Functional analysis of rat acidic calponin

Biological and Pharmaceutical Bulletin

Volumn 25, Issue 5, 2002, Pages 573-579

  Fujii, Toshihiro ^a   Yabe, Sachiko ^a   Nakamura, Kouta ^a   Koizumi, Youichi ^a  

^a SHINSHU UNIVERSITY   (Japan)

Author keywords

Acidic calponin; Actin; Cytoskeleton; Limited digestion; Phosphatidylserine

Indexed keywords

ADENOSINE TRIPHOSPHATASE (MAGNESIUM); CALPONIN; F ACTIN; MYOSIN ADENOSINE TRIPHOSPHATASE; PROTEINASE; RECOMBINANT PROTEIN; ACTIN; ACTIN BINDING PROTEIN; ADENOSINE TRIPHOSPHATASE (CALCIUM MAGNESIUM); CALCIUM BINDING PROTEIN; COMPLEMENTARY DNA; CROSS LINKING REAGENT; PHOSPHATIDYLSERINE;

ACIDITY; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CROSS LINKING; FLUORESCENCE ANALYSIS; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RAT; STRUCTURE ANALYSIS; ANIMAL; BINDING SITE; CHEMISTRY; CIRCULAR DICHROISM; ELECTRON MICROSCOPY; GENETICS; HYDROLYSIS; MASS SPECTROMETRY; METABOLISM; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; WISTAR RAT;

ACTINS; ANIMALS; BINDING SITES; CA(2+) MG(2+)-ATPASE; CALCIUM-BINDING PROTEINS; CIRCULAR DICHROISM; CROSS-LINKING REAGENTS; DNA, COMPLEMENTARY; HYDROLYSIS; MICROFILAMENT PROTEINS; MICROSCOPY, ELECTRON; PHOSPHATIDYLSERINES; PROTEIN BINDING; RATS; RATS, WISTAR; RECOMBINANT PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 0036583885     PISSN: 09186158     EISSN: None     Source Type: Journal    
DOI: 10.1248/bpb.25.573     Document Type: Article

References (45)

