| http://purl.uniprot.org/citations/21613513 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21613513 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21613513 | http://www.w3.org/2000/01/rdf-schema#comment | "The trout heart is 10-fold more sensitive to Ca(2+) than the mammalian heart. This difference is due, in part, to cardiac troponin C (cTnC) from trout having a greater Ca(2+) affinity than human cTnC. To determine what other proteins are involved, we cloned cardiac troponin I (cTnI) from the trout heart and determined how it alters the Ca(2+) affinity of a cTn complex containing all mammalian components (mammalian cTn). Ca(2+) activation of the complex was characterized using a human cTnC mutant that contains anilinonapthalenesulfote iodoacetamide attached to Cys53. When the cTn complex containing labeled human cTnC was titrated with Ca(2+), its fluorescence changed, reaching an asymptote upon saturation. Our results reveal that trout cTnI lacks the N-terminal extension found in cTnI from all other vertebrate groups. This protein domain contains two targets (Ser23 and Ser24) for protein kinase A (PKA) and protein kinase C. When these are phosphorylated, the rate of cardiomyocyte relaxation increases. When rat cTnI in the mammalian cTn complex was replaced with trout cTnI, the Ca(2+) affinity was increased ∼1.8-fold. This suggests that trout cTnI contributes to the high Ca(2+) sensitivity of the trout heart. Treatment of the two cTn complexes with PKA decreased the Ca(2+) affinity of both complexes. However, the change for the complex containing rat cTnI was 2.2-fold that of the complex containing trout cTnI. This suggests that the phosphorylation of trout cTnI does not play as significant a role in regulating cTn function in trout."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.org/dc/terms/identifier | "doi:10.1242/jeb.052860"xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.org/dc/terms/identifier | "doi:10.1242/jeb.052860"xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/author | "Gillis T.E."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/author | "Gillis T.E."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/author | "Kirkpatrick K.P."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/author | "Kirkpatrick K.P."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/author | "Klaiman J.M."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/author | "Klaiman J.M."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/author | "Robertson A.S."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/author | "Robertson A.S."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/name | "J. Exp. Biol."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/name | "J Exp Biol"xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/pages | "1981-1988"xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/pages | "1981-1988"xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/title | "The influence of trout cardiac troponin I and PKA phosphorylation on the Ca2+ affinity of the cardiac troponin complex."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/title | "The influence of trout cardiac troponin I and PKA phosphorylation on the Ca2+ affinity of the cardiac troponin complex."xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/volume | "214"xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://purl.uniprot.org/core/volume | "214"xsd:string |
| http://purl.uniprot.org/citations/21613513 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21613513 |
| http://purl.uniprot.org/citations/21613513 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21613513 |