Abundância de RNA do sistema calpaínas-calpastatina, genes relacionados à qualidade da carne de ruminantes: uma revisão

Autores

  • Isabella Guartieri da Silva UNOESTE Autor
  • Lorraine Pissinin Dutra UNOESTE Autor
  • Ines Cristina Giometti UNOESTE Autor
  • Calie Castilho UNOESTE Autor
  • Gabriella Capitane Sena UNOESTE Autor
  • Letícia Jalloul Guimarães UniFatecie Autor
  • Natália Carolina Vieira UNOESTE Autor
  • Quézia Hadassa Machado Leite UNOESTE Autor
  • Maria Fernanda Gibim UNOESTE Autor
  • Isadora de Souza e Silva UNOESTE Autor
  • Fabíola Cristine de Almeida Rêgo Unopar Autor
  • Marilice Zundt Unoeste Autor

DOI:

https://doi.org/10.61411/rsc202481517

Palavras-chave:

μ-Calpaína, Calpastatina, m-Calpaína, Ovis aries, RT-qPCR

Resumo

As exigências do mercado consumidor com a carne ovina têm aumentado e visando atender essas demandas, a produção deve ser otimizada de modo complexo, sendo que os atributos qualitativos possuem muitas variáveis, influenciados principalmente pela genética, e outros fatores como nutrição e manejo pré e pós-abate. A maciez é o principal atributo considerado pelos consumidores e durante o processo de amaciamento da carne, há ação de genes específicos que determinam o resultado. Esses genes ativam o sistema enzimático das calpaínas-calpastatina, que é formado por duas calpaínas: μ-calpaína e m-calpaína, que desempenham um papel importante nos principais processos intracelulares. Com ênfase na reestruturação do citoesqueleto, regulação do ciclo celular, apoptose e formação de tecido muscular. Em contrapartida o gene CAST inibe as calpaínas e também influencia na produção, maciez e qualidade da carne. Portanto, a análise do RNA é um passo necessário na preparação de métodos como RT-qPCR. Pesquisas mostram que há anos a ação do complexo calpaínas-calpastatina atua diretamente na proteólise muscular, na transformação do músculo em carne, tornando-se responsável pela sua qualidade, porém mais pesquisas são sugeridas sobre o nível de abundância de RNA para os genes CAPN1, CAPN2 e CAST, especialmente em ovinos.

Referências

DELIZA, R. et al. Avaliação dos Hábitos de Compra do Consumidor Brasileiro e Consumo de Carne Ovina. 2018. Disponível em: https://www.embrapa.br/busca-de-publicacoes/-/publicacao/1110438/Avaliacao-Dos-Habitos-de-Compra-Do-Consumidor-Brasileiro-e-Consumo-de-Carne-Ovina.

ALVAREZ, C.; KOOLMAN, L.; WHELAN, M.; MOLONEY, A. Effect of Pre-Slaughter Practises and Early Post-Mortem Interventions on Sheep Meat Tender-ness and Its Impact on Microbial Status. Foods, v. 11, n. 2, p. 181, 2022. DOI: https://doi.org/10.3390/foods11020181. DOI: https://doi.org/10.3390/foods11020181

HUANG, F. et al. Contribution of mitochondria to postmortem muscle tenderiza-tion: a review. Critical Reviews in Food Science and Nutrition, p. 1–17, 2023. DOI: https://doi.org/10.1080/10408398.2023.2266767. DOI: https://doi.org/10.1080/10408398.2023.2266767

PINHEIRO, R. S. B. et al. Physicochemical Quality and Fatty Acid Profile in the Meat of Goats Fed Forage Cactus as a Substitute for Tifton 85 Hay. Animals: An Open Access Journal from MDPI, v. 13, n. 6, p. 957, 2023. DOI: https://doi.org/10.3390/ani13060957 DOI: https://doi.org/10.3390/ani13060957

MARCHEWKA, J. et al. Linking key husbandry factors to the intrinsic quality of broiler meat. Poultry Science, v. 102, n. 2, p. 102384, 2023. DOI: https://doi.org/10.1016/j.psj.2022.102384 DOI: https://doi.org/10.1016/j.psj.2022.102384

