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10.1152/ajpheart.00911.2013 http://scihub22266oqcxt.onion/10.1152/ajpheart.00911.2013 C3962633!3962633!24464749     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Am+J+Physiol+Heart+Circ+Physiol 2014 ; 306 (7): H1032-40 Nephropedia Template TP {{tp|p=24464749|t=2014. Novel role of aminopeptidase-A in angiotensin-(1?7) metabolism post myocardial infarction |pdf=|usr=}}{{24464749}} gab.com Text Novel role of aminopeptidase-A in angiotensin-(1 7) metabolism post myocardial infarction JO: Am J Physiol Heart Circ Physiol http://www.kidney.de/pget.php?&tw=1&pmid=24464749 #FOAvip Aminopeptidase-A (APA) is a less well-studied enzyme of the renin-angiotensin system. We propose that it is involved in cardiac angiotensin (ANG) metabolism and its pathologies. ANG-(1?7) can ameliorate remodeling after myocardial injury. The aims of this study are to 1) develop mass spectrometric (MS) approaches for the assessment of ANG processing by APA within the myocardium; and 2) investigate the role of APA in cardiac ANG-(1?7) metabolism after myocardial infarction (MI) using sensitive MS techniques. MI was induced in C57Bl/6 male mice by ligating the left anterior descending (LAD) artery. Frozen mouse heart sections (in situ assay) or myocardial homogenates (in vitro assay) were incubated with the endogenous APA substrate, ANG II. Results showed concentration- and time-dependent cardiac formation of ANG III from ANG II, which was inhibited by the specific APA inhibitor, 4-amino-4-phosphonobutyric acid. Myocardial APA activity was significantly increased 24 h after LAD ligation (0.82 ± 0.02 vs. 0.32 ± 0.02 ?mol·min?1·?g?1, MI vs. sham, P < 0.01). Both MS enzyme assays identified the presence of a new peptide, ANG-(2?7), m/z 784, which accumulated in the MI (146.45 ± 6.4 vs. 72.96 ± 7.0%, MI vs. sham, P < 0.05). Use of recombinant APA enzyme revealed that APA is responsible for ANG-(2?7) formation from ANG-(1?7). APA exhibited similar substrate affinity for ANG-(1?7) compared with ANG II {Km (ANG II) = 14.67 ± 1.6 vs. Km [ANG-(1?7)] = 6.07 ± 1.12 ?mol/l, P < 0.05}. Results demonstrate a novel role of APA in ANG-(1?7) metabolism and suggest that the upregulation of APA, which occurs after MI, may deprive the heart of cardioprotective ANG-(1?7). Thus APA may serve as a potentially novel therapeutic target for management of tissue remodeling after MI. Twit Text FOAVip Novel role of aminopeptidase-A in angiotensin-(1 7) metabolism post myocardial infarction ????Am J Physiol Heart Circ Physiol http://www.kidney.de/pget.php?&tw=1&pmid=24464749 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24464749 #FOAvip English Wikipedia <ref>{{Cite pmid|24464749}}</ref> Novel role of aminopeptidase-A in angiotensin-(1?7) metabolism post myocardial infarction #MMPMID24464749 Alghamri MS; Morris M; Meszaros JG; Elased KM; Grobe N Am J Physiol Heart Circ Physiol 2014[Apr]; 306 (7): H1032-40 PMID24464749show ga Aminopeptidase-A (APA) is a less well-studied enzyme of the renin-angiotensin system. We propose that it is involved in cardiac angiotensin (ANG) metabolism and its pathologies. ANG-(1?7) can ameliorate remodeling after myocardial injury. The aims of this study are to 1) develop mass spectrometric (MS) approaches for the assessment of ANG processing by APA within the myocardium; and 2) investigate the role of APA in cardiac ANG-(1?7) metabolism after myocardial infarction (MI) using sensitive MS techniques. MI was induced in C57Bl/6 male mice by ligating the left anterior descending (LAD) artery. Frozen mouse heart sections (in situ assay) or myocardial homogenates (in vitro assay) were incubated with the endogenous APA substrate, ANG II. Results showed concentration- and time-dependent cardiac formation of ANG III from ANG II, which was inhibited by the specific APA inhibitor, 4-amino-4-phosphonobutyric acid. Myocardial APA activity was significantly increased 24 h after LAD ligation (0.82 ± 0.02 vs. 0.32 ± 0.02 ?mol·min?1·?g?1, MI vs. sham, P < 0.01). Both MS enzyme assays identified the presence of a new peptide, ANG-(2?7), m/z 784, which accumulated in the MI (146.45 ± 6.4 vs. 72.96 ± 7.0%, MI vs. sham, P < 0.05). Use of recombinant APA enzyme revealed that APA is responsible for ANG-(2?7) formation from ANG-(1?7). APA exhibited similar substrate affinity for ANG-(1?7) compared with ANG II {Km (ANG II) = 14.67 ± 1.6 vs. Km [ANG-(1?7)] = 6.07 ± 1.12 ?mol/l, P < 0.05}. Results demonstrate a novel role of APA in ANG-(1?7) metabolism and suggest that the upregulation of APA, which occurs after MI, may deprive the heart of cardioprotective ANG-(1?7). Thus APA may serve as a potentially novel therapeutic target for management of tissue remodeling after MI. äNovel role of aminopeptidase-A in angiotensin-(1?7) metabolism post my(epmc).pdf DeepDyve Pubget Overpricing