Abstract
Calpain activity was determined by western blot analysis of steady-state concentrations ofm-calpain (calpain requiring millimolar Ca2 for activation) and also by northern blot analysis of steady-state concentrations of mRNA encodingm-calpain in three lines of quail: a random-bred control line (RR) and two lines selected for body weight, one for increased body weight (LL) and another for decreased body weight (SS). Them-calpain activities in skeletal muscle were higher in the SS line and lower in the LL line. From western blot analysis, enzyme levels of calpain were almost the same for all three lines. At the level of gene expression, the mRNA concentration encodingm-calpain was higher in the LL and lower in the SS line. These results suggest that the regulation of calpain activity in skeletal muscle is a three-step process, regulation at the transcription level, regulation at the enzyme level, and regulation of the activation of calpain.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Busch, W. A., Stromer, M. H., Goll, D. E., and Suzuki, A. (1972). Ca2-specific removal of Z lines from rabbit skeletal muscle.J. Cell Biol. 52367.
Goll, D. E., Kleese, W. C., and Szpacenko, A. (1989). In Campion, D. R., Hausman, G. J., and Martin, R. J. (eds.),Animal Growth Regulation Plenum Press, New York.
Inomata, M., Hayashi, M., Nakamura, M., Imahori, K., and Kawashima, S. (1983). Purification and characterization of a calcium-activated neutral protease from rabbit skeletal muscle which requires calcium ion of µM order concentration.J. Biochem. 93291.
Ishiura, S., Sugita, H., Nonaka, I., and Imahori, K. (1980). Calcium-activated neutral protease. Its localization in the myofibril, especially at the Z-band.J. Biochem. 87343.
Johari, S., Maeda, Y., Okamoto, S., and Hashiguchi, T. (1993). The comparison between broiler and layer in calpain calpastatin activities in skeletal muscle.Br. Poultry Sci. 34819.
Kar, N. C., and Pearson, C. M. (1976). A calcium-activated neutral protease in normal and dystrophic human muscle.Clin. Chim. Acta 73293.
Laemmli, U. K. (1970). Cleaveage of structural proteins during the assembly of the head of bacteriophage T4.Nature 227680.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with the follin phenol reagent.J. Biol. Chem. 193265.
Maeda, Y., Hayashi, K., Toyohara, S., and Hashiguchi, T. (1984). Variation among chicken stocks in the fractional rates of muscle protein synthesis and degradation.Biochem. Genet. 22687.
Maeda, Y., Hayashi, K., Hashiguchi, T., and Okamoto, S. (1986). Genetic studies on the muscle protein turnover rate ofCoturnix quail.Biochem. Genet. 24207.
Maeda, Y., Okamoto, S., Okano, K., Tomita, T., and Hashiguchi, T. (1990). The comparison of muscle protein turnover rate among the egg type, meat type and Japanese native chicken stocks.Jpn. J. Zootech. Sci. 61701.
Maeda, Y., Kawabe, K., Okamoto, S., Okamoto, S., and Hashiguchi, T. (1991). Genetical studies on muscle protein turnover rate and calcium activated neutral protease activity on the skeletal muscle of the Japanese quail,Coturnix coturnix japonica.Anim. Sci. Technol. (Jpn.) 62813.
Mayer, M., Anim, R., and Shafrir, E. (1976). Rat myofibrillar protease: Enzyme properties and adaptative changes in conditions of muscle protein degradation.Arch. Biochem. Biophys. 16120.
McDonald, R. J., Swift, G. H., Przybyla, A. E., and Chirgwin, J. M. (1987). Isolation of RNA using guanidinium salts.Methods Enzymol. 152219.
Ohno, S., Emori, Y., Imajoh, S., Kawasaki, H., Kisaragi, M., and Suzuki, K. (1984). Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?Nature 312566.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kawabe, K., Maeda, Y., Oka, T. et al. Different expression of calpain in skeletal muscle of Japanese quail (Coturnix coturnix japonica) lines selected for body weight. Biochem Genet 31, 485–495 (1993). https://doi.org/10.1007/BF02426880
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF02426880