REXROAD, C. et al. Genome to Phenome: Improving Animal Health, Production, and Well-Being – A New USDA Blueprint for Animal Genome Research 2018–2027. Frontiers in Genetics, v. 10, 2019. DOI: https://doi.org/10.3389/fgene.2019.00327 DOI: https://doi.org/10.3389/fgene.2019.00327

LEAL, R. S. et al. Desempenho e rendimento de carcaça de suínos na fase de ter-minação, recebendo dietas com diferentes níveis de ractopamina. Revista Brasilei-ra de Saúde e Produção Animal, v. 16, p. 582-590, 2015. DOI: https://doi.org/10.1590/S1519-99402015000300010

KAUR, L. et al. Endogenous Proteolytic Systems and Meat Tenderness: Influence of Post-Mortem Storage and Processing. Food Science of Animal Resources, v. 41, n. 4, p. 589–607, 2021. DOI: https://doi.org/10.5851/kosfa.2021.e27 DOI: https://doi.org/10.5851/kosfa.2021.e27

LI, X. et al. The effect of caspase-3 in mitochondrial apoptosis activation on deg-radation of structure proteins of Esox lucius during postmortem storage. Food Chemistry, v. 367, p. 130767, 2022. DOI: https://doi.org/10.1016/j.foodchem.2021.130767 DOI: https://doi.org/10.1016/j.foodchem.2021.130767

FARKAS, D. et al. Peripheral thickening of the sarcomeres and pointed end elonga-tion of the thin filaments are both promoted by SALS and its formin interaction partners. PLoS Genetics, v. 20, n. 1, p. e1011117, 2024. DOI: https://doi.org/10.1371/journal.pgen.1011117. DOI: https://doi.org/10.1371/journal.pgen.1011117

MADDOCK CARLIN, K. R. et al. Formation of the calpain-1/calpastatin complex promotes activation of calpain-1 under oxidizing conditions. Journal of Animal Science, v. 102, p. skae135, 2024. DOI: https://doi.org/10.1093/jas/skae135 DOI: https://doi.org/10.1093/jas/skae135

FOURNIER, T.; POULAIN, J. P. Eating according to one’s genes? Exploring the French public’s understanding of and reactions to personalized nutrition. Qualita-tive Health Research, v. 28, n. 14, p. 2195-2207, 2018. DOI: https://doi.org/10.1177/1049732318793417. DOI: https://doi.org/10.1177/1049732318793417

SILVA, S. P. B.; HASS, I. AmEG–Ambientes e Expressão Gênica. Legenda, v. 9, p. 1, 2022. DOI: https://doi.org/10.55838/1980-3540.ge.2022.442

GRAHAM, T. G. W. et al. Simple, Inexpensive RNA Isolation and One-Step RT-qPCR Methods for SARS-CoV-2 Detection and General Use. Current Protocols, v. 1, n. 4, p. e130, 2021. DOI: https://doi.org/10.1002/cpz1.130. DOI: https://doi.org/10.1002/cpz1.130

GAGAOUA, M.; MONTEILS, V.; PICARD, B. Data from the farmgate-to-meat continuum including omics-based biomarkers to better understand the variability of beef tenderness: An integromics approach. Journal of Agricultural and Food Chemistry, v. 66, n. 51, p. 13552-13563, 2018. DOI: https://doi.org/10.1021/acs.jafc.8b05744. DOI: https://doi.org/10.1021/acs.jafc.8b05744

FIRETTI, R. et al. Identificação de demanda e estimulada no consumo de carne ovina com apoio de técnicas de estatística multivariada. Revista de Economia e So-ciologia Rural, v. 55, p. 679-692, 2017. DOI: https://doi.org/10.1590/1234-56781806-94790550404. DOI: https://doi.org/10.1590/1234-56781806-94790550404

GUERRERO, A. B.; SAÑUDO, C. Los desafíos reais pt o consumo de carnes fres-cas. Papel das marcas de qualidade. Revista Eurocarne, p. 71–82, 2019.

