11812163

Source:http://linkedlifedata.com/resource/pubmed/id/11812163

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0031715, umls-concept:C0040223, umls-concept:C0070876, umls-concept:C0086168, umls-concept:C0441712, umls-concept:C0750729, umls-concept:C1704259, umls-concept:C1705987, umls-concept:C1709915, umls-concept:C1882687
pubmed:issue	1
pubmed:dateCreated	2002-1-28
pubmed:abstractText	Sarcoplasmic reticulum (SR) dysfunction is one of the multiple alterations that occurs in ischemia-reperfused hearts. Because SR function is regulated by phosphorylation of phospholamban (PLB), a SR protein phosphorylated by cAMP-dependent protein kinase (PKA) at Ser(16)and Ca(2+)-calmodulin-dependent protein kinase (CaMKII) at Thr(17), the phosphorylation of these residues during ischemia and reperfusion was examined in Langendorff-perfused rat hearts. Ser(16)phosphorylation increased significantly after 20 min of ischemia from 2.5+/-0.6% to 99.8+/-25.5% of maximal isoproterenol-induced site-specific phosphorylation and decreased to control values immediately after reperfusion. Thr(17)phosphorylation transiently increased at 2-5 min of ischemia and at 1 min of reperfusion (R1, 166.2+/-28.2%). The ischemia-induced increase in Ser(16)phosphorylation was significantly diminished in hearts from catecholamine-depleted animals and/or after beta-blockade and abolished in the presence of the PKA-inhibitor, H-89. Thr(17)phosphorylation at the beginning of ischemia was blunted by nifedipine, whereas at R1 it was significantly diminished by perfusion with 0 m m Ca(2+)in the presence of EGTA and by the Na(+)/Ca(2+)exchanger inhibitor KB-R7943. KN-93, used to specifically inhibit CaMKII, decreased Thr(17)phosphorylation at R1 and significantly prolonged half relaxation time. The results demonstrated a dissociation between the phosphorylation of PLB sites, being phosphorylation of Ser(16)dependent on the beta-adrenergic cascade during ischemia and phosphorylation of Thr(17)on Ca(2+)influx both, at the beginning of ischemia and reperfusion. Phosphorylation of Thr(17)at the onset of reflow may provide the cell a mechanism to cope with Ca(2+)overload, transiently favoring the recovery of relaxation during early reperfusion.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0262322
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/2-(2-(4-(4-nitrobenzyloxy)phenyl)eth..., http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Catecholamines, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, beta, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Calcium Exchanger, http://linkedlifedata.com/resource/pubmed/chemical/Thiourea, http://linkedlifedata.com/resource/pubmed/chemical/Threonine, http://linkedlifedata.com/resource/pubmed/chemical/phospholamban
pubmed:status	MEDLINE
pubmed:month	Jan
pubmed:issn	0022-2828
pubmed:author	pubmed-author:FerreroPaolaP, pubmed-author:MattiazziAliciaA, pubmed-author:Mundiña-WeilenmannCeciliaC, pubmed-author:SaidMatildeM, pubmed-author:VittoneLeticiaL
pubmed:copyrightInfo	Copyright 2002 Academic Press.
pubmed:issnType	Print
pubmed:volume	34
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	39-50
pubmed:dateRevised	2007-11-15
pubmed:meshHeading	pubmed-meshheading:11812163-Animals, pubmed-meshheading:11812163-Blotting, Western, pubmed-meshheading:11812163-Calcium, pubmed-meshheading:11812163-Calcium-Binding Proteins, pubmed-meshheading:11812163-Catecholamines, pubmed-meshheading:11812163-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:11812163-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11812163-Enzyme Inhibitors, pubmed-meshheading:11812163-Heart, pubmed-meshheading:11812163-Ischemia, pubmed-meshheading:11812163-Male, pubmed-meshheading:11812163-Myocardium, pubmed-meshheading:11812163-Phosphorylation, pubmed-meshheading:11812163-Rats, pubmed-meshheading:11812163-Rats, Wistar, pubmed-meshheading:11812163-Receptors, Adrenergic, beta, pubmed-meshheading:11812163-Reperfusion Injury, pubmed-meshheading:11812163-Sarcoplasmic Reticulum, pubmed-meshheading:11812163-Serine, pubmed-meshheading:11812163-Sodium-Calcium Exchanger, pubmed-meshheading:11812163-Thiourea, pubmed-meshheading:11812163-Threonine, pubmed-meshheading:11812163-Time Factors
pubmed:year	2002
pubmed:articleTitle	Time course and mechanisms of phosphorylation of phospholamban residues in ischemia-reperfused rat hearts. Dissociation of phospholamban phosphorylation pathways.
pubmed:affiliation	Centro de Investigaciones Cardiovasculares, Facultad de Ciencias Médicas, Universidad Nacional de La Plata, 60 y 120, La Plata, Argentina.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't