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2025 Vol.52, Issue 4 Preview Page

Review Article

Role of apoptosis and anti-apoptosis mechanism in meat quality: An integrated mechanistic review of tenderness development
Jong Ho Lee1
,
Traci Alexandra Cramer1
,
Dylan Dragon Metzel1
,
Yuan H. Brad Kim1*
1Department of Animal Sciences, Purdue University, West Lafayette, IN 47906, USA
*Corresponding Author
1 December 2025. pp. 397-415
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Abstract

Muscle-to-meat conversion is a complex process that determines final meat quality, which in turn influences consumer preference and repurchasing decisions. Traditionally, this conversion process has been explained through the calpain system, but it has a limited ability to account for changes in muscle type, various stress conditions, and breed-specific differences. Recent research has consistently demonstrated that apoptosis initiates this conversion. Therefore, this review proposes apoptosis as a key mechanism regulating postmortem muscle changes, and it introduces an integrated model to explain the complex conversion process. Apoptosis is triggered by hypoxia, energy depletion, and oxidative stress in postmortem muscle. This process is regulated by increased mitochondrial outer membrane permeability, cytochrome c release, and an increase in the Bax/Bcl-2 ratio. Caspases activated by these events degrade structural proteins and calpastatin. However, this apoptotic process may potentially be inhibited by heat shock proteins and endogenous antioxidant enzymes. While apoptosis may contribute to tenderization, it can induce cell shrinkage and mitochondrial damage, which can also negatively impact meat quality attributes such as water-holding capacity and color stability. This integrated understanding can explain complex phenomena such as muscle-specific variations and the differential impacts of antemortem versus postmortem stress. Therefore, this framework is expected to form the basis for new industrial strategies to improve meat quality.

Keywords
apoptosis
calpain
caspase
heat shock proteins
meat quality
References
1

Adrain C, Creagh EM, Martin SJ. 2001. Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2. The EMBO Journal 20:6627-6636.

10.1093/emboj/20.23.662711726499PMC125329
2

Adrain C, Martin SJ. 2001. The mitochondrial apoptosome: A killer unleashed by the cytochrome seas. Trends in Biochemical Sciences 26:390-397.

10.1016/S0968-0004(01)01844-8
3

Alnemri ES, Livingston DJ, Nicholson DW, Salvesen G, Thornberry NA, Wong WW, Yuan J. 1996. Human ICE/CED-3 protease nomenclature. Cell 87:171.

10.1016/S0092-8674(00)81334-3
4

Altan, Ö, Pabuçcuoğlu A, Altan A, Konyalioğlu S, Bayraktar H. 2003. Effect of heat stress on oxidative stress, lipid peroxidation and some stress parameters in broilers. British Poultry Science 44:545-550.

10.1080/00071660310001618334
5

Azad M, Kikusato M, Sudo S, Amo T, Toyomizu M. 2010. Time course of ROS production in skeletal muscle mitochondria from chronic heat-exposed broiler chicken. Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 157:266-271.

10.1016/j.cbpa.2010.07.011
6

Becila S, Herrera-Mendez CH, Coulis G, Labas R, Astruc T, Picard B, Boudjellal A, Pelissier P, Bremaud L, Ouali A. 2010. Postmortem muscle cells die through apoptosis. European Food Research and Technology 231:485-493.

10.1007/s00217-010-1296-5
7

Beere HM. 2005. Death versus survival: Functional interaction between the apoptotic and stress-inducible heat shock protein pathways. The Journal of Clinical Investigation 115:2633-2639.

10.1172/JCI2647116200196PMC1236700
8

Blunt BC, Creek AT, Henderson DC, Hofmann PA. 2007. H2O2 activation of HSP25/27 protects desmin from calpain proteolysis in rat ventricular myocytes. American Journal of Physiology-Heart and Circulatory Physiology 293:H1518-H1525.

10.1152/ajpheart.00269.2006
9

Cadenas E, Davies KJ. 2000. Mitochondrial free radical generation, oxidative stress, and aging. Free Radical Biology and Medicine 29:222-230.

