http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11575
Sorcin modulates cardiac L-type Ca(2+) current by functional interaction with the alpha(1C) subunit in rabbits (Articolo in rivista)
- Type
- Label
- Sorcin modulates cardiac L-type Ca(2+) current by functional interaction with the alpha(1C) subunit in rabbits (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1113/expphysiol.2008.043497 (literal)
- Alternative label
Fowler MR; Colotti G; Chiancone E; Smith GL; Fearon M (2008)
Sorcin modulates cardiac L-type Ca(2+) current by functional interaction with the alpha(1C) subunit in rabbits
in Experimental physiology (Print); Wiley-Blackwell Publishing, Inc., Malden (Stati Uniti d'America)
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- Fowler MR; Colotti G; Chiancone E; Smith GL; Fearon M (literal)
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- ISI Web of Science (WOS) (literal)
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- 1. Univ Glasgow, Fac Biomed & Life Sci, Glasgow G12 8QQ, Lanark, Scotland
2. CNR, Inst Biol & Patol Mol, Univ Roma La Sapienza, Dipartimento Sci Biochim, Rome, Italy
3. Univ Manchester, Core Technol Facil, Fac Life Sci, Manchester M13 9PL, Lancs, England (literal)
- Titolo
- Sorcin modulates cardiac L-type Ca(2+) current by functional interaction with the alpha(1C) subunit in rabbits (literal)
- Abstract
- We examined the modulation of the cardiac L-type Ca(2+) channel (LTCC) by the regulatory protein sorcin and tested the hypothesis that modulation occurred by direct interaction. Whole-cell patch-clamp recordings were made on native rabbit ventricular myocytes and HEK 293 cells expressing cardiac alpha(1C) subunits. In ventricular cells, sorcin increased peak current when using either Ca(2+) or Ba(2+) as charge carriers. In HEK 293 cells, sorcin increased peak current density when using Ba(2+) as a charge carrier but not when using Ca(2+). In ventricular myocytes, current inactivation (tau(fast), in ms) was slowed by sorcin with Ca(2+) as the charge carrier, whilst in the presence of Ba(2+) it was enhanced. In HEK 293 cells, sorcin significantly enhanced tau(fast), but no significant change was observed with Ba(2+). This trend was mimicked by the truncated peptide, sorcin Ca(2+)-binding domain, which lacks the N-terminal domain. These data suggest that sorcin interacts with LTCC via its C-terminal domain, which alters current magnitude and tau(fast). These effects appear to be influenced by the prevailing experimental conditions. (literal)
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