Mp490formation of Ang(1−7) From Angii(1−8) Is Largely Independent of Ace2 and PRCP

Serfózó, Péter; Wysocki, Jan; Liu, Pan; Ye, Minghao; Müller, Tilman; Jin, Jing; Batlle, Daniel

doi:10.1093/ndt/gfx174.mp490

Nephrology Dialysis Transplantation

2017

DOI: 10.1093/ndt/gfx174.mp490

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Mp490formation of Ang(1−7) From Angii(1−8) Is Largely Independent of Ace2 and PRCP

Péter Serfózó

Jan Wysocki

Pan Liu

et al.

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“…Of note, very little is known about the relative strength and actions of enzymes other than ACE2 that form Ang-(1-7) from Ang II (1-8)23. This limited information is due in part to the short half-life of Ang-(1-7) and other downstream metabolites, such as Ang-(1-5)24.…”

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A Fluorometric Method of Measuring Carboxypeptidase Activities for Angiotensin II and Apelin-13

Liu

Wysocki

Serfózó

et al. 2017

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Degradation of the biologically potent octapeptide angiotensin Ang II-(1-8) is mediated by the activities of several peptidases. The conversion of Ang II to the septapeptide Ang-(1-7) is of particular interest as the latter also confers organ protection. The conversion is catalyzed by angiotensin-converting enzyme 2 and other enzymes that selectively cleave the peptide bond between the proline and the phenylalanine at the carboxyl terminus of Ang II. The contribution of various enzyme activities that collectively lead to the formation of Ang-(1-7) from Ang II, in both normal conditions and in disease states, remains only partially understood. This is largely due to the lack of a reliable and sensitive method to detect these converting activities in complex samples, such as blood and tissues. Here, we report a fluorometric method to measure carboxypeptidase activities that cleave the proline-phenylalanine dipeptide bond in Ang II. This method is also suitable for measuring the conversion of apelin-13. The assay detects the release of phenylalanine amino acid in a reaction with the yeast enzyme of phenylalanine ammonia lyase (PAL). When used in cell and mouse organs, the assay can robustly measure endogenous Ang II and apelin-13-converting activities involved in the renin-angiotensin and the apelinergic systems, respectively.

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confidence: 99%

A Fluorometric Method of Measuring Carboxypeptidase Activities for Angiotensin II and Apelin-13

Liu

Wysocki

Serfózó

et al. 2017

Sci Rep

Self Cite

View full text Add to dashboard Cite

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Mp490formation of Ang(1−7) From Angii(1−8) Is Largely Independent of Ace2 and PRCP

Cited by 1 publication

References 0 publications

A Fluorometric Method of Measuring Carboxypeptidase Activities for Angiotensin II and Apelin-13

A Fluorometric Method of Measuring Carboxypeptidase Activities for Angiotensin II and Apelin-13

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