Analysis of Angiotensin Metabolism in the Kidney Using Mass Spectrometry

Nadja Grobe, Khalid M. Elased

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The renin angiotensin system (RAS) is a highly complex enzymatic system consisting of multiple peptide hormones, enzymes, and receptors. A thorough characterization of angiotensin peptide metabolism is crucial for understanding pathological states associated with an imbalanced RAS. Here, we describe two matrix-assisted laser desorption/ionization (MALDI) mass spectrometric (MS) approaches for the assessment of in vitro and in situ RAS enzymatic activities in the kidney using the natural angiotensin peptide substrates. These MS techniques demonstrate high specificity and are superior over conventional spectrophotometric or colorimetric assays since multiple proteolytic cleavage sites can be detected, thus unraveling the complexity of the RAS.
Original languageEnglish
Title of host publicationThe Renin-Angiotensin-Aldosterone System
Subtitle of host publicationMethods and Protocols
EditorsSean E. Thatcher
PublisherHumana Press Inc.
Pages189-197
Number of pages9
ISBN (Electronic)978-1-4939-7030-8
ISBN (Print)978-1-4939-7028-5, 978-1-4939-8373-5
DOIs
StatePublished - 2017

Publication series

NameMethods in Molecular Biology
Volume1614
ISSN (Print)1064-3745

ASJC Scopus Subject Areas

  • Molecular Biology
  • Genetics

Keywords

  • ACE
  • ACE2
  • Angiotensin metabolism
  • Enzyme activity
  • Imaging
  • Kidney
  • MALDI
  • Mass spectrometry
  • NEP
  • Renin-angiotensin system

Disciplines

  • Molecular Biology

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