Angiotensinogen, prorenin, and renin are Co-localized in the secretory granules of all glandular cells of the rat anterior pituitary: an immunoultrastructural study.
نویسندگان
چکیده
In addition to the circulating renin-angiotensin system (RAS), a local system has been postulated in the anterior pituitary because immunodetection of its components in various mammalian species. However, different cell types appear to be involved in different species, and there is no general consensus on the subcellular localization of prorenin, renin and angiotensinogen. In this ultrastructural study, we investigated and quantified the presence of these components using double or triple immunogold labeling methods, in all the immunologically identified glandular cell types of the rat anterior pituitary. In contrast to previous reports, all these components were identified not only in lactotropes and gonadotropes but also in somatotropes, corticotropes, and thyrotropes. The highest levels were detected in lactotropes and gonadotropes, and renin gave the greatest signal. Angiotensinogen, prorenin, and renin were co-localized in the secretory granules of all rat pituitary glandular cell types. The simultaneous detection of the substrate (angiotensinogen) and both its specific cleavage enzyme and its proenzyme within the same granule suggests intragranular processing of this component. Moreover, the localization of these three constituents in the secretory granules also suggests that, in the rat anterior pituitary, they follow the regulated secretory pathway.
منابع مشابه
Rat angiotensinogen is secreted only constitutively when transfected into AtT-20 cells.
To test whether angiotensinogen might be targeted to dense core secretory granules in cells containing a regulated secretory pathway, we expressed rat angiotensinogen in AtT-20 cells, a mouse pituitary cell line that has the demonstrated ability to correctly sort proteins to the constitutive or regulated pathway. We compared the pattern of secretion of angiotensinogen with that of endogenous ad...
متن کاملIn vivo enzymatic assay reveals catalytic activity of the human renin precursor in tissues.
The aspartyl protease renin is secreted into the circulation of mammals in 2 forms: the proteolytically processed active form of the enzyme and the precursor form, prorenin. Prorenin has no detectable enzymatic activity in the circulation, but it is the exclusive form of the enzyme produced by several tissues that also produce the other components of the renin enzymatic cascade (renin-angiotens...
متن کاملProrenin processing by cathepsin B in vitro and in transfected cells.
Renin, which catalyzes the initial proteolytic cleavage reaction in the production of angiotensins, is first synthesized as a zymogen, prorenin, and requires the proteolytic removal of an amino-terminal prosegment for activation in vivo. The lysosomal hydrolase cathepsin B has been proposed as a prorenin processing enzyme based on reports of its co-localization with renin in the secretory granu...
متن کاملHuman prorenin.
Human prorenin is the enzymatically inactive biosynthetic precursor of renin. Recent interest has focused on the posttranslational sorting and processing of prorenin to renin since markedly increased levels of circulating prorenin have been associated with both physiological and pathological changes. These observations raise the question of whether prorenin processing may be a regulatory event ...
متن کاملHigh glucose concentration stimulates intracellular renin activity and angiotensin II generation in rat mesangial cells.
Increased intrarenal renin-angiotensin system activity contributes to diabetic nephropathy. ANG II generation in mesangial cells (MC) is increased by high-glucose (HG) exposure. This study assessed the mechanisms involved in the glucose-induced ANG II generation in rat MC. Under basal conditions, MC mainly secreted prorenin. HG decreased prorenin secretion and induced a striking 30-fold increas...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
دوره 46 3 شماره
صفحات -
تاریخ انتشار 1998