CALL FOR PAPERS Proteomic and Metabolomic Approaches to Cell Physiology and Pathophysiology Identification of prolyl carboxypeptidase as an alternative enzyme for processing of renal angiotensin II using mass spectrometry
نویسندگان
چکیده
Nadja Grobe, Nathan M. Weir, Orly Leiva, Frank S. Ong, Kenneth E. Bernstein, Alvin H. Schmaier, Mariana Morris, and Khalid M. Elased Department of Pharmacology and Toxicology, Wright State University Boonshoft School of Medicine, Dayton, Ohio; Department of Biomedical Sciences, Cedars-Sinai Medical Center, Los Angeles, California; and University Hospitals Case Medical Center, Case Western Reserve University, Cleveland, Ohio
منابع مشابه
Identification of prolyl carboxypeptidase as an alternative enzyme for processing of renal angiotensin II using mass spectrometry.
Angiotensin-converting enzyme 2 (ACE2) catalyzes conversion of ANG II to ANG-(1-7). The present study uses newly established proteomic approaches and genetic mouse models to examine the contribution of alternative renal peptidases to ACE2-independent formation of ANG-(1-7). In situ and in vitro mass spectrometric characterization showed that substrate concentration and pH control renal ANG II p...
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HYPERTENSION, WHICH AFFECTS one-third of the population, is commonly treated with inhibitors of ANG II production or action, as this hormone triggers vasoconstriction and raises extracellular volume by increasing sodium reabsorption along the nephron. ANG II, an octapeptide [ANG-(1–8)], emanates from the enzymatic cleavage of the 50-kDa precursor angiotensinogen by renin and angiotensin-convert...
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To better understand the tissue distribution and activity of enzymes involved in angiotensin II (Ang II) processing, we developed a novel molecular imaging method using matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry. Mouse kidney sections (12 μm) were incubated with 10-1,000 μmol/l Ang II for 5-15 min at 37°C. The formed peptides Ang III and Ang-(1-7) w...
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