10.1016/S0891-5849(00)00317-8
10

Cao J, Sun W, Zhou G, Xu X, Peng Z, Hu Z. 2010. Morphological and biochemical assessment of apoptosis in different skeletal muscles of bulls during conditioning. Journal of Animal Science 88:3439-3444.

10.2527/jas.2009-2412
11

Chen C, Zhang J, Guo Z, Shi X, Zhang Y, Zhang L, Yu Q, Han L. 2020. Effect of oxidative stress on AIF-mediated apoptosis and bovine muscle tenderness during postmortem aging. Journal of Food Science 85:77-85.

10.1111/1750-3841.14969
12

Chen L, Chai Y, Luo J, Wang J, Liu X, Wang T, Xu X, Zhou G, Feng X. 2021. Apoptotic changes and myofibrils degradation in post-mortem chicken muscles by ultrasonic processing. LWT 142:110985.

10.1016/j.lwt.2021.110985
13

Chen L, Feng XC, Lu F, Xu XL, Zhou GH, Li QY, Guo XY. 2011. Effects of camptothecin, etoposide and Ca2+ on caspase-3 activity and myofibrillar disruption of chicken during postmortem ageing. Meat Science 87:165-174.

10.1016/j.meatsci.2010.10.002
14

Chen L, Lan L, Bi S, Zhou M, Wan J, Zhou Y, Liu Y, Zhu Q. 2025. Exploring the internal environmental changes of muscle cells and apoptotic phase of mitochondria in dry-cured loin using electrical stimulation: Promoting the precise regulation of loin ham quality. Journal of Agricultural and Food Chemistry 73:3025-3036.

10.1021/acs.jafc.4c09673
15

Cortese JD, Voglino AL, Hackenbrock CR. 1995. Persistence of cytochrome c binding to membranes at physiological mitochondrial intermembrane space ionic strength. Biochimica et Biophysica Acta (BBA) - Bioenergetics 1228:216-228.

10.1016/0005-2728(94)00178-8
16

Cramer T, Penick ML, Waddell JN, Bidwell CA, Kim YHB. 2018. A new insight into meat toughness of callipyge lamb loins - The relevance of anti-apoptotic systems to decreased proteolysis. Meat Science 140:66-71.

10.1016/j.meatsci.2018.03.002
17

Croall DE, McGrody KS. 1994. Domain structure of calpain: Mapping the binding site for calpastatin. Biochemistry 33:13223-13230.

10.1021/bi00249a008
18

Czabotar PE, Lessene G, Strasser A, Adams JM. 2014. Control of apoptosis by the BCL-2 protein family: Implications for physiology and therapy. Nature Reviews Molecular Cell Biology 15:49-63.

10.1038/nrm3722
19

Delgado E, Geesink G, Marchello J, Goll D, Koohmaraie M. 2001. The calpain system in three muscles of normal and callipyge sheep. Journal of Animal Science 79:398-412.

10.2527/2001.792398x
20

Desagher S, Martinou JC. 2000. Mitochondria as the central control point of apoptosis. Trends in Cell Biology 10:369-377.

10.1016/S0962-8924(00)01803-1
21

Dizdaroglu M, Jaruga P, Birincioglu M, Rodriguez H. 2002. Free radical-induced damage to DNA: Mechanisms and measurement. Free Radical Biology and Medicine 32:1102-1115.

10.1016/S0891-5849(02)00826-2
22

Fridovich I. 1986. Biological effects of the superoxide radical. Archives of Biochemistry and Biophysics 247:1-11.

10.1016/0003-9861(86)90526-6
23

Fuentes-Prior P, Salvesen GS. 2004. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochemical Journal 384:201-232.

10.1042/BJ2004114215450003PMC1134104
24

Garcia-Macia M, Sierra V, Palanca A, Vega-Naredo I, de Gonzalo-Calvo D, Rodriguez-Gonzalez S, Olivan M, Coto-Montes A. 2014. Autophagy during beef aging. Autophagy 10:137-143.

