Hypertrophy of colonic smooth muscle: Contractile proteins, shortening velocity, and regulation

American Journal of Physiology - Gastrointestinal and Liver Physiology

Volumn 272, Issue 6 35-6, 1997, Pages

  Siegman, Marion J ^a   Butler, Thomas M ^a   Mooers, Susan U ^a   Trinkle Mulcahy, Laura ^a   Narayan, Srinivasa ^a   Adam, Len ^b   Chacko, Samuel ^c   Haase, Hannelore ^d   Morano, Ingo ^d  

^a THOMAS JEFFERSON UNIVERSITY   (United States)

^b BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

Author keywords

Actin; Isoforms; myosin; Myosin light chain phosphorylation; Thiophosphorylation

Indexed keywords

CONTRACTILE PROTEIN; MYOSIN LIGHT CHAIN;

ACTIN FILAMENT; ADAPTATION; ALTERNATIVE RNA SPLICING; AMINO ACID COMPOSITION; ANIMAL TISSUE; ARTICLE; AUTOPHOSPHORYLATION; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE PERMEABILITY; COLON MUCOSA; MOUSE; MUSCLE HYPERTROPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONTENT;

EID: 0030753132     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.1997.272.6.g1571     Document Type: Article

References (43)

1. Brann, L., and J. D. Wood. Motility of the large intestine of piebald lethal mice. Dig. Dis. 21: 633-640, 1976.
2. Butler, T. M., and M. J. Siegman. Chemical energy usage and myosin light chain phosphorylation in mammalian smooth muscle. Federation Proc. 42: 57-61, 1983.
3. Calovini, T., H. Haase, and I. Morano. Steroid-hormone regulation of myosin subunit expression in smooth and cardiac muscle. J. Cell. Biochem. 59: 69-78, 1995.
4. Dillon, D. F., M. O. Aksoy, S. P. Driska, and R. A. Murphy. Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle. Science 211: 495-497, 1981.
5. Eddinger, T. J., and R. A. Murphy. Developmental changes in actin and myosin heavy chain isoform expression in smooth muscle. Arch. Biochem. Biophys. 284: 232-237, 1991.
6. Eddinger, T. J., and J. A. Wolf. Expression of four myosin heavy chain isoforms with development in mouse uterus. Cell Motil. Cytoskeleton 25: 358-368, 1993.
7. Edman, K. A. P. The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibers. J. Physiol. (Lond.) 291: 143-159, 1979.
8. Fatigati, V., and R. A. Murphy. Actin and tropomyosin variants in smooth muscles. J. Biol. Chem. 259: 14383-14388, 1984.
9. Haase, H., and I. Morano. Alternative splicing of smooth muscle myosin heavy chains and its functional consequences. J. Cell. Biochem. 60: 521-528, 1996.
10. Haeberle, J. R., S. A. Coolican, A. Evan, and D. R. Hathaway. The effects of a calcium dependent protease on the ultrastructure and contractile mechanics of skinned uterine smooth muscle. J. Muscle Res. Cell Motil. 6: 347-363, 1985.
11. Hai, C. M., and R. A. Murphy. Cross-bridge dephosphorylation and relaxation of vascular smooth muscle. Am. J. Physiol. 256 (Cell Physiol. 25): C282-C287, 1989.
12. Hamada, Y., M. Yanagisawa, Y. Katsuragawa, J. R. Coleman, S. Nagata, G. Matsuda, and T. Masaki. Distinct vascular and intestinal smooth muscle myosin heavy chain mRNAs are encoded by a single-copy gene in the chicken. Biochem. Biophys. Res. Commun. 170: 53-58, 1990.
13. Helper, D. J., J. A. Lash, and D. R. Hathaway. Distribution of isoelectric variants of the 17,000 Dalton myosin light chain in mammalian smooth muscle. J. Biol. Chem. 263: 5748-5753, 1988.
14. Hewett, T. E., A. F. Martin, and R. J. Paul. Correlations between myosin heavy chain isoforms and mechanical parameters in rat myometrium. J. Physiol. (Lond.) 460: 351-364, 1993.
15. Katoh, Y., and P. Periasamy. Growth and differentiation of smooth muscle cells during vascular development. Trends Cardiovasc. Med. 6: 100-106, 1996.
16. Kawamoto, S., and R. S. Adelstein. Characterization of myosin heavy chains in cultured aorta smooth muscle cells: a comparative study. J. Biol. Chem. 262: 7282-7288, 1987.
17. Kelley, C. A., M. Takahashi, J. H. Yu, and R. S. Adelstein. An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. J. Biol. Chem. 268: 12848-12854, 1993.
18. Kim, Y. S., Z. Wang, R. M. Levin, and S. Chacko. Alterations in the expression of the β-cytoplasmic and the γ-smooth muscle actins in hypertrophied urinary bladder smooth muscle. Mol. Cell. Biochem. 131: 115-124, 1994.
19. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T. Nature 227: 680-685, 1996.
