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J. Biol. Chem., Vol. 255, Issue 20, 9523-9525, 10, 1980
MK Skinner and MD Griswold
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.
Sertoli cells synthesize and secrete transferrin-like protein
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