http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11569
Complex modulation of L-type Ca(2+) current inactivation by sorcin in isolated rabbit cardiomyocytes. (Articolo in rivista)
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- Complex modulation of L-type Ca(2+) current inactivation by sorcin in isolated rabbit cardiomyocytes. (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00424-008-0575-5 (literal)
- Alternative label
Fowler MR; Colotti G; Chiancone E; Higuchi Y; Seidler T; Smith GL. (2009)
Complex modulation of L-type Ca(2+) current inactivation by sorcin in isolated rabbit cardiomyocytes.
in Pflügers Archiv; SPRINGER, 233 SPRING ST, NEW YORK, NY 10013 (Stati Uniti d'America)
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- Fowler MR; Colotti G; Chiancone E; Higuchi Y; Seidler T; Smith GL. (literal)
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- 1. Fac Biomed & Life Sci, Glasgow G12 8QQ, Lanark, Scotland
2. Univ Gottingen, Dept Cardiol & Pneumol, D-37075 Gottingen, Germany
3. Univ Roma La Sapienza, CNR, Dipartimento Sci Biochim, Inst Biol & Patol Mol, Rome, Italy
4. Univ Glasgow, Fac Biomed & Life Sci, Glasgow, Lanark, Scotland (literal)
- Titolo
- Complex modulation of L-type Ca(2+) current inactivation by sorcin in isolated rabbit cardiomyocytes. (literal)
- Abstract
- Modulation of the L-type Ca(2+) channel (LTCC) by sorcin was investigated by measuring the L-type Ca(2+) current (I (Ca,L)) in isolated rabbit ventricular myocytes using ruptured patch, single electrode voltage clamp in the absence of extracellular Na(+). Fifty millimolars EGTA (170 nM Ca(2+)) in the pipette solution buffered bulk cytoplasmic [Ca(2+)], but retained rapid Ca(2+)-dependant inactivation of I (Ca,L,). Recombinant sorcin (3 mu M) in the pipette significantly slowed time-dependant inactivation (tau (fast): 8.8 +/- 0.9 vs. 15.1 +/- 1.7 ms). Sorcin had no significant effect on I (Ca,L,) after inhibition of the sarcoplasmic reticulum (SR). Using 10 mM 1,2-bis(o-N,N,N',N'-tetraacetic acid (170 nM Ca(2+)), I (Ca,L) inactivation was then determined by a Ca(2+) -independent, voltage-dependant process. Under these conditions, 3 mu M sorcin speeded up inactivation. A similar effect was observed by substitution of Ca(2+) with Ba(2+). Down-regulation of endogenous sorcin to 27 +/- 7% using an RNAi adenoviral vector slowed inactivation of I (Ca,L) by similar to 42%. The effects of sorcin on voltage-dependant inactivation were mimicked by a truncated form of the protein containing only the Ca(2+)-binding domain. This data is consistent with two independent actions of sorcin on the LTCC: (1) slowing Ca(2+)-dependant inactivation and (2) stimulating voltage-dependant inactivation. The net effect of sorcin on the time-dependent inactivation of I (Ca,L) was a balance between these two effects. Under normal conditions, sorcin slows I (Ca,L) inactivation because the effects of Ca(2+)-dependant inactivation out-weigh the effects on voltage-dependant inactivation. (literal)
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