20. Liddell, R. A., S. U. Mooers, M. J. Siegman, and K. M. McHugh. Altered isoactin gene expression in the affected bowel segments of the lethal spotted mouse. Gastroenterology 105: 441-448, 1993.
21. Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193: 265-275, 1951.
22. Malmqvist, U., and A. Arner. Isoform distribution and tissue contents of contractile and cytoskeletal proteins in hypertrophied smooth muscle from rat portal vein. Circ. Res. 66: 832-845, 1990.
23. Malmqvist, U., and A. Arner. Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle. Pflügers Arch. 418: 523-530, 1991.
24. Merril, C. R., D. Goldman, S. A. Sedman, and M. H. Ebert. Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science 211: 1437-1438, 1981.
25. Morano, I., G. Erb, and B. Sogl. Expression of myosin heavy and light chains changes during pregnancy in the rat uterus. Pflügers Arch. 423: 434-441, 1993.
26. Nagai, R., M. Kuroo, P. Babij, and M. Periasamy. Identification of two types of smooth muscle myosin heavy chain isoforms by cDNA cloning and immunoblot analysis. J. Biol. Chem. 264: 9734-9737, 1989.
27. O'Farrell, P. H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021, 1975.
28. Porzio, M. A., and A. M. Pearson. Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochim. Biophys. Acta 490: 27-34, 1977.
29. Rovner, A. S., M. M. Thompson, and R. A. Murphy. Two different heavy chains are found in smooth muscle myosin. Am. J. Physiol. 250 (Cell Physiol. 19): C861-C870, 1986.
30. Siegman, M. J., T. M. Butler, and S. U. Mooers. Phosphatase inhibition with okadaic acid does not alter the relationship between force and myosin light chain phosphorylation in permeabilized smooth muscle. Biochem. Biophys. Res. Commun. 161: 838-842, 1989.
31. Siegman, M. J., T. M. Butler, S. U. Mooers, and R. E. Davies. Chemical energetics of force development, force maintenance, and relaxation in mammalian smooth muscle. J. Gen. Physiol. 76: 609-629, 1980.
32. max without changes in myosin light chain phosphorylation in smooth muscle. Pflügers Arch. 401: 385-389, 1984.
33. Siegman, M. J., T. M. Butler, S. U. Mooers, L. Trinkle-Mulcahy, S. Narayan, W. S. Stirewalt, and B. C. Starcher. Hypertrophy of colonic smooth muscle: structural remodeling, chemical composition, and force output. Am. J. Physiol. 273 (Gastrointest. Liver Physiol. 36): G1560-G1570, 1997.
34. Somlyo, A. P. Myosin isoforms in smooth muscle: how they may affect function and structure. J. Muscle Res. Cell Motil. 14: 557-563, 1993.
35. Somlyo, A. V., Y. E. Goldman, T. Fujimori, M. Bond, D. R. Trentham, and A. P. Somlyo. Crossbridge kinetics, cooperativity, and negatively strained crossbridges in vertebrate smooth muscle. J. Gen. Physiol. 91: 165-192, 1988.
36. Sparrow, M. P., M. A. Mohammad, A. Arner, P. Hellstrand, and J. C. Ruegg. Myosin composition and functional properties of smooth muscle from the uterus of pregnant and nonpregnant rats. Pflügers Arch. 412: 624-633, 1988.
37. Stephenson, D. G., and D. A. Williams. Calcium-activated force responses in fast and slow-twitch skinned muscle fibres of the rat at different temperatures. J. Physiol. (Lond.) 317: 281-302, 1981.
38. Upadhya, A., M. Samuel, R. H. Cox, R. J. Bagshaw, and S. Chacko. Characteristics of arterial myosin in experimental renal hypertension in the dog. Hypertension 21: 624-631, 1993.
39. Vyas, T. B., S. U. Mooers, S. R. Narayan, M. J. Siegman, and T. M. Butler. Crossbridge cycling at rest and during activation: turnover of myosin-bound ADP in permeabilized smooth muscle. J. Biol. Chem. 269: 7316-7322, 1994.
40. Vyas, T. B., S. U. Mooers, S. R. Narayan, J. C. Witherell, M. J. Siegman, and T. M. Butler. Cooperative activation of myosin by light chain phosphorylation in permeabilized smooth muscle. Am. J. Physiol. 263 (Cell Physiol. 32): C210-C219, 1992.
41. Wang, C. S., and R. L. Smith. Lowry determination of proteins in the presence of Triton X-100. Anal. Biochem. 63: 414-417, 1975.
42. White, S., A. F. Martin, and M. Periasamy. Identification of a novel smooth muscle myosin heavy chain cDNA: isoform diversity in the S1 head region. Am. J. Physiol. 264 (Cell Physiol. 33): C1252-C1258, 1993.
43. Wood, J. D., and H. J. Cooke. Murine models for congenital megacolon: Hirschsprung's disease. In: Animal Models for Intestinal Disease, edited by C. J. Pfeiffer. Boca Raton, FL: CRC, 1985, p. 181-195.