Study on the Apoptosis and Effect Facts of Duck Skeletal Muscle during Postmortem Ageing

doi:10.3969/j.issn.1000-7091.2012.05.036

Abstract

Abstract: This experiment investigate whether the duck skeletal muscle cells apoptosis occurs and what factors affect it and provide new experimental evidence for further use of the mechanism of apoptosis mature mechanism to clarify the water in poultry meat.Analysis detected after slaughter,the duck breast and thigh meat of Bcl-2,Bax in Caspase-3 protein expression and mitochondrial cytochrome-C content,TUNEL detect changes of the number of positive-apoptotic nuclei as well as post-mortem ATP metabolism and pH changes situation.The results showed that the duck skeletal muscle after slaughter Bax/Bcl-2 protein ratio were significantly raised(P0.05),mitochondrial cytochrome-C content was significantly lower(P0.05),Caspase-3 zymogen,respectively split into the activation of about 20 kDa fragment,0.5-8 h skeletal muscle after slaughter,the number of positive apoptotic nuclei were significantly increased(P0.05);content of ATP and pH value in the postmortem 0.5-8 h showed a significant downward trend(P0.05).The results of Bax pro-apoptotic protein expression levels was dominant,the quick emancipation of mitochondrial cytochrome-C,the activation of apoptosis key pro-Caspase-3 and the sharp increase of the number of positive apoptotic nuclei showed that there was a process of apoptosis postmortem in the duck skeletal muscle cells evidently.Consumption of ATP and the pH value reduction provide a necessary environment within the cell apoptosis and,the degree of apoptosis may reach a peak around 8 h postmortem in duck skeletal muscle.

Key words: Bcl-2 Bax, Cytochrome-C, Caspase-3 TUNEL, ATP pH Apoptosis, Duck Postmortem conditioning

CLC Number:

S834

WANG Dao-ying, HUANG Wei, ZHANG Mu-han, LIU Fang, ZHU Yong-zhi, XU Xing-lian, XU Wei-min, CAO Jian-min. Study on the Apoptosis and Effect Facts of Duck Skeletal Muscle during Postmortem Ageing[J]. ACTA AGRICULTURAE BOREALI-SINICA, 2012, 27(5): 191-197. doi: 10.3969/j.issn.1000-7091.2012.05.036.

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References

[1] Delivoria-Papadopoulos M, Gorn M, Ashraf Q M, et al. ATP and cytochrome c-dependent activation of caspase-9 during hypoxia in the cerebral cortex of newborn piglets [J]. Neuroscience Letters, 2007,429 : 115 119.

[2] Eguchi Y, Shimizu S,Tsujimoto Y. Intracellular ATP levels determine cell death fate by apoptosis or necrosis[J]. Cancer Research, 1997,57 : 1835 1840.

[3] Eguchi Y, Srinivasan A, Tomaselli K J, et al. ATP-dependent steps in apoptotic signal transduction [J]. Cancer Research, 1999,59:2174 2181.

[4] Communal C, Sumandea M, Tombe P, et al. Functional consequences of caspase activation in cardiac myocytes [J]. Proceedings of the National Academy of Science, 2002,99:6252 6256.

[5] Fischer U,Janicke R U, Schulze-Osthoff K. Many cuts to ruin : a comprehensive update of caspase substrates [J]. Cell Death & Differentiation,2003,10:76 100.

[6] Ahmed O, Carlos H H, Gerald C,et al. Revisiting the conversion of muscle into meat and the underlying mechanisms[J]. Meat Science ,2006,74:46 48.

[7] Kemp C M, Parr T, Bardsley R G, et al. Comparison of the relative expression of caspase isoforms in different porcine skeletal muscles [J]. Meat Science, 2006b, 73 : 426 431.

[8] Cao J,Sun W ,Zhou G,et al. Morphological and biochemical assessment of apoptosis in different skeletal muscles of bulls during conditioning[J]. Journal of Animal Science, 2010,88:3439 3444.

[9] Matsuyama S, Reed J. Mitochondria-dependent apoptosis and cellular pH regulation[J]. Cell Death and Differentiation ,2000,7 : 1155 1165.

[10] Riva C, Chevrier C, Pasqual N, et al. Bcl-2/bax protein expression in heart, slow-twitch and fast-twitch muscles in young rats growing under chronic hypoxia conditions [J]. Molecular and Cellular Biochemistry, 2001,226 : 9 -16.

[11] Chinnaiyan A M, Orth K, O'Rourke K, et al. Molecular ordering of the cell death pathway, bcl-2 and Bcl-xL function upstream of the CED-3-like apoptotic proteases [J]. Journal of Biological Chemistry, ! 996,271 : 4573 3576.

[12] Yang J, Liu X, Bhalla K,et al. Prevention of apoptosis by bcl-2: Release of cytochrome C from mitochondria blocked [J]. Science, 1997,275 : 1129 1132.

[13] Christian F, Sara C, Luca S. Organelle isolation : functional mitochondria from mouse liver, muscle and cultured filroblasts[J]. Natural Protocols, 2007 : 2 ( 3 ) : 287 295.

[14] Veciana-Nogues M T, Izquierdo-Pulido M, Vidal-Carou M C. Determination of ATP related compounds in fresh and canned tuna fish by HPLC [J]. Food Chemistry, 1997,59:467 472.

[15] Sedlak T W, Oltvai Z N, Yang E, et al. Multiple Bcl-2 family Members demonstrate selective dimerizations with Bax[Jl. Proc Natl Acad Sci USA, 1995,92:7834 7838.

