Ce. Coronel et al., ELECTRON-MICROSCOPIC IMMUNOLOCALIZATION OF CALTRIN PROTEINS IN GUINEA-PIG SEMINAL-VESICLES, Archives of andrology, 35(3), 1995, pp. 233-246
Caltrins, the small, basic proteins of the seminal vesicle secretion t
hat inhibit calcium transport into epididymal spermatozoa, and consequ
ently the onset of the acrosome reaction and the hyperactivated motili
ty, were localized in the epithelial cells and the lumen of the semina
l vesicles of the guinea pig by an immunocytochemical procedure and el
ectron microscopy. Rabbit antisera against each protein (caltrin I or
II), and goat anti-rabbit IgG antiserum labeled with colloidal gold we
re used to detect the caltrin immunoreaction. The subcellular distribu
tion of the gold labeling was occasionally localized in the rough endo
plasmic reticulum but mainly within big secretory vacuoles containing
low electron-dense material, which are components of the Golgi complex
known as condensing vacuoles. These are involved in the intracellular
transport, storage, and discharge of secretory proteins. Gold-labeled
material released to the lumen was also detected. There was no clear
evidence that the discharge was mediated by an exocytotic process. Imm
unoreaction was observed neither in the electron-dense core nor in the
electron-lucent halo of the typical secretory granules of the epithel
ial cells of the seminal vesicles. Using light microscope immunocytoch
emistry, intense positive immunoreactivity was detected in the materia
l secreted to the lumen but not on the epithelial cell laser. Only tho
se cells undergoing a degenerative process and showing a picnotic nucl
eus and condensed cytoplasmic matrix exhibited detectable immunoreacti
on when gold label and silver intensification were applied. The same d
istribution of the immunoprobes was obtained by electron or light micr
oscopy when antiserum to either I or II was used. It would appear that
the two caltrin proteins of the guinea pig are synthesized in the rou
gh endoplasmic reticulum of the epithelial cells and transported quick
ly to the Golgi complex where the secretory vacuoles (condensing vacuo
les) are formed. The proteins are transported by the secretory vacuole
s to the apical ends of the cells to be discharged into the lumen.