This study was conducted to underscore the spatial distribution of some biologically active proteins within the epididymal duct in the dromedary camel. Paraffin-embedded sections from different regions of epididymis were stained by conventional histological techniques and by immunohistochemistry. A battery of primary antibodies against six proteins (S100, alpha smooth muscle actin [alpha-SMA], connexin-43 [Cx43], galactosyltransferase [GalTase], angiotensin converting enzyme [ACE], and vascular endothelial growth factor [VEGF]) were used. The epididymal epithelium consisted of five cell populations: principal, basal, apical, dark, and halo cells. The histochemical findings indicated the absence of binding sites for VEGF and Cx43. The principal cells (PCs) showed variable immunoreactivity (IR) for ACE, S100, and GalTase throughout the whole length of the duct. The apical surfaces of most PCs (at the caput) and some PCs (at the corpus) exhibited intense ACE-IR, whereas those at the cauda displayed alternating negative and strong immunostaining. Similarly, moderate S100-IR was found in cytoplasm and nuclei of all PCs at the caput, few PCs at the corpus, and several PCs alternating with negative PCs at the cauda. In contrast, only some PCs showed weak to strong GalTase-IR in different regions. Apart from negative to weak positive S100-IR, basal cells failed to show IR for all other proteins. Apical cells displayed strong IR for ACE, S100, and GalTase with some regional differences. The peritubular and vascular smooth muscle cells revealed strong alpha-SMA-IR in all regions. In conclusion, the spatial distribution of different proteins in camel epididymis showed similarities and differences to other mammalian species. The region-specific topographic distribution of different proteins and cell types might indicate that the caput and cauda are metabolically more active than that of the corpus.
Actins ; Antibodies ; Binding Sites ; Camels ; Connexin 43 ; Cytoplasm ; Epididymis ; Epithelium ; Histological Techniques ; Immunohistochemistry ; Male ; Muscle, Smooth ; Muscle, Smooth, Vascular ; Peptidyl-Dipeptidase A ; Proteins ; Vascular Endothelial Growth Factor A