Cyclic and Postnatal Developmental Changes of Testin in the Rat Seminiferous Epithelium—An Immunohistochemical Study1

Autor: J Grima, C W Bardin, L J Zhu, S D Zong, G R Aravindan, Cheng Cy
Rok vydání: 1994
Předmět:
Zdroj: Biology of Reproduction. 51:843-851
ISSN: 1529-7268
0006-3363
Popis: Testin is an authentic Sertoli cell secretory protein consisting of two molecular variants designated testin I (M(r) 35 000) and testin II (M(r) 37 000). N-Terminal amino acid sequence analysis revealed that testin I is identical to testin II except that testin II has three extra N-terminal amino acids of threonine-alanine-proline (TAP). Earlier studies by immunoflorescence microscopy have shown that testin is detected in the seminiferous epithelium consistent with localization in the junctions between Sertoli cells as well as Sertoli-germ cells, and that it appears to be a component of junctional complexes in the testis. In the present study, we have examined the localization of testin in different stages of the spermatogenic cycle of the adult rat testis when germ cells migrate from the basal portion of the seminiferous epithelium to the tubular lumen. In stages I-IV, testin was localized mainly in the basement laminae in the junctional complexes between adjacent Sertoli cells as well as between Sertoli cells, spermatogonia, and pachytene spermatocytes. When elongated spermatids were embedded into the seminiferous epithelium in stage VII of the cycle, testin was detected predominantly on the concave side of the elongated spermatids, but relatively few testin reaction products were seen in the round spermatids. In the beginning of stage VIII of the spermatogenic cycle, intense testin immunoreactive substances were detected around the heads of the elongated spermatids; these substances were virtually undetectable in late stage VIII after the release of the mature sperm into the tubular lumen, suggesting that testin may be a novel marker to divide stage VIII into stages VIIIa and VIIIb.(ABSTRACT TRUNCATED AT 250 WORDS)
Databáze: OpenAIRE