| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1976178 | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | 2007 | 6 Pages |
We have compared ubiquitous calpains in chicken (Gallus gallus), turkey (Meleagris gallopavo) and mammals. In chicken, we studied their distribution in different tissues. The calpain activity was determined by casein zymography, a technique avoiding any prior sample purification, thus limiting any autolysis and denaturation reactions. Our results show that two ubiquitous calpains are present in chicken: (1) a μ-calpain having a greater calcium sensitivity and a lower electrophoretic mobility than the mammalian one, (2) a μ/m-calpain, named like this by Sorimachi et al. [Sorimachi, H., Tsukahara, T., Okada-Ban, M., Sugita, H., Ishiura, S., Suzuki, K., 1995. Identification of a third ubiquitous calpain species—chicken muscle expresses four distinct calpains. Biochim. Biophys. Acta, 1261, 381–93.], having a calcium sensitivity intermediate between that of the two mammalian μ-calpain and the m-calpain. Tissue distribution of the two chicken isozymes vary and μ/m-calpain predominates, whereas μ-calpain levels are very low in some tissues, unlike in mammalian tissues. The characteristics of μ/m-calpain and its preponderance in all organs suggest that it may play a different role in chicken than in mammals.