10.4161/auto.2665924225649PMC4389867
25

Green DR, Reed JC. 1998. Mitochondria and apoptosis. Science 281:1309-1312.

10.1126/science.281.5381.1309
26

Guo B, Zhang W, Tume RK, Hudson NJ, Huang F, Yin Y, Zhou G. 2016. Disorder of endoplasmic reticulum calcium channel components is associated with the increased apoptotic potential in pale, soft, exudative pork. Meat Science 115:34-40.

10.1016/j.meatsci.2016.01.003
27

Hanna R, Rozenberg A, Saied L, Ben-Yosef D, Lavy T, Kleifeld O. 2023. In-depth characterization of apoptosis N-terminome reveals a link between caspase-3 cleavage and posttranslational N-terminal acetylation. Molecular & Cellular Proteomics 22:100584.

10.1016/j.mcpro.2023.10058437236440PMC10362333
28

He W, Peng Y, Huang H, Hang L, Liu Z, Yu H, Zhang Y. 2025. Postmortem changes of desmin, talin-2, vinculin, and integrin β1 in chicken breast and their effects on tenderness. Journal of Agricultural and Food Chemistry 73:7393-7404.

10.1021/acs.jafc.4c13003
29

Held KD, Sylvester FC, Hopcia KL, Biaglow JE. 1996. Role of Fenton chemistry in thiol-induced toxicity and apoptosis. Radiation Research 145:542-553.

10.2307/3579272
30

Huang F, Huang M, Zhang H, Zhang C, Zhang D, Zhou G. 2016. Changes in apoptotic factors and caspase activation pathways during the postmortem aging of beef muscle. Food Chemistry 190:110-114.

10.1016/j.foodchem.2015.05.056
31

Hüttemann M, Pecina P, Rainbolt M, Sanderson TH, Kagan VE, Samavati L, Doan JW, Lee I. 2011. The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis. Mitochondrion 11:369-381.

10.1016/j.mito.2011.01.01021296189PMC3075374
32

Kagan VE, Borisenko GG, Tyurina YY, Tyurin VA, Jiang J, Potapovich AI, Kini V, Amoscato AA, Fujii Y. 2004. Oxidative lipidomics of apoptosis: Redox catalytic interactions of cytochrome c with cardiolipin and phosphatidylserine. Free Radical Biology and Medicine 37:1963-1985.

10.1016/j.freeradbiomed.2004.08.016
33

Kagan VE, Tyurin VA, Jiang J, Tyurina YY, Ritov VB, Amoscato AA, Osipov AN, Belikova NA, Kapralov AA, Kini V, et al. 2005. Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors. Nature Chemical Biology 1:223-232.

10.1038/nchembio727
34

Kemp C, Bardsley R, Parr T. 2006. Changes in caspase activity during the postmortem conditioning period and its relationship to shear force in porcine longissimus muscle. Journal of Animal Science 84:2841-2846.

10.2527/jas.2006-163
35

Kemp C, King D, Shackelford S, Wheeler T, Koohmaraie M. 2009. The caspase proteolytic system in callipyge and normal lambs in longissimus, semimembranosus, and infraspinatus muscles during postmortem storage. Journal of Animal Science 87:2943-2951.

10.2527/jas.2009-1790
36

Kemp CM, Parr T. 2012. Advances in apoptotic mediated proteolysis in meat tenderisation. Meat Science 92:252-259.

10.1016/j.meatsci.2012.03.013
37

Kerr JF, Wyllie AH, Currie AR. 1972. Apoptosis: A basic biological phenomenon with wideranging implications in tissue kinetics. British Journal of Cancer 26:239-257.

10.1038/bjc.1972.334561027PMC2008650
38

Kim JY, Lee B, Kim EJ, Choi YM. 2023. Effects of apoptotic factor levels on palatability variation during postmortem aging of Holstein longissimus thoracis muscles classified as Warner-Bratzler shear force change value. Food Chemistry 428:136741.

10.1016/j.foodchem.2023.136741
39

Kötter S, Unger A, Hamdani N, Lang P, Vorgerd M, Nagel-Steger L, Linke WA. 2014. Human myocytes are protected from titin aggregation-induced stiffening by small heat shock proteins. Journal of Cell Biology 204:187-202.

