Calpain specificity and expression in chicken tissues.
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 mu-calpain having a greater calcium sensitivity and a lower electrophoretic mobility than the mammalian one, (2) a mu/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 mu-calpain and the m-calpain. Tissue distribution of the two chicken isozymes vary and mu/m-calpain predominates, whereas mu-calpain levels are very low in some tissues, unlike in mammalian tissues. The characteristics of mu/m-calpain and its preponderance in all organs suggest that it may play a different role in chicken than in mammals.
Lee
Hsiao Lin
HL
Laboratoire de Génie Chimique et Biochimique, Unité Biochimie - CUST - Université Blaise Pascal, 63174 Aubière, France.
Santé-Lhoutellier
Veronique
V
Vigouroux
Sophie
S
Briand
Yves
Y
Briand
Mariele
M
D000818:Animals; D002154:Calpain / Q000096:biosynthesis* / Q000737:chemistry; D002417:Cattle; D002645:Chickens / Q000378:metabolism*; D015971:Gene Expression Regulation, Enzymologic / Q000502:physiology*; D007527:Isoenzymes / Q000096:biosynthesis; D009928:Organ Specificity / Q000502:physiology; D034421:Sus scrofa; D014422:Turkeys
D007527:Isoenzymes; D002154:Calpain