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10.1016/j.peptides.2016.06.005 http://scihub22266oqcxt.onion/10.1016/j.peptides.2016.06.005 C5500233!5500233 !27315786     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27315786 &cmd=llinks): Failed to open stream: HTTP request failed! 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Identification of dipeptidyl peptidase 3 as the Angiotensin-(1-7) degrading peptidase in human HK-2 renal epithelial cells |pdf=|usr=}}{{27315786 }} gab.com Text Identification of dipeptidyl peptidase 3 as the Angiotensin-(1-7) degrading peptidase in human HK-2 renal epithelial cells JO: Peptides http://www.kidney.de/pget.php?&tw=1&pmid=27315786 #FOAvip Angiotensin-(1-7) (Ang-(1-7)) is expressed within the kidney and exhibits renoprotective actions that antagonize the inflammatory, fibrotic and pro-oxidant effects of the Ang II-AT1 receptor axis. We previously identified a peptidase activity from sheep brain, proximal tubules and human HK-2 proximal tubule cells that metabolized Ang-(1-7); thus, the present study isolated and identified the Ang-(1-7) peptidase. Utilizing ion exchange and hydrophobic interaction chromatography, a single 80kDa protein band on SDS-PAGE was purified from HK-2 cells. The 80kDa band was excised, the tryptic digest peptides analyzed by LC-MS and a protein was identified as the enzyme dipeptidyl peptidase 3 (DPP 3, EC: 3.4.14.4). A human DPP 3 antibody identified a single 80kDa band in the purified enzyme preparation identical to recombinant human DPP 3. Both the purified Ang-(1-7) peptidase and DPP 3 exhibited an identical hydrolysis profile of Ang-(1-7) and both activities were abolished by the metallopeptidase inhibitor JMV-390. DPP 3 sequentially hydrolyzed Ang-(1-7) to Ang-(3-7) and rapidly converted Ang-(3-7) to Ang-(5-7). Kinetic analysis revealed that Ang-(3-7) was hydrolyzed at a greater rate than Ang-(1-7) [17.9 vs. 5.5 nmol/min/?g protein], and the Km for Ang-(3-7) was lower than Ang-(1-7) [3 vs. 12?M]. Finally, chronic treatment of the HK-2 cells with 20nM JMV-390 reduced intracellular DPP 3 activity and tended to augment the cellular levels of Ang-(1-7). We conclude that DPP 3 may influence the cellular expression of Ang-(1-7) and potentially reflect a therapeutic target to augment the actions of the peptide. Twit Text FOAVip Identification of dipeptidyl peptidase 3 as the Angiotensin-(1-7) degrading peptidase in human HK-2 renal epithelial cells ????Peptides http://www.kidney.de/pget.php?&tw=1&pmid=27315786 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27315786 #FOAvip English Wikipedia <ref>{{Cite pmid|27315786 }}</ref> Identification of dipeptidyl peptidase 3 as the Angiotensin-(1-7) degrading peptidase in human HK-2 renal epithelial cells #MMPMID27315786 Cruz-Diaz N ; Wilson BA ; Pirro NT ; Brosnihan KB ; Marshall AC ; Chappell MC Peptides 2016[Sep]; 83 (ä): 29-37 PMID27315786 show ga Angiotensin-(1-7) (Ang-(1-7)) is expressed within the kidney and exhibits renoprotective actions that antagonize the inflammatory, fibrotic and pro-oxidant effects of the Ang II-AT1 receptor axis. We previously identified a peptidase activity from sheep brain, proximal tubules and human HK-2 proximal tubule cells that metabolized Ang-(1-7); thus, the present study isolated and identified the Ang-(1-7) peptidase. Utilizing ion exchange and hydrophobic interaction chromatography, a single 80kDa protein band on SDS-PAGE was purified from HK-2 cells. The 80kDa band was excised, the tryptic digest peptides analyzed by LC-MS and a protein was identified as the enzyme dipeptidyl peptidase 3 (DPP 3, EC: 3.4.14.4). A human DPP 3 antibody identified a single 80kDa band in the purified enzyme preparation identical to recombinant human DPP 3. Both the purified Ang-(1-7) peptidase and DPP 3 exhibited an identical hydrolysis profile of Ang-(1-7) and both activities were abolished by the metallopeptidase inhibitor JMV-390. DPP 3 sequentially hydrolyzed Ang-(1-7) to Ang-(3-7) and rapidly converted Ang-(3-7) to Ang-(5-7). Kinetic analysis revealed that Ang-(3-7) was hydrolyzed at a greater rate than Ang-(1-7) [17.9 vs. 5.5 nmol/min/?g protein], and the Km for Ang-(3-7) was lower than Ang-(1-7) [3 vs. 12?M]. Finally, chronic treatment of the HK-2 cells with 20nM JMV-390 reduced intracellular DPP 3 activity and tended to augment the cellular levels of Ang-(1-7). We conclude that DPP 3 may influence the cellular expression of Ang-(1-7) and potentially reflect a therapeutic target to augment the actions of the peptide. |Angiotensin I/*genetics/metabolism [MESH] |Angiotensin II/genetics/*metabolism [MESH] |Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/*genetics/metabolism [MESH] |Epithelial Cells/metabolism [MESH] |Humans [MESH] |Hydrolysis [MESH] |Kidney/drug effects/*metabolism [MESH] |Oligopeptides/administration & dosage [MESH] |Peptide Fragments/*genetics/metabolism [MESH]Identification of dipeptidyl peptidase 3 as the Angiotensin-(1-7) degr(epmc).pdf DeepDyve Pubget Overpricing