The Distribution of Rat Testibumin in the Male Reproductive Tract1
- 1 November 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Biology of Reproduction
- Vol. 37 (4) , 875-885
- https://doi.org/10.1095/biolreprod37.4.875
Abstract
A glycoprotein, designated CMB-1, has been identified in media from Sertoli cell-enriched cultures that increases in concentration in response to follicle-stimulating hormone (FSH) and testosterone. Subsequent studies indicated that CMB-1 is immunologically related to albumin and .alpha.-fetoprotein and is concentrated in the luminal compartment of the testis in adult rats. Thus, CMB-1 was termed testibumin. The goal of the present study was to determine the concentrations of this protein in testes, epididymides, and serum of normal rats between 10 and 180 days of age and to compare them to rat androgen-binding protein (rABP). Testibumin concentration in rat testes increased with age and peaked at Day 60; thereafter, unlike rABP, its concentration declined, reaching a plateau by 150 days of age. Testibumin concentration in the epididymal compartment also increased with age and peaked at Day 90; thereafter, its concentrations remained relatively unchanged. Unlike rABP, which accumulates in the caput epididymis, testibumin did not accumulate preferentially in any particular region of the epididymis. In spite of the marked changes of testibumin concentration in the male reproductive tract, the levels in blood remained relatively constant between 10 and 180 days of age. In adult male and female rats, the serum concentrations of testibumin were similar. Following orchiectomy, serum testibumin concentration decreased by 50% with an apparent t1/2 of .apprx. 8 h. The presence of immunoreactive macromolecules in other species that share epitopes with rat testibumin was also investigated. Material in human sera and extracts of human and monkey testes cross-reacts with rat testibumin. After [35S] methionine was added to the primary Sertoli cell-enriched cultures, anti-testibumin antiserum selectively immunoprecipitated a radiolabeled protein with the same electrophoretic mobility as purified testibumin on sodium dodecyl sulfate (SDS) polyacrylamide gels. We conclude that 1) rat testibumin is synthesized and secreted by Sertoli cell-enriched cultures; 2) the relative concentrations and distribution of testibumin in testis, epididymis, and serum of the rat as a function of age are strikingly different from those of rABP; 3) rat testibumin shares epitopes with proteins in human serum and testicular extracts of monkey and man.This publication has 26 references indexed in Scilit:
- Transferrin and gonadal dysfunction in manFertility and Sterility, 1982
- Hormonal regulation of protein synthesis, secretion, and phosphorylation in cultured rat Sertoli cells.Proceedings of the National Academy of Sciences, 1982
- Analysis of Sertoli Cell-Secreted Proteins by Two-Dimensional Gel ElectrophoresisBiology of Reproduction, 1982
- An improvement of the Coomassie Blue dye binding method allowing an equal sensitivity to various proteins: application to cerebrospinal fluidClinica Chimica Acta; International Journal of Clinical Chemistry, 1982
- Sertoli cells secrete both testis-specific and serum proteins.Proceedings of the National Academy of Sciences, 1981
- Silver staining of proteins in polyacrylamide gelsAnalytical Biochemistry, 1981
- Sertoli cells synthesize and secrete transferrin-like protein.Journal of Biological Chemistry, 1980
- Immunoassay of Androgen Binding Protein in Blood: A New Approach for Study of the Seminiferous TubuleScience, 1978
- Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycolurilBiochemical and Biophysical Research Communications, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976