GOIS, G. C. et al. Qualidade da carne de ovinos terminados em confinamento com dietas com silagens de diferentes cultivares de sorgo. Arquivo Brasileiro de Medi-cina Veterinária e Zootecnia, v. 69, n. 6, p. 1653–1659, 2017. DOI: https://doi.org/10.1590/1678-4162-9231. DOI: https://doi.org/10.1590/1678-4162-9231

ALVES, M. B.; SPERS, E. E.; SILVA, H. M. R. D.; CONTRERAS CASTILLO, C. J. Southeast Brazilian Consumers’ Involvement and Willingness to Pay for Quality Cues in Fresh and Cooked Beef. Journal of Food Products Marketing, v. 28, n. 6, p. 276-293, 2022. DOI: https://doi.org/10.1080/10454446.2022.2129539. DOI: https://doi.org/10.1080/10454446.2022.2129539

CONSTANTINO, P. A. L.; BENCHIMOL, M.; ANTUNES, A. P. Desenhando Terras Indígenas na Amazônia: Garantindo os Direitos Indígenas e a Conservação da Vida Selvagem por meio do Manejo da Caça. Política de Uso da Terra, v. 77, p. 652–660, 2018. DOI: https://doi.org/10.1016/j.landusepol.2018.06.016. DOI: https://doi.org/10.1016/j.landusepol.2018.06.016

HUANG, Y. et al. Feeding regimens affecting carcass and quality attributes of sheep and goat meat - A comprehensive review. Animal Bioscience, v. 36, n. 9, p. 1314–1326, 2023. DOI: https://doi.org/10.5713/ab.23.0051. DOI: https://doi.org/10.5713/ab.23.0051

LANA, A.; ZOLLA, L. Proteolysis in meat tenderization from the point of view of each single protein: A proteomic perspective. Journal of Proteomics, v. 147, p. 85–97, 2016. DOI: https://doi.org/10.1016/j.jprot.2016.02.011 DOI: https://doi.org/10.1016/j.jprot.2016.02.011

VOLPELLI, L. A.; FAILLA, S.; SEPULCRI, A.; PIASENTIER, E. Calpain system in vitro activity and myofibril fragmentation index in fallow deer (Dama dama): effects of age and supplementary feeding. Meat Science, v. 69, n. 3, p. 579-582, 2005. DOI: https://doi.org/10.1016/j.meatsci.2004.09.009. DOI: https://doi.org/10.1016/j.meatsci.2004.09.009

HE, J. et al. Investigation of the relationships between different enzymes and postmortem duck muscle tenderization. Poultry Science, v. 98, n. 11, p. 6125–6130, 2019. DOI: https://doi.org/10.3382/ps/pez301. DOI: https://doi.org/10.3382/ps/pez301

DA CRUZ, B. C. C. et al. Avaliação e composição centesimal e as características físico-químicas da carne de ovinos. Pubvet, v. 10, p. 111-189, 2015. DOI: https://doi.org/10.22256/pubvet.v10n2.147-162. DOI: https://doi.org/10.22256/pubvet.v10n2.147-162

CRETOIU, D. et al. Myofibers. In: ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY, 1088, p. 23-46, 2018. DOI: https://doi.org/10.1007/978-981-13-1435-3_2. DOI: https://doi.org/10.1007/978-981-13-1435-3_2

GANDOLFI, G. et al. Investigation on CAST, CAPN1 and CAPN3 porcine gene polymorphisms and expression in relation to post-mortem calpain activity in mus-cle and meat quality. Meat Science, v. 88, n. 4, p. 694-700, 2011. DOI: https://doi.org/10.1016/j.meatsci.2011.02.031. DOI: https://doi.org/10.1016/j.meatsci.2011.02.031

GE, Y. et al. Effect of Postmortem Phases on Lamb Meat Quality: A Physicochemi-cal, Microstructural and Water Mobility Approach. Food Science of Animal Re-sources, v. 41, n. 5, p. 802–815, 2021. DOI: https://doi.org/10.5851/kosfa.2021.e37. DOI: https://doi.org/10.5851/kosfa.2021.e37

VALADEZ-GARCÍA, K. M. et al. Free ferulic acid supplementation of heat-stressed hair ewe lambs: Oxidative status, feedlot performance, carcass traits and meat quality. Meat Science, v. 173, p. 108395, 2021. DOI: https://doi.org/10.1016/j.meatsci.2020.108395. DOI: https://doi.org/10.1016/j.meatsci.2020.108395

BAI, Y. et al. Phosphorylation of Calpastatin Negatively Regulates the Activity of Calpain. Life (Basel, Switzerland), v. 13, n. 3, p. 854, 2023. DOI: https://doi.org/10.3390/life13030854. DOI: https://doi.org/10.3390/life13030854

PFLANZER, S. B.; GOMES, C. L.; FELÍCIO, P. E. D. O resfriamento tardio da carcaça melhora a maciez do músculo glúteo médio bovino. Pesquisa Agropecuá-ria Brasileira, v. 54, 2019. DOI: https://doi.org/10.1590/s1678-3921.pab2019.v54.00099

BRIDI, A. M.; CONSTANTINO, C.; TARSITANO, M. A. Qualidade da carne de bovino produzida em pasto. In: SIMPÓSIO DE PRODUÇÃO ANIMAL À PASTO, 1. Anais... [s.l.: s.n.], p. 311-332, 2011.

