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10.1016/s0006-291x(03)00453-4 http://scihub22266oqcxt.onion/10.1016/s0006-291x(03)00453-4 12670503!ä!12670503 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Biophys+Res+Commun 2003 ; 303 (3): 947-53 Nephropedia Template TP {{tp|p=12670503|t=2003. Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells |pdf=|usr=}}{{12670503}} gab.com Text Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells JO: Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=12670503 #FOAvip Three HIF-alpha prolyl-4-hydroxylases (PHDs) (named PHD1, PHD2, and PHD3) effect the proteasome-mediated degradation of HIF by catalyzing the hydroxylation of key proline residues in the HIF-1 alpha subunit under normoxic conditions. When oxygen tension is reduced, PHD-mediated hydroxylation cannot occur, HIF-1 alpha accumulates in the nucleus, resulting in HIF-mediated gene transcription. In the present study, the expression and regulation of PHD mRNA and HIF protein expression was examined in human tissues and primary cells of cardiovascular origin. Treatment of human cardiac myocytes, smooth muscle cells, and endothelial cells with hypoxia or CoCl(2), a hypoxia mimic, resulted in a significant time-dependent increase in PHD3, but not PHD1 or PHD2, mRNA levels, which correlated with an increase in HIF-1 alpha protein expression. Overexpression studies revealed that PHD3 levels influence HIF-1 alpha stability in both normoxic and hypoxic conditions, suggesting that PHD3 may participate in a feedback loop controlling HIF activity. Twit Text FOAVip Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells ????Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=12670503 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=12670503 #FOAvip English Wikipedia <ref>{{Cite pmid|12670503}}</ref> Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells #MMPMID12670503 Cioffi CL; Liu XQ; Kosinski PA; Garay M; Bowen BR Biochem Biophys Res Commun 2003[Apr]; 303 (3): 947-53 PMID12670503show ga Three HIF-alpha prolyl-4-hydroxylases (PHDs) (named PHD1, PHD2, and PHD3) effect the proteasome-mediated degradation of HIF by catalyzing the hydroxylation of key proline residues in the HIF-1 alpha subunit under normoxic conditions. When oxygen tension is reduced, PHD-mediated hydroxylation cannot occur, HIF-1 alpha accumulates in the nucleus, resulting in HIF-mediated gene transcription. In the present study, the expression and regulation of PHD mRNA and HIF protein expression was examined in human tissues and primary cells of cardiovascular origin. Treatment of human cardiac myocytes, smooth muscle cells, and endothelial cells with hypoxia or CoCl(2), a hypoxia mimic, resulted in a significant time-dependent increase in PHD3, but not PHD1 or PHD2, mRNA levels, which correlated with an increase in HIF-1 alpha protein expression. Overexpression studies revealed that PHD3 levels influence HIF-1 alpha stability in both normoxic and hypoxic conditions, suggesting that PHD3 may participate in a feedback loop controlling HIF activity. |Base Sequence[MESH] |Cardiovascular System/*metabolism[MESH] |Cell Hypoxia/genetics[MESH] |Cells, Cultured[MESH] |Cobalt/pharmacology[MESH] |DNA Primers/genetics[MESH] |Endothelium, Vascular/metabolism[MESH] |Feedback[MESH] |Gene Expression Regulation/drug effects[MESH] |Humans[MESH] |Hypoxia-Inducible Factor 1, alpha Subunit[MESH] |Hypoxia/*genetics[MESH] |Kinetics[MESH] |Muscle, Smooth, Vascular/metabolism[MESH] |Myocardium/metabolism[MESH] |Procollagen-Proline Dioxygenase/*genetics[MESH] |RNA, Messenger/genetics/metabolism[MESH] |Reverse Transcriptase Polymerase Chain Reaction[MESH]Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by h(epmc).pdf DeepDyve Pubget Overpricing