Testins Are Structurally Related Sertoli Cell Proteins Whose Secretion Is Tightly Coupled to the Presence of Germ Cells

Previous studies from this laboratory have shown that Sertoli cell-enriched culture medium contained two immunologically and structurally related proteins designated CMB-22 and CMB-23 with Mr of 37,000 and 40,000, respectively. We have now demonstrated that both CMB-22 and CMB-23 are monomeric prote...

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Published in:The Journal of biological chemistry 1989-12, Vol.264 (35), p.21386-21393
Main Authors: Cheng, C Y, Grima, J, Stahler, M S, Lockshin, R A, Bardin, C W
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cells, Cultured
Fundamental and applied biological sciences. Psychology
Glycoproteins - analysis
Glycoproteins - blood
Glycoproteins - isolation & purification
Immune Sera
Male
Miscellaneous
Molecular Sequence Data
Molecular Weight
Orchiectomy
Organ Specificity
Proteins
Radioimmunoassay
Rats
Rats, Inbred Strains
Sertoli Cells - physiology
testin
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Summary:Previous studies from this laboratory have shown that Sertoli cell-enriched culture medium contained two immunologically and structurally related proteins designated CMB-22 and CMB-23 with Mr of 37,000 and 40,000, respectively. We have now demonstrated that both CMB-22 and CMB-23 are monomeric proteins with the following NH2-terminal amino acid sequences: CMB-22, NH2-TPDPSLDVEWNEWRTKHGKTYNMNEERLKR; CMB-23, NH2-XAPXPDPSLDVEXNEXRTK. These sequences are virtually identical except that CMB-23 has three extra NH2 terminus amino acids of X-A-P. Comparison of these sequences with those in the Protein Identification Resource revealed that they are unique proteins. CMB-22 and CMB-23 are highly concentrated in testes and their levels in this tissue increase with age. Studies using [35S]methionine incorporation and immunoprecipitation demonstrated that Sertoli cells synthesize and secrete these proteins in vitro. Because they seem not to have been isolated previously, are concentrated in and synthesized by the testes, and are structurally related, we propose that CMB-22 and CMB-23 be designated testin I and testin II, respectively. The distribution of these proteins in biological fluids were compared with those of testibumin and rat androgen binding protein (rABP), two other Sertoli cell proteins. The results suggest that testins, unlike testibumin and rABP, are not transported to the epididymis. Although the amount of testins secreted by Sertoli cells in vitro is similar to that of testibumin and rABP, the concentrations in testis and rete testis fluid are several orders of magnitude less than that of testibumin and rABP. These observations suggest that the secretion of these proteins in vivo might be suppressed by germ cells. The fact that 10 times more testins are secreted by tubules from immature rats than by those from adult rats and that there is an increase in the testicular content of testins following a single dose of busulfan, which depleted the germ cells from the seminiferous epithelium, supports this hypothesis. Thus, the secretion of testins by Sertoli cells appears to be tightly coupled to the presence of germ cells; there is an inverse relationship between the amount of testins in the testis and the number of germ cells. These results suggest that testins are unique testicular proteins that can be used to study Sertoli cell-germ cell interactions in the seminiferous epithelium.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)30092-4