Effects of missense mutations Phe110Ile and Glu244Asp in human cardiac troponin T on force generation in skinned cardiac muscle fibers

Journal of Biochemistry

Volumn 126, Issue 3, 1999, Pages 457-460

  Nakaura, Hiroyuki ^a,b   Yanaga, Fumi ^a   Ohtsuki, Iwao ^a   Morimoto, Sachio ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Calcium sensitivity; Familial hypertrophic cardiomyopathy; Force; Skinned fiber; Troponin

Indexed keywords

CALCIUM ION; MUTANT PROTEIN; TROPONIN T;

AMINO ACID SUBSTITUTION; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; HEART MUSCLE CELL; HUMAN; HYPERTROPHIC CARDIOMYOPATHY; MISSENSE MUTATION; MUSCLE FORCE; NONHUMAN; RABBIT; SKINNED MUSCLE FIBER; STRUCTURE ACTIVITY RELATION;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0032824580     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022473     Document Type: Article

References (17)

1. Ebashi, S. and Endo, M. (1968) Calcium ion and muscle contraction. Prog. Biophys. Mol. Biol. 18, 123-183
2. Ohtsuki, I., Maruyama, K., and Ebashi, S. (1986) Regulatory and cytoskeletal proteins of vertebrate skeletal muscle. Adv. Protein Chem. 38, 1-67
3. Perry, S.V. (1998) Troponin T: genetics, properties and function. J. Muscle Res. Cell Motil. 19, 575-602
4. 2+-sensitizing effects of the mutations at Ile-79 and Arg-92 of troponin T in hypertrophic cardiomyopathy. Am. J. Physiol. 275 (Cell Physiol. 44), C200-C207
5. Morimoto, S., Nakaura, H., Yanaga, F., and Ohtsuki, I. (1999) Functional consequences of a carboxyl terminal missense mutation Arg278Cys in human cardiac troponin T. Biochem. Biophys. Res. Commun. 261, 79-82
6. Nakaura, H., Morimoto, S., Yanaga, F., Nakata, M., Nishi, H., Imaizumi, T., and Ohtsuki, I. (1999) Functional changes in troponin T by a splice donor site mutation that causes hypertrophic cardiomyopathy. Am. J. Physiol. 277 (Cell Physiol. 46), C225-C232
7. 2+ sensitization and potentiation of the maximum level of myofibrillar ATPase activity caused by mutations of troponin T found in familial hypertrophic cardiomyopathy. J. Biol. Chem. 274, 8806-8812
8. Horton, R.M. (1993) In vitro recombination and mutagenesis of DNA. Method Mol. Biol. 15, 251-261
9. Hatakenaka, M. and Ohtsuki, I. (1991) Replacement of three troponin components with cardiac troponin components within single glycerinated skeletal muscle fibers. Biochem. Biophys. Res. Commun. 181, 1022-1027
10. 2+-activated tension development of single glycerinated rabbit skeletal muscle fibers. Eur. J. Biochem. 205, 985-993
11. 2+-sensitivity of the ATPase activity of rabbit skeletal myofibrils: effect of the complete substitution of troponin C with cardiac troponin C, calmodulin, and parvalbumins. J. Biochem. 101, 291-301
12. Watkins, H., McKenna, W.J., Thierfelder, L., Suk, H.J., Anan, R., O'Donoghue, A., Spirito, P., Matsumori, A., Moravec, C.S., Seidman, J.G., and Seidman, C.E. (1995) Mutations in the genes for cardiac troponin T and α-tropomyosin in hypertrophic cardiomyopathy. N. Engl. J. Med. 332, 1058-1064
13. Anan, R., Shono, H., Kisanuki, A., Arima, S., Nakao, S., and Tanaka, H. (1998) Patients with familial hypertrophic cardiomyopathy caused by a Phe110Ile missense mutation in the cardiac troponin T gene have variable cardiac morphologies and a favorable prognosis. Circulation 98, 391-397
14. Rüegg, J.C. (1986) Calcium in Muscle Activation, Springer-Verlag, Berlin and Tokyo
15. Tanokura, M., Tawada, Y., Ono, A., and Ohtsuki, I. (1983) Chymotryptic subfragments of troponin T from rabbit skeletal muscle. Interaction with tropomyosin, troponin I and troponin C. J. Biochem. 93, 331-337
16. 2+ in the presence of troponin-C. J. Biol. Chem. 257, 10587-10592
17. Morimoto, S., Harada, K., and Ohtsuki, I. (1999) Roles of troponin isoforms in pH dependence of contraction in rabbit fast and slow skeletal and cardiac muscles. J. Biochem. 126, 121-129