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• W2074998024 abstract "Mutations in the gene encoding human cardiac troponin T can cause familial hypertrophic cardiomyopathy, a disease that is characterized by ventricular hypertrophy and sudden, premature death. Troponin T is the tropomyosin-binding subunit of troponin required for thin filament regulation of contraction. One mutation, a change in the intron 15 splice donor site, results in two truncated forms of troponin T [Thierfelder et al. (1994) Cell 77, 701−712]. In one form, the mRNA skips exon 16 that encodes the C-terminal 14 amino acids; in the other, seven novel residues replace the exon 15- and 16-encoded C-terminal 28 amino acids. The two troponin T cDNAs were expressed in Escherichia coli for functional analysis. Both C-terminal deletion mutants formed a complex with cardiac troponin C and troponin I that exhibited the same concentration dependence as wild-type for regulation of the actomyosin MgATPase. However, both mutants showed severely reduced activation of the regulated actomyosin in the presence of Ca2+, though the inhibition in the absence of Ca2+ and the Ca2+-dependence of activation were not altered. The C-terminal deletions reduce the effectiveness of Ca2+-troponin to switch the thin filament from the “off” to the “on” state. Both mutant troponin Ts have reduced affinity for troponin I; the shorter mutant is at least 6-fold weaker than wild-type. The low level of activation of the ATPase would be consistent with reduced contractile performance, and the results suggest reduced troponin I affinity may be the molecular basis for the disease." @default.
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• W2074998024 date "1999-09-14" @default.
• W2074998024 modified "2023-10-18" @default.
• W2074998024 title "Altered Regulatory Function of Two Familial Hypertrophic Cardiomyopathy Troponin T Mutants" @default.
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• W2074998024 doi "https://doi.org/10.1021/bi9906120" @default.
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