Site of Actin Fiber Depolymerization within Rat Sertori Cells as Detected by Localization of .BETA.-thymosin.

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The localization of actin sequestering peptide thymosin β10 in rat testis was analyzed by light and electron microscopic immunohistochemistry using the anti-thymosin β10 antibody. A positive reaction of thymosin β10 was detected in a closely associated portion within the developing spermatid head. In step 15 spermatids, localized deep in the seminiferous epithelium, a prominent positive reaction was detected in the Sertoli cell cytoplasm adjacent to the spermatids. In step 19 spermatids, just before spermiation, thymosin β10 was highly concentrated in the Sertoli cell cytoplasm situated at the concave side of the sickle shaped spermatid head, where the tubulobulbar complex is formed. According to previous ultrastructural observations, actin bundles of ectoplasmic specialization change to electron dense material just prior to spermiation. The localization of thymosin β10 suggests that large amounts of actin monomers accumulate in the region of the tubulobulbar complex just prior to spermiation. These findings suggest that thymosin β10 accumulation is correlated with fragmentation of the ectoplasmic specialization, and strongly support the hypothesis that the tubulobulbar complex is an actin-disorganizing organelle of the Sertoli cell.

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