SILVA, P. C. G. et al. Carcass traits and meat quality of Texel lambs raised in Bra-chiaria pasture and feedlot systems. Animal Science Journal = Nihon Chikusan Gakkaiho, v. 91, n. 1, p. e13394, 2020. DOI: https://doi.org/10.1111/asj.13394. DOI: https://doi.org/10.1111/asj.13394

LYU, J.; ERTBJERG, P. Ca2+-induced binding of calpain-2 to myofibrils: Prelimi-nary results in pork longissimus thoracis muscle supporting a role on myofibrillar protein degradation. Meat Science, v. 172, p. 108364, 2021. DOI: https://doi.org/10.1016/j.meatsci.2020.108364 DOI: https://doi.org/10.1016/j.meatsci.2020.108364

WANG, D. et al. Changes in actomyosin dissociation and endogenous enzyme ac-tivities during heating and their relationship with duck meat tenderness. Food Chemistry, v. 141, n. 2, p. 675–679, 2013. DOI: https://doi.org/10.1016/j.foodchem.2013.04.034. DOI: https://doi.org/10.1016/j.foodchem.2013.04.034

CUI, W. et al. Free fatty acid induces endoplasmic reticulum stress and apoptosis of β-cells by Ca2+/calpain-2 pathways. PloS One, v. 8, n. 3, p. e59921, 2013. DOI: https://doi.org/10.1371/journal.pone.0059921

SORIMACHI, H.; HATA, S.; ONO, Y. Impact of genetic insights into calpain biol-ogy. Journal of Biochemistry, v. 150, n. 1, p. 23–37, 2011. DOI: https://doi.org/10.1093/jb/mvr070. DOI: https://doi.org/10.1093/jb/mvr070

LAFITA-NAVARRO, M. D. C.; CONACCI-SORRELL, M. Identification of Cal-pain-Activated Protein Functions. In: Methods in Molecular Biology (Clifton, N.J.). New York: Springer, 2019, v. 1915, p. 149–160. DOI: https://doi.org/10.1007/978-1-4939-8988-1_12 DOI: https://doi.org/10.1007/978-1-4939-8988-1_12

KOOHMARAIE, M. The role of Ca2+-dependent proteases (calpains) in post mor-tem proteolysis and meat tenderness. Biochimie, v. 74, n. 3, p. 239–245, 1992. DOI: https://doi.org/10.1016/0300-9084(92)90122-U DOI: https://doi.org/10.1016/0300-9084(92)90122-U

GAYA, L. G.; FERRAZ, J. B. S. Aspectos genético-quantitativos da qualidade da carne em frangos. Ciência Rural, v. 36, n. 1, p. 349–356, 2006. DOI: https://doi.org/10.1590/S0103-84782006000100058. DOI: https://doi.org/10.1590/S0103-84782006000100058

HUFF LONERGAN, E.; ZHANG, W.; LONERGAN, S. M. Biochemistry of post-mortem muscle — Lessons on mechanisms of meat tenderization. Meat Science, v. 86, n. 1, p. 184–195, 2010. DOI: https://doi.org/10.1016/j.meatsci.2010.05.004. DOI: https://doi.org/10.1016/j.meatsci.2010.05.004

KANAWA, R.; JI, J. R.; TAKAHASHI, K. Inactivity of μ-Calpain Throughout Postmortem Aging of Meat. Journal of Food Science, v. 67, n. 2, p. 635–638, 2002. DOI: https://doi.org/10.1111/j.1365-2621.2002.tb10651.x DOI: https://doi.org/10.1111/j.1365-2621.2002.tb10651.x

