Hydrolysis of Biological Peptides by Human Angiotensin-converting Enzyme-related Carboxypeptidase

Vickers, Chad; Hales, Paul; Kaushik, Virendar K.; Dick, Lawrence R.; Gavin, James M.; Jin, Tao; Godbout, Kevin; Parsons, Thomas F.; Baronas, Elizabeth; Hsieh, F.; Acton, Susan; Patane, Michael A.; Nichols, Andrew J.; Tummino, Peter J.

doi:10.1074/jbc.m200581200

Cited by 1,302 publications

(1,488 citation statements)

References 26 publications

Supporting

Mentioning

1,427

Contrasting

Unclassified

Order By: Relevance

“…Blood vessels are an important target for the actions of Ang peptides. Ang II is converted to Ang 1-7 by angiotensin converting enzyme-2 in the endothelial cells [21,22]. The vascular action of Ang 1-7 is vasodilation; therefore the opposite to Ang II induce vasoconsriction.…”

Section: Applications Of the Lc-ms And Lc-ms/ms Methodsmentioning

confidence: 99%

Simultaneous analysis of angiotensin peptides by LC–MS and LC–MS/MS: Metabolism by bovine adrenal endothelial cells

Cui

Nithipatikom

Campbell

2007

Analytical Biochemistry

View full text Add to dashboard Cite

Liquid chromatography-electrospray ionization-mass spectrometry and liquid chromatographytandem mass spectrometry methods were developed to simultaneously determine the concentrations of angiotensin (Ang) II, Ang 1-7, Ang III and Ang IV in biological samples. The samples were extracted with C18 solid-phase extraction cartridges, and separated by a reverse-phase C18 column using acetonitrile in water with 0.1 % formic acid as a mobile phase. Angiotensin peptides were ionized by electrospray and detected by triple quadrupole mass spectrometry in the positive ion mode. (M+3H) 3+ and (M+2H) 2+ ions were chosen as the detected ions in the single ion recording (SIR) mode for LC-MS. The limits of detection (S/N=3) using SIR are 1 pg for Ang IV and 5 pg for Ang 1-7, Ang III and Ang II. Multiple reaction monitoring (MRM) mode was used for LC-MS/MS. The limits of detection (S/N=3) using MRM are 20 pg for Ang IV and 25 pg for Ang 1-7, Ang III and Ang II. These methods were applied to analyze angiotensin peptides in bovine adrenal microvascular endothelial cells. The results show that Ang II is metabolized by endothelial cells to Ang 1-7, Ang III and Ang IV with Ang 1-7 being the major metabolite.

show abstract

Section: Applications Of the Lc-ms And Lc-ms/ms Methodsmentioning

confidence: 99%

Simultaneous analysis of angiotensin peptides by LC–MS and LC–MS/MS: Metabolism by bovine adrenal endothelial cells

Cui

Nithipatikom

Campbell

2007

Analytical Biochemistry

View full text Add to dashboard Cite

show abstract

“…ACE2 shares 42% sequence identity to the catalytic domain of ACE (Vickers et al 2002;Towler et al 2004); however, it is insensitive to ACE inhibitors. ACE2 mediates the conversion of Ang I to angiotensin-(1-9) [Ang-(1-9)]-which can be metabolized into Ang-(1-7) by ACE-as well as the conversion of Ang II into Ang-(1-7).…”

Section: Angiotensin-converting Enzymementioning

confidence: 99%

“…Indeed, a balance of the two peptides may be required to circumvent many cardiovascular processes. Both ACE2 and prolyl oligopeptidase (POP), since they mediate the direct conversion of Ang II into Ang-(1-7) (Koida and Walter 1976;Vickers et al 2002), may work to regulate and balance the levels of the two peptides (Fig. 2).…”

Section: Angiotensin-(1-7) 163mentioning

confidence: 99%

Angiotensin‐(1‐7): Pharmacology and New Perspectives in Cardiovascular Treatments

Trask

Ferrario

2007

Cardiovascular Drug Reviews

101

View full text Add to dashboard Cite

Many advances have been made in the cardiovascular field in the last several decades. Among them is the progress completed to date on the heptapeptide member of the reninangiotensin system (RAS), angiotensin-(1-7) [Ang-(1-7)]. The peptide's beneficial actions against pathophysiological processes, such as cardiac arrhythmia, heart failure, hypertension, renal disease, preeclampsia, and even cancer are continuously being uncovered. This review encompasses the pharmacology of Ang-(1-7) and expounds upon the peptide's potential as a therapeutic agent against pathological processes both within and outside the cardiovascular continuum.

show abstract

“…ACE is the main enzyme that is responsible for the conversion of ANG I into ANG II, and ACE2 then cleaves ANG II into ANG-(1-7) [163]. Furthermore, ACE2 forms ANG-(1-9) from ANG I, and ANG-(1-9) can be converted into ANG-(1-7) by ACE [119].…”

Section: Synthesis Of Ang-(1-7)mentioning

confidence: 99%

“…Furthermore, ACE2 forms ANG-(1-9) from ANG I, and ANG-(1-9) can be converted into ANG-(1-7) by ACE [119]. However, the preferable physiological substrate for ACE2 is ANG II [120,163].…”

Section: Synthesis Of Ang-(1-7)mentioning

confidence: 99%

ANG II, ANG-(1-7), ALDO and AVP biphasic effects on Na+/H+ transport: the role of cellular calcium

Mello-Aires¹,

Dellova²,

Castelo‐Branco³

et al. 2017

Nephrol Renal Dis

View full text Add to dashboard Cite

This article reviews the main body of knowledge regarding NHE1 and NHE3 exchangers and their interaction with Angiotensin II, Angiotensin-(1-7), Aldosterone and Arginine Vasopressin, particularly their renal actions. This work addresses the biphasic effects of different hormonal doses on NHE1 or NHE3 in proximal tubule in Wistar, SHR (hypertensives) and their control WKY (normotensives) rats or MDCK cells (which share similarities with the collecting duct). The hormones were applied alone, with their inhibitors or plus agents that change the [Ca 2+ ]i. The data are compatible with hormonal stimulation of these exchangers by increases of [Ca 2+ ]i in lower range, and inhibition at high [Ca 2+ ]i. In MDCK cells and Wistar rats, low doses of ANG II, ALDO or AVP stimulated the exchangers, while high doses inhibited them. ANG-(1-7), in Wistar or WKY rats has inverse, dose-dependent effects. In SHR rats, the biphasic effects of ANG-(1-7) were similar to the effects of ANG II, ALDO or AVP in Wistar rats. The interactions between these effects may represent a mechanism that regulates extracellular volume. In hypertensives animals, a high plasma level of ANG-(1-7) inhibited NHE3 in the proximal tubule, which mitigated hypertension. Figure 6 shows a schematic model to describe these biphasic hormonal effects.

show abstract

Hydrolysis of Biological Peptides by Human Angiotensin-converting Enzyme-related Carboxypeptidase

Cited by 1,302 publications

References 26 publications

Simultaneous analysis of angiotensin peptides by LC–MS and LC–MS/MS: Metabolism by bovine adrenal endothelial cells

Simultaneous analysis of angiotensin peptides by LC–MS and LC–MS/MS: Metabolism by bovine adrenal endothelial cells

Angiotensin‐(1‐7): Pharmacology and New Perspectives in Cardiovascular Treatments

ANG II, ANG-(1-7), ALDO and AVP biphasic effects on Na+/H+ transport: the role of cellular calcium

Contact Info

Product

Resources

About