Angiotensin I (human, mouse, rat)

Angiotensin I (Ang I) (C62H89N17O14), with the sequence H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-OH, is formed by the action of renin on angiotensinogen. Renin is produced in the kidneys in response to renal sympathetic activity, decreased intrarenal blood pressure (<90mmHg systolic blood pressure) at the juxtaglomerular cells. Ang I appears to have no biological activity and exists solely as a precursor to angiotensin II (A II). Ang I is cleaved to Ang II by the angiotensin-converting enzyme (ACE). Ang II increases blood pressure by stimulating the Gq protein in vascular smooth muscle cells (which in turn activates contraction by an IP3-dependent mechanism).

 

 

 

Ref:

1. Lundequist, A. et al. J. Biol. Chem. 279, 32339 (2004); Olson, S. et al. Am. J. Physiol. Lung. Cell Mol. Physiol. 287, L559 (2004); Sanker, S. et al. J. Biol. Chem. 272, 2963 (1997).

2. Preston RA, Materson BJ, Reda DJ, et al. Age-Race Subgroup Compared With Renin Profile as Predictors of Blood Pressure Response to Antihypertensive Therapy. JAMA. 1998;280(13):1168-1172. doi:10.1001/jama.280.13.1168.

Potency and selectivity of RXP407 on human, rat, and mouse angiotensin-converting enzyme.[Pubmed:11274969]

Biochem Pharmacol. 2001 Apr 1;61(7):835-41.

By screening phosphinic peptide libraries, we recently reported the discovery of RXP407 (Ac-Asp-PheY(PO2-CH2)LAla-Ala-NH2), a potent N-domain-selective inhibitor of recombinant human angiotensin-converting enzyme (ACE). Preliminary studies to evaluate the in vivo activity of RXP407 in rat led us to suspect possible differences in the binding property of RXP407 between human and rat ACE. The aim of the present study was thus to determine the potency of RXP407 toward rat and mouse ACEs, as compared to non-recombinant human ACE, and to assess the efficacy of this inhibitor in discriminating between the N- and C-domains of these ACE enzymes. By comparing the ability of RXP407 to block purified somatic and germinal ACE from mice, RXP407 was shown to be a potent N-domain-selective inhibitor of mouse somatic ACE, a behavior similar to that observed with human somatic ACE. In contrast, RXP407 appeared less potent toward purified ACE from rat and furthermore was unable to block ACE activity present in crude rat plasma. This study demonstrated that for further evaluation of the in vivo efficacy of RXP407, mice rather than rats should be used as the animal model. Thus, following the change in the Ac-S-D-K-P plasmatic levels, after i.v. injection of RXP407 to mice, will permit the potency and selectivity of this novel ACE inhibitor to be assessed.

Analysis of the evolution of angiotensin II type 1 receptor gene in mammals (mouse, rat, bovine and human).[Pubmed:1497638]

Biochem Biophys Res Commun. 1992 Jul 31;186(2):1042-9.

The nucleotide and amino acid sequences for mouse angiotensin II (AII) type 1A and 1B receptors were deduced from their complementary and genomic DNAs. Evolutionary analyses based on the nucleotide sequences of the coding region of AII type 1 receptor genes indicated that the duplication event of the type 1 gene occurred 24 +/- 2 million years ago before the divergence between the rat and mouse but after the divergence between rodents and the human/artiodactyls couple. This conclusion was consistent with the results of genomic Southern blot analyses, which revealed that the mouse and rat possess 2 similar but separate genes, whereas the bovine and human have only a single class gene.

Renal metabolism of angiotensin I and II.[Pubmed:2175370]

Kidney Int Suppl. 1990 Nov;30:S24-7.

The enzymatic hydrolysis of angiotensin I and II is reviewed briefly with emphasis on two enzymes, the angiotensin I converting enzyme and neutral endopeptidase 24.11. Angiotensin I is converted to angiotensin II by converting enzyme present in many tissues and highly concentrated in the human kidney and in kidney of some laboratory animals. In addition, there is mounting evidence, collected mostly in experiments in vitro, that other enzymes may be able to activate angiotensin I, for example by the stepwise release of the C-terminal His and Leu residues. Angiotensin I, instead of being activated, could be inactivated by the cleavage of its C-terminal tripeptide either by neutral endopeptidase 24.11 or by prolyl endopeptidase. Angiotensin II is cleaved by several peptidases widely distributed in the kidney. One of the products, des-Phe8-angiotensin II, is not entirely inactive as it has an effect in the CNS.

Endothelium-dependent contractions induced by angiotensin I and angiotensin II in canine cerebral artery.[Pubmed:2795464]

J Pharmacol Exp Ther. 1989 Oct;251(1):317-20.

Whether angiotensin I and angiotensin II caused endothelium-dependent contraction was examined in canine cerebral arteries. In endothelium-intact preparations, angiotensin I and angiotensin II at 10(-8) to 10(-6) M caused dose-dependent contractions, whereas both angiotensins caused much less contractions in endothelium-removed preparations. The contractions induced by angiotensin I and angiotensin II were strongly attenuated by aspirin (cyclooxygenase inhibitor) (5 x 10(-5) M), OKY-046 [thromboxane (TX) A2 synthetase inhibitor] (10(-5) M) and ONO-3708 (TX)A2 antagonist) (5 X 10(-9) M). Captopril (10(-6) M) significantly attenuated the contractions induced by angiotensin I but not those induced by angiotensin II. Angiotensin I- and angiotensin II- induced contractions were inhibited markedly by Sar1, Ala8-angiotensin II (10(-9) and 10(-8) M). The present experiments demonstrate that angiotensin I and angiotensin II produce endothelium-dependent contraction in canine cerebral artery via a factor which appears to be TXA2. Angiotensin I may be converted by endothelial cells to angiotensin II, which may activate the cells to produce TXA2 in canine cerebral artery.

Conversion of angiotensin I to angiotensin II.[Pubmed:190881]

Am J Med. 1976 May 31;60(6):749-59.

The angiotensin I converting enzyme has two important functions: it inactivates bradykinin and converts angiotensin I to angiotensin II. Inhibition of the enzyme blocks the renin-angiotensin system and decreases systemic blood pressure if the pressure is maintained or increased by renin. The enzyme occurs in a variety of tissues and cell forms. The vascular endothelial cells of the lung and of peripheral blood vessels, and the epithelial cells of the kidney tubules are major sources of the enzyme. In addition to inactivating hypotensive peptides and activating a hypertensive one in the systemic circulation, the enzyme may affect organ functions by hydrolyzing peptides that are formed and released locally.

Angiotensin 1 (Human) is the precursor to the vasoconstrictor peptide angiotensin II, cleaved by the angiotensin-converting enzyme (ACE).

Angiotensin I (human, mouse, rat),484-42-4,Natural Products, buy Angiotensin I (human, mouse, rat) , Angiotensin I (human, mouse, rat) supplier , purchase Angiotensin I (human, mouse, rat) , Angiotensin I (human, mouse, rat) cost , Angiotensin I (human, mouse, rat) manufacturer , order Angiotensin I (human, mouse, rat) , high purity Angiotensin I (human, mouse, rat)