SACCÀ, E.; CORAZZIN, M.; BOVOLENTA, S.; PIASENTIER, E. Meat quality traits and the expression of tenderness-related genes in the loins of young goats at different ages. Animal, v. 13, n. 10, p. 2419–2428, 2019. DOI: https://doi.org/10.1017/S1751731119000405. DOI: https://doi.org/10.1017/S1751731119000405

GOLL, D. E. et al. Myofibrillar protein turnover: the proteasome and the calpains. Journal of Animal Science, v. 86, n. suppl_14, p. E19-E35, 2008. DOI: https://doi.org/10.2527/jas.2007-0395. DOI: https://doi.org/10.2527/jas.2007-0395

RAYNAUD, P. et al. Correlation between bovine calpastatin mRNA transcripts and protein isoforms. Archives of Biochemistry and Biophysics, v. 440, n. 1, p. 46-53, 2005. DOI: https://doi.org/10.1016/j.abb.2005.05.028 DOI: https://doi.org/10.1016/j.abb.2005.05.028

FRAYSSE, B. et al. Fiber type-related changes in rat skeletal muscle calcium ho-meostasis during aging and restoration by growth hormone. Neurobiology of Dis-ease, v. 21, n. 2, p. 372-380, 2006. DOI: https://doi.org/10.1016/j.nbd.2005.07.012. DOI: https://doi.org/10.1016/j.nbd.2005.07.012

DE BRITO, Gerlane F.; PONNAMPALAM, Eric N.; HOPKINS, David L. The effect of extensive feeding systems on growth rate, carcass traits, and meat quality of fin-ishing lambs. Comprehensive Reviews in Food Science and Food Safety, v. 16, n. 1, p. 23-38, 2017. DOI: https://doi.org/10.1111/1541-4337.12230 DOI: https://doi.org/10.1111/1541-4337.12230

RUBIO LOZANO, M. S.; NGAPO, T. M.; HUERTA-LEIDENZ, N. Tropical Beef: Is There an Axiomatic Basis to Define the Concept?. Foods (Basel, Switzerland), v. 10, n. 5, p. 1025, 2021. DOI: https://doi.org/10.3390/foods10051025. DOI: https://doi.org/10.3390/foods10051025

FERNANDES, M. H. M. R. et al. Human-edible protein contribution of tropical beef cattle production systems at different levels of intensification. Animal : an in-ternational journal of animal bioscience, v. 16, Suppl 3, p. 100538, 2022. DOI: https://doi.org/10.1016/j.animal.2022.100538. DOI: https://doi.org/10.1016/j.animal.2022.100538

CORIA, M. S. et al. Feeding strategies alter gene expression of the calpain system and meat quality in the longissimus muscle of Braford steers. Asian-Australasian Journal of Animal Sciences, v. 33, n. 5, p. 753, 2020. DOI: https://doi.org/10.5713/ajas.19.0163. DOI: https://doi.org/10.5713/ajas.19.0163

ZAREIAN JAHROMI, E. et al. Allelic Polymorphism of Calpastatin Gene (CAST) in Khalkhali Goats: A Possible Marker for Meat Tenderness. Iranian Journal of Applied Animal Science, v. 5, n. 4, p. 605–909, 2015. Disponível em: http://ijas.iaurasht.ac.ir/article_516542.html.

HUANG, Z. et al. Selenoprotein K Is a Novel Target of m-Calpain, and Cleavage Is Regulated by Toll-like Receptor-induced Calpastatin in Macrophages. Journal of Biological Chemistry, v. 286, n. 40, p. 34830–34838, 2011. DOI: https://doi.org/10.1074/jbc.M111.265520. DOI: https://doi.org/10.1074/jbc.M111.265520

QUREISCHI, M. et al. mRNA-based therapies: Preclinical and clinical applica-tions. International Review of Cell and Molecular Biology, v. 372, p. 1–54, 2022. DOI: https://doi.org/10.1016/bs.ircmb.2022.04.007 DOI: https://doi.org/10.1016/bs.ircmb.2022.04.007

GENTRY, R. C. et al. The mechanism of mRNA activation. bioRxiv : the preprint server for biology, 2023. DOI: https://doi.org/10.1101/2023.11.15.567265. DOI: https://doi.org/10.1101/2023.11.15.567265

MORGAN, J. B. et al. Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers. Journal of Animal Science, v. 71, n. 6, p. 1471–1476, 1993. DOI: https://doi.org/10.2527/1993.7161471x DOI: https://doi.org/10.2527/1993.7161471x

OTSUKA, Y.; GOLL, D. E. Purificação do inibidor de proteinase dependente de Ca++ do músculo cardíaco bovino e sua interação com a proteinase dependente de Ca++ milimolar. Diário do Biológico Chemistry, v. 262, p. 5839–5851, 1987.

