells in culture secrete both testis-specific proteins, such as inhibin and androgen binding protein (ABP), and proteins which are very similar, if not identical, to serum proteins, such as transferrin (TF), ceruloplasmin, and IGF-I. It is also well known that very few data have been reported about the secretory activity and the hormonal regulation of the Sertoli cell in man, mainly because of the difficulties associated with the isolation of pure cell populations from human tissue. Using histoimmunochemical techniques we tried to localize, with specific antisera, Sertoli cell proteins and, when possible, their receptors in the human testis. The results obtained with our Light Microscopy studies suggest that: (1) human Sertoli cells produce and/or store transferrin (TF), IGF-I, an albumin-like protein and ABP; (2) TF receptors are localized in spermatocytes and early spermatids and are absent in spermatogonia, in the cytoplasm of Sertoli cells and in differentiated spermatids; (3) IGF-I type I receptors are localized in the same germ cells and in the cytoplasm of Sertoli cells. The results obtained with our Electron Microscopy studies suggest that TF and IGF-I are internalized through a receptor mediated endocytosis mechanism both in Sertoli cells (basal compartment) and in germ cells (spermatocytes and early spermatids).
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PMID:Sertoli cell proteins in the human seminiferous tubule. 291 7

The secretions of the Sertoli cell were examined with two polyvalent antisera--one prepared against proteins in rat serum and the other against testis-specific proteins in rete testis fluid. These antisera detected 12 serum and 9 testis-specific proteins in rete testis fluid. To determine the origin of these proteins, primary cultures enriched in Sertoli cells were incubated with [35S]methionine, and the radiolabeled proteins in the medium were immunoprecipitated. Gel electrophoresis of the two immunoprecipitates resolved eight serum and nine testis-specific proteins. These two sets of proteins were specifically bound to their respective antiserum and were immunologically distinct. Medium from Sertoli cell cultures contained 10 times more of the testis-specific proteins than did cultures enriched for testicular myoid or interstitial cells. The concentration of the serum proteins in Sertoli cell medium was 5 and 10 times greater, respectively, than in myoid or interstitial cell preparations. The proteins from Sertoli cells were next characterized on two-dimensional gels. Seven of the proteins recognized by antiserum against serum proteins had identical molecular weights and isoelectric points as serum proteins. Three of these proteins were ceruloplasmin, transferrin, and glycoprotein 2. In addition to the proteins immunoprecipitated by the two antisera, more than 60 other proteins were detected on two-dimensional gels of the total secretory proteins. We conclude that the Sertoli cell secretes many proteins, some of which are specific to the testis and others of which are similar to serum proteins.
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PMID:Sertoli cells secrete both testis-specific and serum proteins. 695 Mar 98