1. Takahashi K., Hiwada K., Kokubu T., Biochem. Biophys. Res. Commun., 141, 20-26 (1986).
2. Abe M., Takahashi K., Hiwada K., J. Biochem. (Tokyo), 108, 835-838 (1990).
3. Winder S. J., Walsh M. P., J. Biol. Chem., 265, 10148-10155 (1990).
4. Makuch R., Birukov K., Shirinsky V., Dabrowska R., Biochem. J., 280, 33-38 (1991).
5. Winder S. J., Walsh M. P., Vasulka C., Johnson J. D., Biochemistry, 32, 13327-13333 (1993).
6. Kolakowski J., Makuch R., Stepkowski D., Dabrowska R., Biochem. J., 306, 199-204 (1995).
7. Takahashi K., Nadal-Ginard B., J. Biol. Chem., 266, 13284-13288 (1991).
8. Strasser P., Gimona M., Moessler H., Herzog M., Small J. V., FEBS Lett., 330, 13-18 (1993).
9. Applegate D., Feng W., Green R. S., Taubman M. B., J. Biol. Chem., 269, 10683-10690 (1994).
10. Maguchi M., Nishida W., Kohara K., Kuwano A., Kondo I., Hiwada K., Biochem. Biophys. Res. Commun., 217, 238-244 (1995).
11. Masuda H., Tanaka K., Takagi M., Ohgami K., Sakamaki T., Shibata N., Takahashi K., J. Biochem. (Tokyo), 120, 415-424 (1996).
12. Gimona M., Mital R., J. Cell Sci., 111, 1813-1821 (1998).
13. Trabelsi-Terzidis H., Fattoum A., Represa A., Dessi F., Ben-Ari Y., der Terrossian E., Biochem. J., 306, 211-215 (1995).
14. Plantier M., Fattoum A., Menn B., Ben-Ari Y., der Terrossian E., Represa A., Eur. J. Neurosci., 11, 2801-2812 (1999).
15. Takahashi K., Abe M., Hiwada K., Kokubu T., J. Hypertension, 6, S40-S43 (1988).
16. Fujii T., Chem. Pharm. Bull. 39, 2622-2626 (1991).
17. Szymanski P. T., Tao T., FEBS Lett., 334, 379-382 (1993).
18. Szymanski P. T., Goyal R. K., Biochemistry, 38, 3778-3784 (1999).
19. Wang P., Gusev N. B., FEBS Lett., 392, 255-258 (1996).
20. Mabuchi K., Li B., Ip W., Tao T., J. Biol. Chem., 272, 22662-22666 (1997).
21. Fujii T., Takagi H., Arimoto M., Ootani H., Ueeda T., J. Biochem. (Tokyo), 127, 457-465 (2000).
22. Fujii T., Hiromori T., Hamamoto M., Suzuki T., J. Biochem. (Tokyo), 122, 344-351 (1997).
23. Fujii T., Koizumi Y., J. Biochem. (Tokyo), 125, 869-875 (1999).
24. Fujii T., Oomatsuzawa A., Kuzumaki N., Kondo Y., J. Biochem. (Tokyo), 116, 121-127 (1994).
25. Bogatcheva N. V., Ma Y., Urosev D., Gusev N. B., FEBS Lett., 457, 369-374 (1999).
26. Leinweber B. D., Leavis P. C., Grabarek Z., Wang C.-L. A., Morgan K. G., Biochem. J., 344, 117-123 (1999).
27. Fujii T., Yamana K., Ogoma Y., Kondo Y., J. Biochem. (Tokyo), 117, 999-1003 (1995).
28. Bogatcheva N. V., Gusev N. B., FEBS Lett., 371, 123-126 (1995).
29. Fujii T., Ozawa J., Ogoma Y., Kondo Y., J. Biochem. (Tokyo), 104, 734-737 (1988).
30. Laemmli U. K., Nature (London), 227, 680-685 (1970).
31. Kouyama T., Mihashi T., Eur. J. Biochem., 114, 33-38 (1981).
32. Cooper J. A., Walker S. B., Pollard T. D., J. Muscle. Res. Cell Motil., 4. 253-262 (1983).
33. Stafford W. F., Mabuchi K., Takahashi K., Tao T., J. Biol. Chem., 270, 10576-10579 (1995).
34. Lu F. W. M., Freedman M. V., Chalovich J. M., Biochemistry, 34, 11864-11871 (1995).
35. Yoshimoto R., Hori M., Ozaki H., Karaki H., J. Biochem. (Tokyo), 128, 1045-1049 (2000).
36. Tang J. X., Szymanski P. T., Janmey P. A., Tao T., Eur. J. Biochem., 247, 432-440 (1997).
37. Bonet-Kerrache A., Mornet D., Biochem. Biophys. Res. Commun., 206, 127-132 (1995).
38. Elzinga M., Collins J. H., Kuehl W. M., Adelstein R. S., Proc. Natl. Acad. Sci. U.S.A., 70, 2684-2691 (1973).
39. Winder S. J., Kargacin G. J., Bonet-Kerrache A. A., Pato M. D., Walsh M. P., Jpn. J. Plarmacol., 58, 29P-34P (1992).
40. Mezgueldi M., Fattoum A., Derancourt J., Kassab R., J. Biol. Chem., 267, 15943-15951 (1992).
41. Mornet D., Ue K., Proc. Natl. Acad. Sci. U.S.A., 81, 3680-3684 (1984).
42. Noda S., Ito M., Watanabe S., Takahashi K., Maruyama K., Biochem. Biophys. Res. Commun., 185, 481-187 (1992).
43. Nakamura F., Mino T., Yamamoto J., Naka M., Tanaka T., J. Biol. Chem., 268, 6194-6201 (1993).
44. EL-Mezgueldi M., Mendre C., Calas B., Kassab R., Fattoum A., J. Biol. Chem., 270, 8867-8876 (1995).
45. EL-Mezgueldi M., Int. J. Biochem. Cell Biol., 28, 1185-1189 (1996).