GERI, C. et al. Arabidopsis mutants that suppress the phenotype induced by transgene-mediated expression of cauliflower mosaic virus (CaMV) gene VI are less susceptible to CaMV-infection and show reduced ethylene sensitivity. Plant Molecular Biology, v. 56, p. 111-124, 2004. DOI: https://doi.org/10.1007/s11103-004-2649-x. DOI: https://doi.org/10.1007/s11103-004-2649-x

CARLSON, K. B. et al. Postmortem protein degradation is a key contributor to fresh pork loin tenderness. Journal of Animal Science, v. 95, n. 4, p. 1574-1586, 2017. DOI: https://doi.org/10.2527/jas.2016.1032. DOI: https://doi.org/10.2527/jas.2016.1032

KIM, Y. H. B. et al. Understanding postmortem biochemical processes and post-harvest aging factors to develop novel smart-aging strategies. Meat Science, v. 144, p. 74–90, 2018. DOI: https://doi.org/10.1016/j.meatsci.2018.04.031 DOI: https://doi.org/10.1016/j.meatsci.2018.04.031

CHEN, L. et al. Effects of camptothecin, etoposide and Ca2+ on caspase-3 activity and myofibrillar disruption of chicken during postmortem ageing. Meat Science, v. 87, n. 3, p. 165-174, 2011. DOI: https://doi.org/10.1016/j.meatsci.2010.10.002. DOI: https://doi.org/10.1016/j.meatsci.2010.10.002

CHOUDHARY, G. S.; AL-HARBI, S.; ALMASAN, A. Caspase-3 activation is a critical determinant of genotoxic stress-induced apoptosis. In: METHODS IN MOLECULAR BIOLOGY (CLIFTON, N.J.), 1219, p. 1-9, 2015. DOI: https://doi.org/10.1007/978-1-4939-1661-0_1. DOI: https://doi.org/10.1007/978-1-4939-1661-0_1

NGUYEN, T. T. M.; GILLET, G.; POPGEORGIEV, N. Caspases in the Developing Central Nervous System: Apoptosis and Beyond. Frontiers in Cell and Develop-mental Biology, v. 9, p. 702404, 2021. DOI: https://doi.org/10.3389/fcell.2021.702404 DOI: https://doi.org/10.3389/fcell.2021.702404

MCILWAIN, D. R.; BERGER, T.; MAK, T. W. Caspase Functions in Cell Death and Disease. Cold Spring Harbor Perspectives in Biology, v. 5, n. 4, a008656, 2013. DOI: https://doi.org/10.1101/cshperspect.a00865 DOI: https://doi.org/10.1101/cshperspect.a008656

GUILLEMIN, N. et al. Functional analysis of beef tenderness. Journal of Prote-omics, v. 75, n. 2, p. 352-365, 2011. DOI: https://doi.org/10.1016/j.jprot.2011.07.026. DOI: https://doi.org/10.1016/j.jprot.2011.07.026

LOPPNOW, H.; GUZIK, K.; PRYJMA, J. The Role of Caspases in Modulating Cy-tokines and Other Molecules in Apoptosis and Inflammation. In: Madame Curie Bioscience Database [Internet]. Landes Bioscience, 2013. Disponível em: https://www.ncbi.nlm.nih.gov/books/NBK6184/. Acesso em: [data de acesso].

CHUA, B. T.; GUO, K.; LI, P. Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. Journal of Biological Chemistry, v. 275, n. 7, p. 5131-5135, 2000. DOI: https://doi.org/10.1074/jbc.275.7.5131. DOI: https://doi.org/10.1074/jbc.275.7.5131

NAKAGAWA, T.; YUAN, J. Cross-Talk between Two Cysteine Protease Families. Journal of Cell Biology, v. 150, n. 4, p. 887–894, 2000. DOI: https://doi.org/10.1083/jcb.150.4.887 DOI: https://doi.org/10.1083/jcb.150.4.887

