Degradation of angiotensin I to [des-Asp1]angiotensin I by a novel aminopeptidase in the rat hypothalamus

Sim, Melvyn; Choo, Maurice H.; Qiu, Xi-Min

doi:10.1016/0006-2952(94)90376-x

Cited by 33 publications

(8 citation statements)

References 13 publications

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“…Thus sequential removal of single amino acid residues from the NH 2 -terminal of ANG I and ANG II, which takes place through aminopeptidases, results in modified active peptides ANG III and ANG IV, respectively (7). Asp-AP and APA can delete Asp 1 -Arg 2 residue from both ANG I and ANG II (1,24,39); PSA and APN can also remove this residue from ANG I and furthermore Arg 2 -Val 3 from ANG III (24), and it has recently been reported that APB processes ANG peptides in peripheral organs (30). Therefore, all the peptidase activities we have described as significantly modified in CCRCC samples compared with adjacent unaffected tissue (Asp-AP, APB, PSA, and APN) would appear to participate in the ANG metabolism at different levels of the pathway.…”

Section: Discussionmentioning

confidence: 99%

Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma

Varona¹,

Blanco²,

López³

et al. 2007

American Journal of Physiology-Renal Physiology

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Peptides play important roles in cell regulation and signaling in many tissues and are regulated by peptidases, most of which are highly expressed in the kidney. Several peptide convertases have a function in different tumor stages, and some have been clearly characterized as diagnostic and prognostic markers for solid tumors, including renal cancer; however, little is known about their in vivo role in kidney tumors. The present study compares the activity of a range of peptidases in human tumor samples and nontumor tissue obtained from clear cell renal cell carcinoma (CCRCC) patients. To cover the complete spectrum and subcellular distribution of peptide-converting activity, acid, neutral, basic, and omega activities were selected. CCRCC displays a selective and restricted pattern of peptidase activities. Puromycin-sensitive aminopeptidase activity in the tumor increases [tumor (t) = 10,775 vs. nontumor (n) = 7,635 units of peptidase (UP)/mg protein; P < 0.05], whereas aminopeptidase N decreases (t = 6,664 vs. n = 33,381 UP/mg protein; P < 0.001). Aminopeptidase B activity of the particulate fraction in tumors decreases (t = 2,399 vs. n = 13,536 UP/mg protein; P < 0.001) compared with nontumor tissues, and aspartyl-aminopeptidase activity decreases significantly in CCRCC (t = 137 vs. n = 223 UP/mg protein; P < 0.05). Soluble and particulate pyroglutamyl peptidase I activities, aminopeptidase A activity, and soluble aminopeptidase B activity do not vary in renal cancer. The relative expression for the aforementioned peptidases, assayed using quantitative RT-PCR, increases in CCRCC for aminopeptidases B (1.5-fold) and A (19-fold), aspartyl-aminopeptidase (3.9-fold), puromycin-sensitive aminopeptidase (2.5-fold), and pyroglutamyl peptidase I (7.6-fold). Only aminopeptidase N expression decreases in tumors (1.3-fold). This peptidase activity profile in the neoplastic kidney suggests a specific role for the studied convertases and the possible involvement of an intracrine renin-angiotensin system in the pathogenesis of CCRCC.

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Section: Discussionmentioning

confidence: 99%

Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma

Varona¹,

Blanco²,

López³

et al. 2007

American Journal of Physiology-Renal Physiology

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“…We found that, in the atrium, AspAP activity increased more than two-fold after high oleic intake. There is evidence that the enzyme responsible for the metabolism of Ang I to des-Asp 1 -Ang I is AspAP (Sim et al, 1994). The nonapeptide des-Asp 1 -Ang I has been proposed as a modulator of the contractile actions of Ang II and Ang III in the rabbit aortic ring, where it potentiates the former and attenuates the latter (Sim and Yuan, 1995).…”

Section: Tissue Rasmentioning

confidence: 99%

Angiotensinase Activity and Olive Oil Supplementation

Ramírez-Expósito

Carrera

Martínez-Martos

2010

Olives and Olive Oil in Health and Disease Prevention

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“…1B). At least in the rat hypothalamus, angiotensin I is mainly degraded to [des-Asp1]-angiotensin I instead of angiotensin II [54,55]. At least in the rat hypothalamus, angiotensin I is mainly degraded to [des-Asp1]-angiotensin I instead of angiotensin II [54,55].…”

Section: Biosynthesis and Degradation Of Angio-tensinsmentioning

confidence: 99%

The Renin-Angiotensin System in the Mammalian Central Nervous System

Halbach

2005

CPPS

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The brain renin-angiotensin system enables the formation of different biological active forms of angiotensins within the brain. All enzymes and peptides necessary for the biosynthesis of these angiotensins have been recognized within the central nervous system. Since there are considerable mismatches concerning the localization of the different enzymes, this system is not fully understood. Moreover, since alternative pathways of the angiotensin biosynthesis exists, localization and generation, especially of the short forms of biologically active angiotensins, are largely enigmatic. The brain renin-angiotensin system mediates several classic physiological effects including body water balance, maintenance of blood pressure, sexual behaviors, and regulation of pituitary gland hormones. Beside these classic functions, the brain renin-angiotensin system has more subtle functions involving complex mechanisms such as learning and memory. The mechanisms of action seem to differ depending on the utilized different bioactive angiotensin fragments, which are formed by the action of a variety of enzymes. This phenomenon appears to represent an important mechanism for neuromodulation. Moreover, there is evidence to suggest that the renin-angiotensin system is involved in neurological disorders, as e.g. Alzheimer's or Parkinson's disease.

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Degradation of angiotensin I to [des-Asp1]angiotensin I by a novel aminopeptidase in the rat hypothalamus

Cited by 33 publications

References 13 publications

Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma

Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma

Angiotensinase Activity and Olive Oil Supplementation

The Renin-Angiotensin System in the Mammalian Central Nervous System

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