Crystalloids of actin-like filaments in the Sertoli cell of the swine testis.
Normal swine testes, congenital cryptorchid swine testes, and normal human tests were exposed to HMM (heavy meromyosin) after either glycerination or saponin treatment in order to determine whether the fine filaments composing the crystalloids in the Sertoli cells of the cryptorchid swine testes bind HMM to form arrowhead complexes. Short bundles of microfilaments observed in the basal part of the Sertoli cells in both normal and cryptorchid testes also bind HMM. Similar bundles of HMM-bound filaments are observed in the vicinity of spermatocytes. The periodicity of the arrowhead complexes is about 35 nm, and all arrowheads on a given filament point in the same direction. In addition, the polarity of the HMM-bound filaments in a given crystalloid or bundle is uni-directional. A mechanism for the formation of the swine crystalloids has been strongly support this hypothesis. Fine filaments of Charcot-Boettcher's crystalloid in human Sertoli cells did not bind HMM. Therefore the fine filaments of the human crystalloid are not actin-like in nature.
D000199:Actins; D000368:Aged; D000818:Animals; D003456:Cryptorchidism / Q000473:pathology; D003461:Crystallography; D003599:Cytoskeleton / Q000648:ultrastructure*; D006801:Humans; D002479:Inclusion Bodies / Q000648:ultrastructure; D008297:Male; D015879:Myosin Subfragments; D012708:Sertoli Cells / Q000648:ultrastructure*; D013552:Swine; D013737:Testis / Q000648:ultrastructure*
D000199:Actins; D015879:Myosin Subfragments