WANG, K. K. W. et al. Caspase-Mediated Fragmentation of Calpain Inhibitor Pro-tein Calpastatin during Apoptosis. Archives of Biochemistry and Biophysics, v. 356, n. 2, p. 187–196, 1998. DOI: https://doi.org/10.1006/abbi.1998.0748. DOI: https://doi.org/10.1006/abbi.1998.0748

FUENTE-GARCÍA, C. et al. Caspase activity in post mortem muscle and its rela-tion to cattle handling practices. Journal of the Science of Food and Agriculture, v. 101, n. 15, p. 6258–6264, 2021. DOI: https://doi.org/10.1002/jsfa.11293. DOI: https://doi.org/10.1002/jsfa.11293

DÍAZ-LUIS, A. et al. Nuevos indicadores de carnes DFD: estrés oxidativo, autofa-gia y apoptosis. Informacion Tecnica Economica Agraria. 2020. DOI: https://doi.org/10.12706/itea.2020.006. DOI: https://doi.org/10.12706/itea.2020.006

GUILLEMIN, N. et al. Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type. Animal, v. 5, n. 6, p. 885–894, 2011. DOI: https://doi.org/10.1017/S1751731110002612. DOI: https://doi.org/10.1017/S1751731110002612

PICARD, B.; GAGAOUA, M. Proteomic Investigations of Beef Tenderness. In: Proteomics in Food Science. Amsterdam: Elsevier, 2017. p. 177–197. DOI: https://doi.org/10.1016/B978-0-12-804007-2.00011-4 DOI: https://doi.org/10.1016/B978-0-12-804007-2.00011-4

ROMANOWSKI, T.; MARKIEWICZ, A.; BEDNARZ, N.; BIELAWSKI, K. P. Maintenance genes as a reference in real-time quantitative RT-PCR. Postępy Hi-gieny i Medycyny Doświadczalnej, v. 28, n. 61, p. 500–510, 2007. PMID: 17909518.

KOZERA, B.; RAPACZ, M. Reference genes in real-time PCR. Journal of Applied Genetics, v. 54, n. 4, p. 391–406, 2013. DOI: https://doi.org/10.1007/s13353-013-0173-x

CHERVONEVA, I. et al. Selection of optimal reference genes for normalization in quantitative RT-PCR. BMC Bioinformatics, v. 11, p. 253, 2010. DOI: https://doi.org/10.1186/1471-2105-11-253. DOI: https://doi.org/10.1186/1471-2105-11-253

SILVA, Isabella G. et al. Different nutritional systems influence the tenderness and lipid oxidation of ewe lamb meat without altering gene expression. Anais da Aca-demia Brasileira de Ciências, v. 95, n. suppl 2, p. e20220562, 2023. DOI: https://doi.org/10.1590/0001-3765202320220562

SALWAY, J. Metabolism at a Glance. 4. ed. New York: John Wiley & Sons, 2017.

LIN, Y. W.; WANG, J. Structure and function of heme proteins in non-native states: A mini-review. Journal of Inorganic Biochemistry, v. 129, p. 162–171, 2013. DOI: https://doi.org/10.1016/j.jinorgbio.2013.07.023 DOI: https://doi.org/10.1016/j.jinorgbio.2013.07.023

HUNDALL, S. D. Ferro, Heme e Hemoglobina. In: EM HEMATOLOGIA: UMA ABORDAGEM FISIOPATOLÓGICA. Elsevier, 2011. p. 17–25.

DYNLACHT, B. D.; HOEY, T.; TJIJAN, R. Isolation of coactivators associated with the TATA-binding protein that mediate transcriptional activation. Cell, v. 66, n. 3, p. 563–576, 1991. DOI: https://doi.org/10.1016/0092-8674(81)90019-2. DOI: https://doi.org/10.1016/0092-8674(81)90019-2

Downloads

Publicado

2024-10-16

Edição

Seção

Ciências Agrárias

Categorias

Como Citar

GUARTIERI DA SILVA, Isabella et al. Abundância de RNA do sistema calpaínas-calpastatina, genes relacionados à qualidade da carne de ruminantes: uma revisão. Revista Sociedade Científica, [S. l.], v. 7, n. 1, p. 4796–4825, 2024. DOI: 10.61411/rsc202481517. Disponível em: https://journal.scientificsociety.net/index.php/sobre/article/view/815.. Acesso em: 22 jun. 2026.