Destabilization of the Ca2+-ATPase of sarcoplasmic reticulum by thiol- specific, heat shock inducers results in thermal denaturation at 37 °C

Biochemistry

Volumn 36, Issue 36, 1997, Pages 11002-11011

  Senisterra, Guillermo A ^a   Huntley, Steven A ^b   Escaravage, Michel ^a   Sekhar, Konjeti R ^c   Freeman, Michael L ^c   Borrelli, Michael ^d   Lepock, James R ^a,b  

^a Waterloo Campus   (Canada)

^b UNIVERSITY OF WATERLOO   (Canada)

^c VANDERBILT UNIVERSITY MEDICAL CENTER   (United States)

^d WILLIAM BEAUMONT HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ADENOSINE TRIPHOSPHATASE (CALCIUM); ARSENIC TRIOXIDE; DIAMIDE; HEAT SHOCK PROTEIN; N ETHYLMALEIMIDE; THIOL DERIVATIVE; ARSENOUS ACID DERIVATIVE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME INDUCTION; ENZYME STABILITY; ERYTHROCYTE; HEAT SHOCK RESPONSE; HEAT TOLERANCE; HUMAN; HUMAN CELL; HYDROPHOBICITY; LIGHT SCATTERING; NONHUMAN; NORTHERN BLOTTING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; RABBIT; SARCOPLASMIC RETICULUM; TEMPERATURE; ANIMAL; CHEMISTRY; ENZYMOLOGY; HEAT; METABOLISM; PROTEIN DENATURATION; SKELETAL MUSCLE; ULTRASTRUCTURE;

ANIMALS; ARSENITES; CALCIUM-TRANSPORTING ATPASES; DIAMIDE; HEAT; MUSCLE, SKELETAL; PROTEIN DENATURATION; RABBITS; SARCOPLASMIC RETICULUM; SULFHYDRYL COMPOUNDS;

EID: 0030610918     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9711590     Document Type: Article

References (37)

1. Ananthan, J., Goldberg, A. L., & Voellmy, R. (1986) Science 232, 522-524.
2. Ariki, M., & Shamoo, A. E. (1983) Biochim. Biophys. Acta 734, 83-90.
3. Baler, R., Zou, J., & Voellmy, R. (1996) Cell Stress and Chaperones 1, 33-39.
4. Becker, P. S., Cohen, C. M., & Lux, S. E. (1986) J. Biol. Chem. 261, 4620-4628.
5. Birmachu, W., Nisswandt, F., & Thomas, D. (1989) Biochemistry 28, 3940-3947.
6. Brandl, C. J., Green, N. M., Korczak, B., & MacLennan, D. H. (1986) Cell 44, 597-607.
7. Campbell, K. P., Franzini-Armstrong, C., & Shamoo, A. E. (1980) Biochim. Biophys. Acta 602, 97-105.
8. Cardamone, M., & Puri, N. (1992) Biochem. J. 282, 589-593.
9. Chen, Q., Yu, K., & Stevens, J. L. (1992) J. Biol. Chem. 267, 24322-24327.
10. Eletr, S., & Inesi, B. (1972) Biochim. Biophys. Acta 282, 174-179.
11. Freeman, M. L., Sierra-Rivera, E., Voorhees, G. J., Eisert, D. R., & Meredith, M. J. (1993) Radiat. Res. 135, 387-393.
12. Freeman, M. L., Borrelli, M. J., Syed, K., Senisterra, G. A., Stafford, D. M. & Lepock, J. R. (1995) J. Cell. Physiol. 164, 356-366.
13. Goff, S. A., & Goldberg, A. L. (1985) Cell 41, 587-595.
14. Gross, M., & Rabinovitz, M. (1973) Biochem. Biophys. Res. Commun. 50, 832-838.
15. Haest, C. W. M., Kamp, D., Plaza, G., & Deuticke, B. (1977) Biochim. Biophys. Acta 469, 226-230.
16. Hightower, L. E., & White, F. P. (1981) J. Cell. Physiol. 108, 261-275.
17. Hightower, L. E., Guidon, P. T., Whelan, S. A., & White, C. N. (1985) in Changes in Eukaryotic Gene Expressions in Response to Environmental Stress (Atkinson, B. G., & Walden, D. B., Eds.) pp 369-377, Academic Press, Orlando, FL.
18. Janatova, J., Fuller, J. K., & Hunter, J. (1968) J. Biol. Chem. 243, 3612-3622.
19. Kawakita, M., & Yamashita, T. (1987) J. Biochem. 102, 103-109.
20. Kono, M., Sen, A. C., & Chakrabarti, B. (1990) Biochemistry 29, 464-470.
21. Lepock, J. R., Frey, H. E., Bayne, H., & Markus, J. (1989) Biochim. Biophys. Acta 980, 191-201.
22. Lepock, J. R., Rodahl, M., Zhang, C. H., Heynen, M., Waters, B., & Cheng, K. (1990) Biochemistry 29, 681-689.
23. Lepock, J. R., Ritchie, K. P., Kolios, M. L., Rodahl, A. M., Heinz, K. A., & Kruuv, J. (1992) Biochemistry 31, 12706-12712.
24. Lepock, J. R., Frey, H. E., & Ritchie, K. P. (1993) J. Cell Biol. 122, 1267-1276.
25. Levinson, W., Oppermann, U., & Jackson, J. (1980) Biochim. Biophys. Acta 606, 170-180.
26. Liu, R. Y., Kim, D., Yang, S. H., & Li, G. C. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 3078-3082.
27. Lysko, K., Carlson, R., Taverna, R., Snow, W., & Brandts, J. F. (1981) Biochemistry 20, 5570-5576.
28. McDuffee, A. T., Senisterra, G., Huntley, S., Lepock, J. R., Sekhar, M. J., Meredith, M. J., Borrelli, M. J., Morrow, J. D., & Freeman, M. L. (1997) J. Cell. Physiol. 171, 143-151.
29. Mifflin, L., & Cohen, R. (1994) J. Biol. Chem. 267, 15710-15717.
30. Morimoto, R. I., Jurivich, D. A., Kroeger, P. E., Mathur, S. K., Murphy, S. P., Nakai, A., Sarge, K., Abravaya, K., & Sistonen, L. T. (1994) in The Biology of Heat Shock Proteins and Molecular Chaperones ;(Morimoto, R. I., Tissieres, A., & Georgopoulos, C., Eds.) pp 417-455, Cold Spring Harbor Laboratory Press, Plainview, NY.
31. Nover, L., Scharf, D. K., & Neumann, D. (1989) Mol. Cell. Biol. 9, 1298-1308.
32. Pahl, H. L., & Baeuerle, P. A. (1996) FEBS Lett. 392, 129-136.
33. Privalov, P. L. (1979) Adv. Protein Chem. 33, 167-241.
34. Ptitsyn, O. B. (1992) The Molten Globule. In Protein Folding (Creighton, T. E., Ed.) pp 243-300, W. H. Freeman and Company, New York.
35. Stefanova, H. I., East, J. M., Gore, M. G., & Lee, A. G. (1992) Biochemistry 31, 6023-6031.
36. Torchinsky, Y. M. (1981) Sulfur in Proteins, pp 46-48, Pergamon Press, Toronto.
37. Zuo, J. R., Rungger, D., & Voellmy, R. (1995) Mol. Cell. Biol. 15, 4319-4430.