Localization of transferrin and transferrin receptors in rat testes

• Published in: Biology of reproduction Vol. 31; no. 1; pp. 195 - 203
• Main Authors: Sylvester, S R, Griswold, M D
• Format: Journal Article
• Language: English
• Published: United States Society for the Study of Reproduction 01.08.1984
• Subjects: Animals; electron microscopy; Fluorescent Antibody Technique; Histocytochemistry; immunofluorescence; Male; Rats; Rats, Inbred Strains; Receptors, Cell Surface - analysis; Receptors, Transferrin; Sertoli cells; Spermatozoa - analysis; Testis - analysis; transferrin; Transferrin - analysis
• ISSN: 0006-3363; 1529-7268
• DOI: 10.1095/biolreprod31.1.195

One of the major proteins secreted by rat Sertoli cells in culture is a transferrin-like protein (Skinner and Griswold, 1980). The purpose of this study was to quantitate the amount of testicular transferrin in fluids isolated from the testis by the use of a radioimmunoassay and to determine the location of transferrin and transferrin receptors in the testis by indirect immunofluorescence. Seminiferous tubule fluid, rete testis fluid, and testicular lymph were collected from rat testes and were found to contain 141 micrograms, 47 micrograms and 3.7 mg transferrin per ml of fluid, respectively. Serum was found to contain 3.7 mg/ml transferrin. Paraffin sections of rat testis were incubated with rabbit anti-rat transferrin, biotinylated goat anti-rabbit and fluorescein-conjugated avidin. Immunoreactive transferrin was thus localized on the proacrosome and nuclear cap of developing spermatids. Late spermatids showed transferrin over the entire region of the head but mature testicular spermatozoa exhibited little fluorescence. The interstitial tissue between seminiferous tubules fluoresced brightly, indicating a large amount of transferrin in this area. By pretreating sections with rat transferrin, the receptor for the protein was localized on and in spermatocytes and early round spermatids. Dividing germ cells were brightly fluorescent.