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      Polymorphisms of the CAST gene in the Meishan and five other pig populations in China

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          Abstract

          The aim of the study was to characterize the polymorphism of the Calpastatin (CAST) gene identified with three restriction enzymes (TaqI, HinfI, MspI) in Meishan and five other pig populations, and to provide information on their potential in marker-assisted selection and conservation. Meishan pigs appeared to be monomorphic at loci CAST/HinfIand CAST/MspI. A high frequency of the favoured genotype, FF, in terms of meat quality was detected in Meishan pigs, a breed well known for high quality meat. However, the frequency of the genotype, FF, was very low in Sutai pigs, a breed developed from a Duroc (50%) * Meishan (50%) cross. This is probably partially due to the fact that genetic improvement in this breed was achieved through the use of traditional quantitative genetics. It is suggested that traditional selection techniques combined with the use of the polymorphisms discovered have an important potential to improve overall meat quality.

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          Most cited references14

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          Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses.

          Postmortem proteolysis in skeletal muscle and factors affecting this process were examined in pork, lamb and beef longissimus muscles (LM) to determine the cause of differences in meat tenderness among these species. Fat thickness differed among species in the following order: pork greater than beef greater than lamb. The following patterns were observed for rate of temperature and pH decline: lamb greater than pork greater than beef and pork greater than beef greater than lamb, respectively. At 1 d postmortem, pork was the most tender, followed by beef and lamb, respectively. Between 1 and 14 d of postmortem storage, lamb LM was the most improved in tenderness, followed by beef and pork, respectively. Species did not differ (P greater than .05) in LM collagen solubility. Pork LM from fed pigs had the highest (P less than .05) level of cathepsins B + L and cystatin(s) activities, whereas no differences (P greater than .05) were observed among the species for cathepsin B activity. The lowest (P less than .01) Ca2(+)-dependent protease (CDP)-II and CDP inhibitor activities were observed in pork LM. Beef LM had the highest CDP inhibitor activity (P less than .05) but was intermediate in CDP-II activity. No differences were observed among species for CDP-I activity. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of myofibrils isolated at 0, 1 and 14 d postmortem indicated that by d 1, desmin hydrolysis was most extensive in pork muscle, followed by lamb and beef.(ABSTRACT TRUNCATED AT 250 WORDS)
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            Intracellular Ca2+-dependent protease (CALPAIN) and its high-molecular-weight endogenous inhibitor (CALPASTATIN)

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              Effects of cimaterol on rabbit growth and myofibrillar protein degradation and on calcium-dependent proteinase and calpastatin activities in skeletal muscle.

              The objectives of this study were to examine effects of a beta-adrenergic agonist (cimaterol) on growth and muscle development in rabbits and to examine cimaterol's effects on myofibrillar protein degradation (MPD) and on activities of several proteolytic enzymes including the calcium-dependent proteinases (CDP). Twelve New Zealand White rabbits were assigned to either control diets or to diets containing cimaterol for 35 d, after which they were killed and effects on performance and tissue weight gains were determined. Urine was collected from d 21 through 28 from each rabbit for assessment of N tau-methylhistidine (NMH) excretion. Cimaterol increased rates of gain, efficiency of gain and skeletal muscle weights. Enhancement in muscle weight was associated with an increase in total DNA and with a reduction in NMH. Cimaterol did not affect activities of cathepsin B, cathepsin D or neutral serine proteinase, but it reduced activities of the millimolar and micromolar forms of the CDP by 58 and 57%, respectively, and it reduced activity of the inhibitor of the CDP (calpastatin) by 52%. Cimaterol-dependent myofibrillar protein accretion was likely mediated, at least in part, by a reduction in MPD. The change in MPD was associated with a reduction in muscle CDP activities. Cimaterol-dependent muscle hypertrophy therefore may involve changes in calcium-dependent proteolysis of myofibrillar proteins. The significance of the effects of cimaterol on calpastatin activity is not known.
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                Author and article information

                Journal
                sajas
                South African Journal of Animal Science
                S. Afr. j. anim. sci.
                The South African Society for Animal Science (SASAS) (Pretoria, Gauteng, South Africa )
                0375-1589
                2221-4062
                2007
                : 37
                : 1
                : 27-30
                Affiliations
                [01] Shanghai orgnameShanghai Jiaotong University orgdiv1School of Agriculture and Biology orgdiv2Department of Animal Science P.R. China
                [02] Shanghai orgnameShanghai Institute of Veterinary Hygienic P.R. China
                Article
                S0375-15892007000100004 S0375-1589(07)03700100004
                6267216e-6a4e-432d-a54c-8051cacc74d2

                This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

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                Figures: 0, Tables: 0, Equations: 0, References: 14, Pages: 4
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                SciELO South Africa

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                Polymorphism,CAST,Meishan,Sutai
                Polymorphism, CAST, Meishan, Sutai

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