title: μ-Calpain is involved in the postmortem proteolysis of gizzard smooth muscle.
abstract: Postmortem changes in proteins that have been implicated in affecting muscle integrity were examined in goose (GG) and duck (DG) gizzard smooth muscle stored at 5°C. GG and DG smooth muscles were sampled at 0, 1, 3 and 7 day of storage. The pH was approximately 7 in both GG and DG samples during postmortem storage. Casein zymograms showed that 0-day μ-calpain activity was higher (p<0.05) in GG than in DG samples. As postmortem time progressed, μ-calpain was activated and autolyzed more extensively in GG than in DG samples. However, μ/m-calpain remained relatively stable in both samples. Western blots indicated that postmortem desmin degradation was more rapid in GG than in DG samples. In contrast, α-actinin remained nearly unchanged in both samples. Therefore, our results suggest that μ-calpain has an important role in the postmortem proteolysis of gizzard smooth muscle.
authors.affiliation: Department of Animal Science, National Chiayi University, Chiayi City, Taiwan.
authors.forename: Ya-Shiou
authors.initials: YS
authors.lastname: Chang
authors.forename: Marvin H
authors.initials: MH
authors.lastname: Stromer
authors.forename: Rong-Ghi R
authors.initials: RG
authors.lastname: Chou
mesh_terms: D000185:Actinin / Q000378:metabolism; D000818:Animals; D030161:Avian Proteins / Q000378:metabolism*; D002154:Calpain / Q000378:metabolism*; D003893:Desmin / Q000378:metabolism; D004372:Ducks / Q000378:metabolism*; D005777:Geese / Q000378:metabolism*; D005895:Gizzard, Avian / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009130:Muscle, Smooth / Q000737:chemistry / Q000201:enzymology*; D011180:Postmortem Changes; D059748:Proteolysis
chemical_list: D030161:Avian Proteins; D003893:Desmin; D000185:Actinin; D002154:Calpain; C449002:mu-calpain