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Published on: June 3, 2014
Passive stiffness changes caused by upregulation of compliant titin isoforms in human dilated cardiomyopathy hearts
I Makarenko1, C A Opitz, M C Leake
1Physiology and Biophysics Laboratory, University of Muenster,Muenster, Germany.
Insights
Dilated cardiomyopathy (DCM) alters titin protein expression, shifting towards larger isoforms and reducing titin
Area of Science:
- Cardiovascular Biology
- Molecular Cardiology
- Biophysics
Background:
- Cytoskeletal proteins are crucial in dilated cardiomyopathy (DCM) pathogenesis.
- Titin, a key cytoskeletal protein, influences myocardial mechanics.
Purpose of the Study:
- To investigate titin expression and its functional consequences in human dilated cardiomyopathy.
- To analyze titin isoform shifts and their impact on passive tension and stiffness.
Main Methods:
- Gel-electrophoresis, immunoblotting, and quantitative RT-PCR were used to analyze titin and obscurin expression in human heart samples.
- Histological analysis assessed myocyte area and connective tissue.
- Force measurements on isolated cardiomyofibrils and heart fiber bundles evaluated passive tension and stiffness.
Main Results:
- Dilated cardiomyopathy hearts showed a shift in titin isoforms, with increased expression of larger N2BA isoforms.
- Total titin mRNA levels were reduced in DCM hearts, correlating with increased fibrosis and reduced myocyte area.
- Passive tension and the contribution of titin to passive stiffness were significantly reduced in DCM hearts.
Conclusions:
- End-stage failing hearts exhibit a reduced proportion of titin-based stiffness due to titin loss, fibrosis, and isoform shifts.
- The observed titin-isoform shift in DCM may impact diastolic function favorably but could impair systolic performance.
Abstract:
In the pathogenesis of dilated cardiomyopathy, cytoskeletal proteins play an important role. In this study, we analyzed titin expression in left ventricles of 19 control human donors and 9 severely diseased (nonischemic) dilated cardiomyopathy (DCM) transplant-patients, using gel-electrophoresis, immunoblotting, and quantitative RT-PCR. Both human-heart groups coexpressed smaller (approximately 3 MDa) N2B-isoform and longer (3.20 to 3.35 MDa) N2BA-isoforms, but the average N2BA:N2B-protein ratio was shifted from approximately 30:70 in controls to 42:58 in DCM hearts, due mainly to increased expression of N2BA-isoforms >3.30 MDa. Titin per unit tissue was decreased in some DCM hearts. The titin-binding protein obscurin also underwent isoform-shifting in DCM. Quantitative RT-PCR revealed a 47% reduction in total-titin mRNA levels in DCM compared with control hearts, but no differences in N2B, all-N2BA, and individual-N2BA transcripts. The reduction in total-titin transcripts followed from a decreased area occupied by myocytes and increased connective tissue in DCM hearts, as detected by histological analysis. Force measurements on isolated cardiomyofibrils showed that sarcomeric passive tension was reduced on average by 25% to 30% in DCM, a reduction readily predictable with a model of wormlike-chain titin elasticity. Passive-tension measurements on human-heart fiber bundles, before and after titin proteolysis, revealed a much-reduced relative contribution of titin to total passive stiffness in DCM. Results suggested that the titin-isoform shift in DCM depresses the proportion of titin-based stiffness by approximately 10%. We conclude that a lower-than-normal proportion of titin-based stiffness in end-stage failing hearts results partly from loss of titin and increased fibrosis, partly from titin-isoform shift. The titin-isoform shift may be beneficial for myocardial diastolic function, but could impair the contractile performance in systole.
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