Analysis of Angiotensin Metabolism in the Kidney Using Mass Spectrometry
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.
Key wordsMass spectrometry MALDI Imaging Renin-angiotensin system Kidney Enzyme activity Angiotensin metabolism ACE ACE2 NEP
This work was supported by National Institutes of Health Grants F32 DK-093226 and the Carl W. Gottschalk Research Scholar Grant of the ASN Foundation for Kidney Research to N.G. and R01 HL-093567 to K.M.E.
- 2.Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, Breitbart RE, Acton S (2000) A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res 87:E1–E9CrossRefPubMedGoogle Scholar