10.1083/jcb.20130607724421331PMC3897184
40

Landis GN, Tower J. 2005. Superoxide dismutase evolution and life span regulation. Mechanisms of Ageing and Development 126:365-379.

10.1016/j.mad.2004.08.012
41

Laville E, Sayd T, Morzel M, Blinet S, Chambon C, Lepetit J, Renand G, Hocquette JF. 2009. Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization. Journal of Agricultural and Food Chemistry 57:10755-10764.

10.1021/jf901949r
42

Lee B, Choi YM. 2024. A new perspective on apoptosis: Its impact on meat and organoleptic quality in different animals. Food Chemistry: X 25:102120.

10.1016/j.fochx.2024.10212039844962PMC11751429
43

Lee B, Kim JY, Choi YM. 2022. Associations of apoptotic and anti-apoptotic factors with beef quality, histochemical characteristics, and palatability of Hanwoo Longissimus thoracis muscle. Animals 12:467.

10.3390/ani1204046735203175PMC8868170
44

Li C, Yin X, Xue P, Wang F, Song R, Song Q, Su J, Zhang H. 2022a. Apoptosis and autophagy of muscle cell during pork postmortem aging. Animal Bioscience 37:284.

10.5713/ab.23.014837905320PMC10766493
45

Li K, Li Y, Shelton JM, Richardson JA, Spencer E, Chen ZJ, Wang X, Williams RS. 2000. Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis. Cell 101:389-399.

10.1016/S0092-8674(00)80849-1
46

Li X, Hu L, Zhu X, Guo X, Deng X, Zhang J. 2022b. The effect of caspase-3 in mitochondrial apoptosis activation on degradation of structure proteins of Esox lucius during postmortem storage. Food Chemistry 367:130767.

10.1016/j.foodchem.2021.130767
47

Liu Y, Du M, Li X, Chen L, Shen Q, Tian J, Zhang D. 2016. Role of the ubiquitin-proteasome pathway on proteolytic activity in postmortem proteolysis and tenderisation of sheep skeletal muscle. International Journal of Food Science and Technology 51:2353-2359.

10.1111/ijfs.13214
48

Lomiwes D, Farouk M, Wiklund E, Young O. 2014. Small heat shock proteins and their role in meat tenderness: A review. Meat Science 96:26-40.

10.1016/j.meatsci.2013.06.008
49

Longo V, Lana A, Bottero MT, Zolla L. 2015. Apoptosis in muscle-to-meat aging process: The omic witness. Journal of Proteomics 125:29-40.

10.1016/j.jprot.2015.04.023
50

Lowe SW, Lin AW. 2000. Apoptosis in cancer. Carcinogenesis 21:485-495.

10.1093/carcin/21.3.485
51

Lv Z, Song X, Xu J, Jia Z, Yang B, Jia Y, Qiu L, Wang L, Song L. 2019. The modulation of Smac/DIABLO on mitochondrial apoptosis induced by LPS in Crassostrea gigas. Fish & Shellfish Immunology 84:587-598.

10.1016/j.fsi.2018.10.035
52

Ma D, Kim YHB. 2020. Proteolytic changes of myofibrillar and small heat shock proteins in different bovine muscles during aging: Their relevance to tenderness and water-holding capacity. Meat Science 163:108090.

10.1016/j.meatsci.2020.108090
53

Ma J, Chen C, Yu Q, Han L. 2022a. AMP-activated protein kinase contributes to myofibrillar protein hydrolysis in bovine skeletal muscle through postmortem mitochondrial dysfunction-induced apoptosis. Journal of Food Biochemistry 46:e14028.

10.1111/jfbc.14028
54

Ma J, Yu Q, Han L. 2022b. The effect of postmortem pH decline rate on caspase-3 activation and tenderness of bovine skeletal muscle during aging. Journal of Food Biochemistry 46:e14215.

