Sertoli cells synthesize and secrete transferrin-like protein.

One of the major proteins secreted by Sertoli cells (Band 3) has a molecular weight on sodium dodecyl sulfate-polyacrylamide gels which corresponds to rat serum transferrin. The preparation of Sertoli cell-secreted proteins contains an iron-binding protein with electrophoretic properties on native polyacrylamide gels similar to serum transferrin. Antibodies against Sertoli cell-secreted proteins contain a component which will immunoprecipitate serum transferrin. Antibodies to serum transferrin cross-react with and immunoprecipitate a major component (Band 3) of [35S]-methionine-labeled Sertoli cell-secreted proteins. We propose that testicular transferrin is a major secretory product of Sertoli cells in culture. In addition to transferrin, antiserum to rat serum proteins will immunoprecipitate one other polypeptide from preparations of Sertoli cell-secreted proteins.

• Publication year

  1980

• Venue

  Journal of Biological Chemistry

• Publication date

  1980-10-25

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/s0021-9258(18)43419-9PMID 6776100
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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