期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 601, 期 -, 页码 88-96出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2016.02.023
关键词
Heart; Troponin I; Mammalian two-hybrid; In vitro motility assay; Unloaded filament sliding; Calcium
资金
- Hellman Fellowship
- NIH/NHLBI [HL63974, HL096819]
The C-terminal region of cardiac troponin I (cTnI) is known to be important in cardiac function, as removal of the last 17 C-terminal residues of human cTnI has been associated with myocardial stunning. To investigate the C-terminal region of cTnl, three C-terminal deletion mutations in human cTnl were generated: Delta 1 (deletion of residue 210), Delta 3 (deletion of residues 208-210), and Delta 5 (deletion of residues 206-210). Mammalian two-hybrid studies showed that the interactions between cTnl mutants and cardiac troponin C (cTnC) or cardiac troponin T (cTnT) were impaired in Delta 3 and Delta 5 mutants when compared to wild-type cTnl. Troponin complexes containing 2-[4'-(iodoacetamido) anilinol naphthalene-6-sulfonic acid (IAANS) labeled cTnC showed that the troponin complex containing cTnI Delta 5 had a small increase in Ca2+ affinity (P < 0.05); while the cTnl Delta 1- and Delta 3 troponin complexes showed no difference in Ca2+ affinity when compared to wild-type troponin. In vitro motility assays showed that all truncation mutants had increased Ca2+ dependent motility relative to wild-type cTnI. These results suggest that the last 5 C-terminal residues of cTnI influence the binding of cTnl with cTnC and cTnT and affect the Ca2+ dependence of filament sliding, and demonstrate the importance of this region of cTnI. (C) 2016 Elsevier Inc. All rights reserved.
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