10.1111/jfbc.14215
55

Ma Y, Dong X, Wang Y, Wang Z, Xie Y, Zhang W, Pan D, Zhou H, Xu B. 2024a. New findings on post-mortem chicken quality changes: The ROS-influenced MAPK-JNK signaling pathway affects chicken quality by regulating muscle cell apoptosis. Food Chemistry 459:140298.

10.1016/j.foodchem.2024.140298
56

Ma Y, Wang Y, Wang Z, Xie Y, Tang C, Li C, Xu F, Zhou H, Xu B. 2024b. New perspective for Calpain-Mediated regulation of meat Quality: Unveiling the impact on mitochondrial pathway apoptosis in post-mortem. Food Chemistry 441:138287.

10.1016/j.foodchem.2023.138287
57

Maki M, Takano E, Mori H, Sato A, Murachi T, Hatanaka M. 1987. All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II. FEBS Letters 223:174-180.

10.1016/0014-5793(87)80531-8
58

Malheiros J, Enríquez-Valencia CE, Braga CP, Vieira JCS, Vieira D, Pereira GL, Curi RA, Neto OM, Oliveira H, Padilha PM, et al. 2021. Application of proteomic to investigate the different degrees of meat tenderness in Nellore breed. Journal of Proteomics 248:104331.

10.1016/j.jprot.2021.104331
59

Michiels C, Raes M, Toussaint O, Remacle J. 1994. Importance of SE-glutathione peroxidase, catalase, and CU/ZN-SOD for cell survival against oxidative stress. Free Radical Biology and Medicine 17:235-248.

10.1016/0891-5849(94)90079-5
60

Miller R. 2020. Drivers of consumer liking for beef, pork, and lamb: A review. Foods 9:428.

10.3390/foods904042832260287PMC7230179
61

Namura S. 2017. Neuroprotectants: Cell-death based. In Primer on Cerebrovascular Diseases (2nd) edited by Caplan LR, Biller J, Leary MC, Lo EH, Thomas AJ, Yenari M, Zhang JH. pp. 189-192. Academic Press, UK.

10.1016/B978-0-12-803058-5.00038-2
62

Norberg E, Orrenius S, Zhivotovsky B. 2010. Mitochondrial regulation of cell death: Processing of apoptosis-inducing factor (AIF). Biochemical and Biophysical Research Communications 396:95-100.

10.1016/j.bbrc.2010.02.163
63

Ouali A, Herrera-Mendez CH, Coulis G, Becila S, Boudjellal A, Aubry L, Sentandreu MA. 2006. Revisiting the conversion of muscle into meat and the underlying mechanisms. Meat Science 74:44-58.

10.1016/j.meatsci.2006.05.010
64

Pandey P, Farber R, Nakazawa A, Kumar S, Bharti A, Nalin C, Weichselbaum R, Kufe D, Kharbanda S. 2000. Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3. Oncogene 19:1975-1981.

10.1038/sj.onc.1203531
65

Parsell D, Lindquist S. 1993. The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Annual Review of Genetics 27:437-497.

10.1146/annurev.ge.27.120193.002253
66

Paul C, Manero F, Gonin S, Kretz-Remy C, Virot S, Arrigo AP. 2002. Hsp27 as a negative regulator of cytochrome c release. Molecular and Cellular Biology 22:816-834.

10.1128/MCB.22.3.816-834.200211784858PMC133538
67

Pörn-Ares MI, Samali A, Orrenius S. 1998. Cleavage of the calpain inhibitor, calpastatin, during apoptosis. Cell Death & Differentiation 5:1028-1033.

10.1038/sj.cdd.4400424
68

Rønning SB, Andersen PV, Pedersen ME, Hollung K. 2017. Primary bovine skeletal muscle cells enters apoptosis rapidly via the intrinsic pathway when available oxygen is removed. PLOS ONE 12:e0182928.

10.1371/journal.pone.018292828792534PMC5549745
69

Saccà E, Corazzin M, Bovolenta S, Piasentier E. 2019. Meat quality traits and the expression of tenderness-related genes in the loins of young goats at different ages. Animal 13:2419-2428.