[16] Rosse T, Olivier R, Monney L, et al. Bcl-2 prolongs cell survival after bax-induced release of cytochrome c [J]. Nature, 1998,391:496 499.

[17] Dhyan C, Grace C, Peter T D,et al. Bax-dependent regu-lation of bak by vohage-dependent nion Channel 2[J]. J Biol Chem ,2005,280( 5 ) : 19051 19061.

[18] 01tvai Z N, Milliman C L, Korsmeyer S J. Bcl-2 heterodimerizes in vivo with a conserved homolog,bax,that accelerates programmed cell death [J]. Cell, 1993,74 : 609 619.

[19] Xie Z, Koyama T, Suzuki J, et al. Coronary reperfusion following is chemia:different expression of bcl-2 and bax proteins,and cardiomyocyte apoptosis [J]. Jpn Heart J, 2001,42 (6) :759 770.

[20] McClintock D S,Santore M T,Lee V Y,et al. Bcl-2 family members and functional electron transport chain regulate oxygen deprivation-induced cell death [J]. Mol Cell Biol,2002,22 ( 1 ) :94 104.

[21] Korsmeyer S J. Bcl-2 gene family and the regulation of programmed cell death[J]. Cancer Res, 1999,59 : 1693 1700.

[22] Liu H F, Liu W W, Fang D C,et al. Expression of bcl-2 protein in gastric carcinoma and its significe[J]. World J Gastroenterol, 1998,4 : 228 230.

[23] Yu X, Kubota H, Wang R, et al. Involvement of Bcl-2 family genes and Fas signaling system in primary and secondary male germ cell apoptosis induced by 2-bromoprapane in rat [J]. Toxical Appl Pharmacol, 2001 , 174(1) :35 -48.

[24] Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of bax is responsible for mitochondrial cytochrome c release during apoptosis [J]. Journal of Cell Biology, 1999,144:891 901.

[25] Li P, Nijhawan D, Budihardjo I,et al. Cytochrome c and dATP-dependt formation of Apaf-1/ Caspase-9 complex initiates an apoptotic protease cascade [J]. Cell, 1997, 91(4) :479 -489.

[26] Zou H, Henzel W J, Liu X, et al. Apaf-1, a human protein homologous to C. elegans CED-4,participates in Cytochrome c-dependent activation of caspase-3 [J]. Cell, 1997,90(3) :405 -415.

[27] Phaneuf S,Leeuwenburgh C. Cytochrome-C release from mitochondria in the aging heart: a possible mechanism for apoptosis with age [J]. Am J Physiol Regul Integr Comp Physiol,2002 ,282 :423 430.

[28] Cosulich S C, Savory P J, Clarke P R. Bcl-2 regulates amplification of caspase activation by cytochrome c [J]. Current Biolgy, 1999,9 : 147 150.

[29] Adams J M. Ways of dying: muhiple pathways to apopto-sis[J]. Genes Dev,2003,17:2481 2495.

[30] Grutter M G. Caspases:key players in programmed cell death [J]. Current Opinion in Structural Biology, 2000, 10:649 655.

[31] Fujimura M, Morita F Y, Murakami K,et al. Cytosolic redistribution of cytochrome C after transient focal cerebral ischemia in rats [J]. J Cereb Blood Flow Metab, 1998, 18 ( 11 ) : 1239 1247.

[32] Deng X L,Wang Y, Chou J, et al. Methamphetamine causes widespread apoptosis in the mouse brain: evidence from using an improved TUNEL histochemical method [J]. Molecular Brain Research ,2001,93:64 69.

[33] Wijsman J H,Jonker R,Keijzer R,et al. A new method to detect apoptosis in paraffin sections: in situend-labeling of frag-mented DNA [J]. Histochem Cytochem, 1993,41(1) :7.

[34] Tidball J G,Albrecht D E,Lokensgard B E, et al. Apoptosis precedes necrosis in dystrophin-deficient muscle [J]. Journal of Cell Science, 1995,108:2197 2204.

[35] Eguchi Y,Shimizu S,TsujimotoY. Intracellular ATP levels determine cell death fate by apoptosis or necrosis[J]. Cancer Research, 1997,57 : 1835 1840.

[36] Ferrari D, Stepczynska A, Los M,et al. Differential regulation and ATP requirement for caspase-8 and caspase-3 activation during CD95 and anticancer drug-induced apoptosis [J]. Journal of Experimental Medicine, 1998, 188:979 984.

[37] Kass G E N,Eriksson J E,Weis M,et al. Research Communication Chromatin condensation during apoptosis requires ATP [J]. Biochem. J, 1996,318:749 752.

[38] Liu X, Kim C N, Yang J, et al. Induction of apoptotic program in cell-free extracts:requirement for dATP and cytochrome c[J]. Cell, 1996,86 : 147 157.

[39] Qian T, Nieminen A L, Herman B. Mitochondrial permeability transition in pH-dependent reperfusion injury to rat hepatocytes [J]. Am J Physiol, 1997, 273 : 1783 1792.

[40] Matsuyama S,Llopi J,Deveraux Q, et al. Changes in intramitochondrial and cytosolic pH: Early events that modulate caspases activation during apoptosis [J]. Nature Cell Biology,2000,2:318 325.

[41] 《鱼藤酮致帕金森大鼠的脑黑质中凋亡相关蛋白Bcl-2、Bax表达改变》[J].中国实验动物学报,2009(1).

[42] 《宰后成熟过程中麻鸭肉质指标变化研究》[J].浙江农业学报,2010(5).

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