Presence of renin within intramitochondrial dense bodies of the rat adrenal cortex

Abstract

It has been suggested that tissue-specific expression of the genes of the renin-angiotensin system (RAS) leads to local generation of angiotensin (ANG) II with specific physiological implications. We demonstrate here that an intracellular RAS exists in adrenal glomerulosa cells; 60 h after bilateral nephrectomy and hemodialysis, renin and prorenin were eliminated from the circulation, whereas intra-adrenal renin content increased (control rats: 2 +/- 0.5 ng ANG I.mg-1.h-1; anephric rats: 25 +/- 2). Thus renin is produced locally within adrenal cells. We obtained immunocytochemical and biochemical evidence for the presence of renin within intramitochondrial dense bodies of the zona glomerulosa. After nephrectomy, dense bodies increased in number, size, and renin content (control rats: 2.5 +/- 0.7 ngANGI.mg-1.h-1; anephric rats: 43 +/- 7). Angiotensin-converting enzyme (ACE) was also present within mitochondria and their dense bodies. In addition, in adrenal cortex of anephric rats, giant dense bodies were observed, which contain renin and strongly react with an anti-angiotensinogen antibody. The localization of renin, ACE, and angiotensinogen at these sites provides new evidence for the existence of an intracellular adrenal RAS.

Angiotensin II in Septic Shock

“…Evidence has indicated a direct interaction between angiotensin II and mitochondrial components [42][43][44][45]. In a study using 125 I-labeled angiotensin II in rats, angiotensin II was detected in the mitochondria and nuclei of the heart, brain and smooth muscle cells [42,43].…”

Lectin chromatography of extrarenal renin protein in human plasma and tissues: Potential endocrine function via the renin receptor

“…However, our purpose was not to pursue these differences, but to identify a tissue storing only Con A non-binding renin, as this could indicate cells lacking a specific glycosyl transferase for mannose, or possibly possessing a mannose removing glycosidase. 5 While this study has not identified a tissue 25 and is presumably not glycosylated, because, although coded by nuclear DNA, it lacks a signal for entry into the endoplasmic reticulum. 26 This form of tissue renin may be a truncated amannosylated prorenin, 26 but would not be expected to be secreted into plasma at consistent levels, either before or after incorporation into mitochondria.…”

Involvement of the Renin‐Angiotensin System in Atherosclerosis

“…This way Ang II may stimulate an increase in mitochondrial oxidative stress, thus leads to VCMC senescence. Also, mitochondria may endogenously produce Ang II [36][37][38]. Several animal studies show that Ang II causes and contributes to aortic endothelial dysfunction [39][40][41].…”