10.1017/S1751731119000405
70

Salo DC, Donovan CM, Davies KJ. 1991. HSP70 and other possible heat shock or oxidative stress proteins are induced in skeletal muscle, heart, and liver during exercise. Free Radical Biology and Medicine 11:239-246.

10.1016/0891-5849(91)90119-N
71

Sentandreu M, Coulis G, Ouali A. 2002. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends in Food Science & Technology 13:400-421.

10.1016/S0924-2244(02)00188-7
72

Shackelford S, Koohmaraie M, Cundiff L, Gregory K, Rohrer G, Savell J. 1994. Heritabilities and phenotypic and genetic correlations for bovine postrigor calpastatin activity, intramuscular fat content, Warner-Bratzler shear force, retail product yield, and growth rate. Journal of Animal Science 72:857-863.

10.2527/1994.724857x
73

Sierra V, Oliván M. 2013. Role of mitochondria on muscle cell death and meat tenderization. Recent Patents on Endocrine, Metabolic & Immune Drug Discovery 7:120-129.

10.2174/1872214811307020005
74

Tie H, Lu X, Yu D, Yang F, Jiang Q, Xu Y, Xia W. 2022. Apoptosis inducing factors involved in the changes of flesh quality in postmortem grass carp (Ctenopharyngodon idella) muscle. Foods 12:140.

10.3390/foods1201014036613356PMC9818144
75

Tuell JR, Kim HW, Zhang J, Guedes J, Seo JK, Schoonmaker JP, Kim YHB. 2021. Arginine supplementation may improve color and redox stability of beef loins through delayed onset of mitochondrial-mediated apoptotic processes. Food Chemistry 343:128552.

10.1016/j.foodchem.2020.128552
76

Underwood K, Means W, Du M. 2008. Caspase 3 is not likely involved in the postmortem tenderization of beef muscle. Journal of Animal Science 86:960-966.

10.2527/jas.2007-0549
77

Valko M, Rhodes C, Moncol J, Izakovic M, Mazur M. 2006. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chemico-Biological Interactions 160:1-40.

10.1016/j.cbi.2005.12.009
78

Vincent JP, Fletcher AG, Baena-Lopez LA. 2013. Mechanisms and mechanics of cell competition in epithelia. Nature Reviews Molecular Cell Biology 14:581-591.

10.1038/nrm3639
79

Voss OH, Batra S, Kolattukudy SJ, Gonzalez-Mejia ME, Smith JB, Doseff AI. 2007. Binding of caspase-3 prodomain to heat shock protein 27 regulates monocyte apoptosis by inhibiting caspase-3 proteolytic activation. Journal of Biological Chemistry 282:25088-25099.

10.1074/jbc.M701740200
80

Wang L, Ma G, Zhang Y, Shi X, Han L, Yu Q, Zhao S, Ma J. 2018a. Effect of mitochondrial cytochrome c release and its redox state on the mitochondrial-dependent apoptotic cascade reaction and tenderization of yak meat during postmortem aging. Food Research International 111:488-497.

10.1016/j.foodres.2018.05.049
81

Wang LL, Yu QL, Han L, Ma XL, Song RD, Zhao SN, Zhang WH. 2018b. Study on the effect of reactive oxygen species-mediated oxidative stress on the activation of mitochondrial apoptosis and the tenderness of yak meat. Food Chemistry 244:394-402.

10.1016/j.foodchem.2017.10.034
82

Wang T, Feng X, Li L, Luo J, Liu X, Zheng J, Fan X, Liu Y, Xu X, Zhou G. 2022. Effects of quercetin on tenderness, apoptotic and autophagy signalling in chickens during post-mortem ageing. Food Chemistry 383:132409.

10.1016/j.foodchem.2022.132409
83

Wang X, Huang L, Zhang Y, Zhu L, Yang X, Zuo H, Luo X, Mao Y, Hopkins DL. 2023. Exploratory study on the potential regulating role of Peroxiredoxin 6 on proteolysis and relationships with desmin early postmortem. Meat Science 195:109021.

