| pubmed-article:14596793 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C0949658 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C0001291 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C1305957 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:14596793 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:14596793 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:14596793 | pubmed:dateCreated | 2003-11-4 | lld:pubmed |
| pubmed-article:14596793 | pubmed:abstractText | cAMP-dependent protein kinase (PKA)-dependent phosphorylation of the two serine residues in the amino terminal region unique to cardiac troponin I (cTnI) is known to cause two effects: (i) decrease of the maximum Ca2+-controlled thin filament-activated myosin S1-ATPase (actoS1-ATPase) activity and mean sliding velocity of reconstituted thin filaments; (ii) rightward shift of the Ca2+ activation curves of actoS1-ATPase activity, filament sliding velocity, and force generation. We have studied the influence of phosphorylation of human wild-type cTnI and of two mutant cTnI (G203S and K206Q) causing familial hypertrophic cardiomyopathy (fHCM) on the secondary structure by circular dichroism spectroscopy and on the Ca2+ regulation of actin-myosin interaction using actoS1-ATPase activity and in vitro motility assays. Both mutations slightly influence the backbone structure of cTnI but only the secondary structure of cTnI-G203S is also affected by bis-phosphorylation of cTnI. In functional studies, cTnI-G203S behaves similarly to wild-type cTnI, i.e. the mutation itself has no measurable effect and bis-phosphorylation alters the actoS1-ATPase activity and the in vitro thin filament motility in the same way as does bis-phosphorylation of wild-type cTnI. In contrast, the mutation K206Q leads to a considerable increase in the maximum actoS1-ATPase activity as well as filament motility compared to wild-type cTnI. Bis-phosphorylation of this mutant cTnI still suppresses the maximum actoS1-ATPase activity and filament sliding velocity but does no longer affect the Ca2+ sensitivity of these processes. Thus, these two fHCM-linked cTnI mutations, although reflecting similar pathological situations, exert different effects on the actomyosin system per se and in response to bis-phosphorylation of cTnI. | lld:pubmed |
| pubmed-article:14596793 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:14596793 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14596793 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14596793 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:14596793 | pubmed:issn | 0022-2828 | lld:pubmed |
| pubmed-article:14596793 | pubmed:author | pubmed-author:DingA SAS | lld:pubmed |
| pubmed-article:14596793 | pubmed:author | pubmed-author:SchmidtmannAn... | lld:pubmed |
| pubmed-article:14596793 | pubmed:author | pubmed-author:JaquetKorneli... | lld:pubmed |
| pubmed-article:14596793 | pubmed:author | pubmed-author:HeilmeyerLudw... | lld:pubmed |
| pubmed-article:14596793 | pubmed:author | pubmed-author:ThieleczekRol... | lld:pubmed |
| pubmed-article:14596793 | pubmed:author | pubmed-author:KruseSebastia... | lld:pubmed |
| pubmed-article:14596793 | pubmed:author | pubmed-author:FilatovVladim... | lld:pubmed |
| pubmed-article:14596793 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14596793 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:14596793 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14596793 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14596793 | pubmed:pagination | 1365-74 | lld:pubmed |
| pubmed-article:14596793 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:14596793 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14596793 | pubmed:articleTitle | Phosphorylation of human cardiac troponin I G203S and K206Q linked to familial hypertrophic cardiomyopathy affects actomyosin interaction in different ways. | lld:pubmed |
| pubmed-article:14596793 | pubmed:affiliation | St. Josef-Hospital, Klinik der Ruhr-Universität Bochum, Gudrunstrasse 56, 44791 Bochum, Germany. | lld:pubmed |
| pubmed-article:14596793 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14596793 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:14596793 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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