The epididymis of the male reproductive system is known to be involved in sperm maturation via the production of polypeptides, glycoproteins, surface proteins, enzymes and other factors. During the annual reproductive cycle, the epididymis of the lizard Eutropis carinata undergoes dramatic changes, both morphologically and biochemically, that occur in a well-organized sequence. The present study reveals the sequential changes that occur in the production and concentration of proteins in the epididymal luminal fluid throughout the annual reproductive cycle. A one-dimensional electrophoretic profile of the epididymal luminal proteins revealed a total of 18 bands in the regenerative phase, 22 bands during breeding and 17 bands in the post-breeding as well as regressed phases of the reproductive cycle. By two-dimensional electrophoresis, the protein complexes that are unique to the breeding phase were further resolved based on their pI and the molecular weight of each protein of the protein complex was determined. This is the first study to observe that proteins that are present during the reproductively inactive phase disappear during the reproductively active phase. The Periodic Acid Schiff (PAS) test for protein profiles revealed the presence of proteins with a carbohydrate moiety. Certain enzymes, such as acid phosphatase, alkaline phosphatase, and α-glucosidase, are highly sensitive to seasonal changes and their activity parallels the production of the epididymal proteins. This study provides evidence for androgen-dependent cyclical changes in the pattern of protein profiles and enzyme activity of the epididymal lumen in the lizard E. carinata.
Beta-hexosaminidase (Hex) is the major lysosomal enzyme associated with the event of fertilization. In this study, we have analyzed the distribution of Hex in the testis and the epididymis of the lizard, Eutropis carinata by a polyclonal antibody of β-hexosaminidase isoform (Hex A). Presence of Hex in the epididymis was performed by Western blotting. The result reveals that Hex A is present in the epididymal epithelium, lumen as well as spermatozoa. The anatomical distribution of Hex was studied by immunohistochemical localization. The study reveals that Hex is intensely stained in the epithelium of anterior and middle regions of the epididymis, whereas, posterior epididymal epithelium shows moderate staining. In addition, seminiferous epithelium of the testis shows staining for Hex. But lumen of the testis did not show any reaction for Hex. Further, immunohistochemical localization of Hex on the spermatozoa from the testis and different regions of the epididymis revealed that the Hex from the testis did not show any staining; the epididymal epithelium is moderately localized in the spermatozoa of the anterior region and gradually increases in the intensity in the spermatozoa of the posterior region of the epididymis. This indicates that the Hex is released from the epididymal epithelium and binds to the spermatozoa, and in the lumen, it gradually increases from anterior to the posterior region of the epididymis. The result also suggests that Hex A bound to the epididymal spermatozoa originates from the epididymis and not from the testis. The regional difference in the expression of Hex in the epididymis of the lizard, E. carinata, indicates the possible site of secretion of this enzyme.
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