10.1016/j.meatsci.2022.109021
84

Wendt A, Thompson VF, Goll DE. 2004. Interaction of calpastatin with calpain: A review. Biological Chemistry 385:465-472.

10.1515/BC.2004.054
85

Yan Y, Chen X, Huang J, Huan C, Li C. 2022. H2O2-induced oxidative stress impairs meat quality by inducing apoptosis and autophagy via ROS/NF-κB signaling pathway in broiler thigh muscle. Poultry Science 101:101759.

10.1016/j.psj.2022.10175935240354PMC8889410
86

Yang B, Chen T, Li H, Li Y, Yang R. 2021. Impact of postmortem degradation of cytoskeletal proteins on intracellular gap, drip channel and water-holding capacity. Meat Science 176:108472.

10.1016/j.meatsci.2021.108472
87

Youle RJ, Van Der Bliek AM. 2012. Mitochondrial fission, fusion, and stress. Science 337:1062-1065.

10.1126/science.121985522936770PMC4762028
88

Zhang J, Li M, Yu Q, Han L, Ma Z. 2019. Effects of lysosomal–mitochondrial apoptotic pathway on tenderness in post-mortem bovine longissimus muscle. Journal of Agricultural and Food Chemistry 67:4578-4587.

10.1021/acs.jafc.9b00894
89

Zhang J, Ma D, Kim YHB. 2020a. Mitochondrial apoptosis and proteolytic changes of myofibrillar proteins in two different pork muscles during aging. Food Chemistry 319:126571.

10.1016/j.foodchem.2020.126571
90

Zhang J, Ma G, Guo Z, Yu Q, Han L, Han M, Zhu Y. 2018. Study on the apoptosis mediated by apoptosis-inducing-factor and influencing factors of bovine muscle during postmortem aging. Food Chemistry 266:359-367.

10.1016/j.foodchem.2018.06.032
91

Zhang J, Wang S, Ge W. 2022. Mechanisms of mitochondrial apoptosis-mediated meat tenderization based on quantitative phosphoproteomic analysis. Foods 11:3751.

10.3390/foods1123375136496558PMC9741025
92

Zhang J, Yu Q, Han L, Han M, Han G. 2020b. Effects of lysosomal iron involvement in the mechanism of mitochondrial apoptosis on postmortem muscle protein degradation. Food Chemistry 328:127174.

10.1016/j.foodchem.2020.127174
93

Zhang M, Wang D, Huang W, Liu F, Zhu Y, Xu W, Cao J. 2013. Apoptosis during postmortem conditioning and its relationship to duck meat quality. Food Chemistry 138:96-100.

10.1016/j.foodchem.2012.10.142
94

Zou B, Jia F, Wang H, Duan M, Li X, Dai R. 2023. Changes of postmortem apoptotic factors, genes and proteins and their potential associations with beef tenderization. Food Science of Animal Products 1:9240040-9240040.

10.26599/FSAP.2023.9240040
95

Zou B, Liu X, Yu H, Zhang S, Xie P, Sun B, Zang M. 2025. Effects of mitoquinone on various patterns of postmortem apoptosis and beef tenderization. Food Bioscience 68:106379.

10.1016/j.fbio.2025.106379
96

Zou B, Yu Q, Shao L, Sun Y, Li X, Dai R. 2022. Alteration of mitochondrial lipidome and its potential effect on apoptosis, mitochondrial reactive oxygen species production, and muscle oxidation in beef during early postmortem. Journal of Agricultural and Food Chemistry 70:8064-8074.

10.1021/acs.jafc.2c02519
Information
  • Publisher :Institute of Agricultural Science, Chungnam National University
  • Publisher(Ko) :충남대학교 농업과학연구소
  • Journal Title :Korean Journal of Agricultural Science
  • Journal Title(Ko) :농업과학연구
  • Volume : 52
  • No :4
  • Pages :397-415
  • Received Date : 2025-11-20
  • Revised Date : 2025-11-26
  • Accepted Date : 2025-11-26
  • DOI :https://doi.org/10.7744/kjoas.520402
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