Exchange of β- for α-tropomyosin in hearts of transgenic mice induces changes in thin filament response to Ca2+, strong cross-bridge binding, and protein phosphorylation

Journal of Biological Chemistry

Volumn 271, Issue 20, 1996, Pages 11611-11614

  Palmiter, Kimberly A ^a   Kitada, Yoshimi ^a   Muthuchamy, Mariappan ^b   Wieczorek, David F ^b   Solaro, R John ^a  

^a UNIVERSITY OF ILLINOIS   (United States)

^b UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA; MUS MUSCULUS;

CALCIUM ION; CYCLIC AMP; TROPOMYOSIN;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; GENE EXPRESSION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PHOSPHORYLATION; THIN FILAMENT; TRANSGENIC MOUSE;

ANIMALS; CALCIUM; MICE; MICE, TRANSGENIC; MICROFILAMENTS; MYOCARDIUM; PHOSPHORYLATION; PROTEINS; TROPOMYOSIN;

EID: 0029977762     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.20.11611     Document Type: Article

References (42)

1. Solaro, R. J., and Van Eyk, J. E. (1996) J. Mol. Cell. Cardiol. 28, 217-230
2. Lehrer, S. S. (1994) J Muscle Res. Cell Motil. 15, 232-236
3. Huxley, H. E. (1973) Cold Spring Harbor Symp. Quant. Biol. 37, 361-376
4. Hill, T. L., Eisenberg, E., and Greene, L. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 3186-3190
5. McKillop, D. F. A., and Geeves, M. A. (1993) Biophys. J. 65, 693-701
6. Bremel, R. D., Murray, J. M., and Weber, A. M. (1972) Cold Spring Harbor Symp. Quant. Biol. 37, 267-275
7. Popp, D., and Maeda, Y. (1993) J. Mol. Biol. 229, 279-285
8. O'Brien, E. J., Gillis, J. M., and Couch, J. (1975) J. Mol. Biol. 99, 461-475
9. Phillips, G. N., Jr., Fillers, J. P., and Cohen, C. (1986) J. Mol. Biol. 192, 111-131
10. Lehman, W., Craig, R., and Vilbert, P. (1994) Nature 368, 65-67
11. Chalovich, J. M., and Eisenberg, E. (1982) J. Biol. Chem. 257, 2432-2437
12. Cummins, P., and Perry, S. V. (1973) Biochem. J. 133, 765-777
13. Thomas, L. B., and Smillie, L. B. (1994) Biophys. J. 66, A310
14. Greenfield, N. J., Strafford, W. F., and Hitchcock-DeGregori, S. E. (1994) Protein Sci. 3, 402-410
15. Cho, Y.-J., Liu, J., and Hitchcock-DeGregori, S. E. (1990) J. Biol. Chem. 265, 538-545
16. Amphlett, G. W., Syska, H., and Perry, S. V. (1976) FEBS Lett. 63, 22-26
17. Moss, R. L. (1992) Circ. Res. 70, 865-884
18. Theirfelder, L., Watkins, H., MacRae, C., Lamas, R., McKenna, W., Vosberg, H., Seidman, J. G., and Seidman, C. E. (1994) Cell 77, 701-712
19. Nakajima-Taniguchi, C., Matsui, H., Nagata, S., Kishimoto, T., and YamauchiTakihara, J. (1995) J. Mol. Cell. Cardiol. 27, 2053-2058
20. Watkins, H., McKenna, W. J., Theirfelder, L., Suk, H. J., Anan, R., O'Donoghue, A., Spirito, P., Matsumori, A., Moravec, C. S., Seidman, J. G., and Seidman, C. E. (1995) N. Engl. J. Med. 332, 1058-1064
21. Muthuchamy, M., Grupp, I. L., Grupp, G., O'Toole, B. A., Kier, A. B., Boivin, G. P., Neumann, J., and Wieczorek, D. F. (1995) J. Biol. Chem. 270, 30593-30603
22. Palmiter, K. A., Kitada, Y., Muthuchamy, M., Wieczorek, D., and Solaro, R. J. (1995) Biophys. J. 68, 57 (abstr.)
23. Subramaniam, A., Jones, W. K., Gulick, J., Wert, S., Neumann, J., and Robbins, J. (1990) J. Biol. Chem. 266, 24613-24620
24. Laemmli, U. K. (1970) Nature 227, 680-685
25. Pagani, E. D., and Solaro, R. J. (1984) in Methods in Pharmacology (Schwartz, A., ed) pp. 44-61, Plenum Publishing Corp., New York
26. Towbin, H., Staehelin, T., and Gordon, J. (1979) Proc. Natl. Acad. Sci. U. S. A. 76, 4350-4354
27. Chiu, Y., Asayama, J., and Ford, L. E. (1982) Am. J. Physiol. 248, C299-C302
28. Godt, R. E., and Lindley, B. D. (1982) J. Gen. Physiol. 80, 279-297
29. Herzig, J. W., Kohler, G., Pfitzer, G., Ruegg, J. C., and Wolffle, G. (1981) Pfluegers Arch. Eur. J. Physiol. 391, 208-212
30. Lowry, D. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 165-175
31. Solaro, R. J., Moir, A. J. G., and Perry, S. V. (1976) Nature 262, 615-617
32. Guo, X., Wattanapermpool, J., Palmiter, K. A., Murphy, A. M., and Solaro, R. J. (1994) J. Biol. Chem. 269, 15210-15216
33. Pan, B.-S., Gordon, A. M., and Luo, Z. (1989) J. Biol. Chem. 264, 8495-8498
34. Iio, T. (1985) J. Biochem. (Tokyo) 98, 261-263
35. Tao, T., Gong, B., and Leavis, P. C. (1990) Science 2, 1339-1341
36. Strasburg, G. M., Leavis, P. C., and Gergely, J. (1985) J. Biol. Chem. 260, 366-370
37. Pearlstone, J. R., and Smillie, L. B. (1982) J. Biol. Chem. 257, 10587-10592
38. Al-Hillawi, E., Bhandari, D. G., Trayer, H. R., and Trayer, I. P. (1995) Eur. J. Biochem. 228, 962-970
39. Zhang, R., Zhao, J., Mandiveno, A., and Potter, J. D. (1995) Circ. Res. 76, 1028-1035
40. Durand, J.-B., Anchee, A. B., and Roberts, R. (1995) Ann. Med. 27, 311-317
41. Sweeny, H. L., Straceski, A. J., Leinwand, L. A., Tukunor, B. A., and Faust, L. (1994) J. Biol. Chem. 269, 1603-1605
42. Cuda, G., Fananapazir, L., Zhu, W., Sellers, J. R., and Epstein, N. D. (1993) J. Clin. Invest. 91, 2861-2865