RGD Reference Report - Expression and functional properties of four slow skeletal troponin T isoforms in rat muscles. - Rat Genome Database

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Expression and functional properties of four slow skeletal troponin T isoforms in rat muscles.

Authors: Kischel, P  Bastide, B  Muller, M  Dubail, F  Offredi, F  Jin, JP  Mounier, Y  Martial, J 
Citation: Kischel P, etal., Am J Physiol Cell Physiol. 2005 Aug;289(2):C437-43. Epub 2005 Mar 23.
RGD ID: 1599482
Pubmed: PMID:15788488   (View Abstract at PubMed)
DOI: DOI:10.1152/ajpcell.00365.2004   (Journal Full-text)

We investigated the expression and functional properties of slow skeletal troponin T (sTnT) isoforms in rat skeletal muscles. Four sTnT cDNAs were cloned from the slow soleus muscle. Three isoforms were found to be similar to sTnT1, sTnT2, and sTnT3 isoforms described in mouse muscles. A new rat isoform, with a molecular weight slightly higher than that of sTnT3, was discovered. This fourth isoform had never been detected previously in any skeletal muscle and was therefore called sTnTx. From both expression pattern and functional measurements, it appears that sTnT isoforms can be separated into two classes, high-molecular-weight (sTnT1, sTnT2) and low-molecular-weight (sTnTx, sTnT3) isoforms. By comparison to the apparent migration pattern of the four recombinant sTnT isoforms, the newly described low-molecular-weight sTnTx isoform appeared predominantly and typically expressed in fast skeletal muscles, whereas the higher-molecular-weight isoforms were more abundant in slow soleus muscle. The relative proportion of the sTnT isoforms in the soleus was not modified after exposure to hindlimb unloading (HU), known to induce a functional atrophy and a slow-to-fast isoform transition of several myofibrillar proteins. Functional data gathered from replacement of endogenous troponin complexes in skinned muscle fibers showed that the sTnT isoforms modified the Ca(2+) activation characteristics of single skeletal muscle fibers, with sTnT2 and sTnT1 conferring a similar increase in Ca(2+) affinity higher than that caused by low-molecular-weight isoforms sTnTx and sTnT3. Thus we show for the first time the presence of sTnT in fast muscle fibers, and our data show that the changes in neuromuscular activity on HU are insufficient to alter the sTnT expression pattern.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
slow-twitch skeletal muscle fiber contraction  IDA 1599482 RGD 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
troponin complex  IDA 1599482 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
troponin T binding  IDA 1599482 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Tnnt1  (troponin T1, slow skeletal type)


Additional Information