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Journals / Kafkas Üniversitesi Veteriner Fakültesi Dergisi / 2018 / Cilt: 24 - Sayı: 5

Differential Expression of Proteins in Datong Yak and Chaidamu Yellow Cattle Longissimus lumborum Muscles and Relation to Meat Water Holding Capacity

Datong Yak ve Chaidamu Sarı Sığırı Longissimus lumborum Kasında Proteinlerin Farklı Ekspresyonu ve Etin Su Tutma Kapasitesi İle İlişkisi

Jianlei JIA
Qinwen ZHANG
Hongjian ZHANG
Fangming LIN
Jing ZHAO
Qian CHENG
Pages
691–700
Publication Date
2022-10-18
DOI
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

The functions ofthe identified proteins contribute to a more detailed molecular view of the processes behind WHC and are a valuable resource for futureinvestigations.

📌 3 Key Takeaways

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Objective & Hypothesis:We investigated that proteins differently expressed in Datong Yak and Chaidamu Yellow Cattle Longissimus longurum muscles and theirrelation to tissue water-holding capacity.
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Key Findings & Data:Samples were classified according to breed and postmortem aging into Yak0h, Cattle0h,Yak24h and Cattle24h groups.
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Conclusion & Impact:The functions ofthe identified proteins contribute to a more detailed molecular view of the processes behind WHC and are a valuable resource for futureinvestigations.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

We investigated that proteins differently expressed in Datong Yak and Chaidamu Yellow Cattle Longissimus longurum muscles and theirrelation to tissue water-holding capacity. Samples were classified according to breed and postmortem aging into Yak0h, Cattle0h,Yak24h and Cattle24h groups. Fifty seven differentially expressed proteins were confirmed by MALDI-TOF/TOF-MS. Twenty eight proteinscould be identified and were divided into five main categories: structural proteins, metabolic enzymes, stress related proteins, transporterproteins and binding proteins. Myosin light chain (MLC), Heat Shock 27kDa (HSP 27) and Keratin 10 (KRT 10) proteins showed significantdifferences in expression between yak and cattle meat and may have the potential to be used as biological markers of tissue WHC.Bioinformatics analysis showed differentially these proteins included both metabolic enzymes and structural proteins. The functions ofthe identified proteins contribute to a more detailed molecular view of the processes behind WHC and are a valuable resource for futureinvestigations.

Özet

Bu çalışmada Datong Yak ve Chaidamu Sarı Sığırı Longissimus lumborum kasında proteinlerin farklı ekspresyonu ve bu proteinlerin etin su tutma kapasitesi ile ilişkisi araştırılmıştır. Örnekler ırka ve postmortem yaşlanmaya göre sınıflandırıldı (Yak0h, Cattle0h, Yak24h ve Cattle24h). Elli yedi farklı eksprese edilen protein MALDI-TOF/TOF-MS ile onaylandı. Yirmi sekiz protein tanımlanarak yapısal proteinler, metabolik enzimler, stres ilişkili proteinler, taşıyıcı proteinler ve bağlayıcı proteinler olmak üzere beş ana kategoriye ayrıldı. Myosin hafif zincir, Isı şok 27kDa (HSP 27) ve Keratin 10 proteinlerinin yak ve sığır etleri arasında ekspresyon bakımından önemli farklar göstermesi sebebiyle bu proteinlerin doku su tutma kapasitesi için biyolojik marker olarak kullanılabilecekleri kanısına varıldı. Biyoinformatik analizi bu proteinlerin farklı metabolik enzimler ve yapısal proteinleri içerdiğini gösterdi. Tespit edilen proteinlerin fonksiyonları su tutma kapasitesinin arkasında yatan daha derinlemesine moleküler ilişkiye ışık tutmakta ve gelecek araştırmalar için değerli bir kaynak oluşturmaktadır.

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Cite This Article

JIA, J., ZHANG, Q., ZHANG, H., LIN, F., ZHAO, J., CHENG, Q. (2022). Differential Expression of Proteins in Datong Yak and Chaidamu Yellow Cattle Longissimus lumborum Muscles and Relation to Meat Water Holding Capacity. Kafkas Üniversitesi Veteriner Fakültesi Dergisi, Cilt: 24 - Sayı: 5, 691–700. https://ajindex.com/articles/569929

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References (1)

  1. Zheng A, Liu G, Zhang Y, Hou S, Chang W, Zhang S, Cai H, Chen G: Proteomic analysis of liver development of lean Pekin duck (Anas platyrhynchosdomestica).J Proteomics, 75, 5396-5413, 2012. DOI: 10.1016/ j.jprot.2012.06.019 Bendixen E: The use of proteomics in meat science. Meat Sci, 71 (1): 138-149, 2005. DOI: 10.1016/j.meatsci.2005.03.013 Paredi G, Raboni S, Bendixen E, de Almeida AM, Mozzarelli A: “Muscle to meat” molecular events and technological transformations: The proteomics insight. J Proteomics, 75 (14): 4275-4289, 2012. DOI: 10.1016/j.jprot.2012.04.011 Lametsch R, Karlsson A, Rosenvold K, Andersen HJ, Roepstorff P, Bendixen E: Postmortem proteome changes of porcine muscle related to tenderness. J Agric Food Chem, 51 (24): 6992-6997, 2003. DOI: 10.1021/ jf034083p Lo Bello M, Nuccetelli M, Caccuri AM, Stella L, Parker MW, Rossjohn J, McKinstry WJ, Mozzi AF, Federici G, Polizio F, Pedersen JZ, Ricci G: Human glutathione transferase P1-1 and nitric oxide carriers: A new role for an old enzyme. J Biol Chem, 276, 42138-42145, 2001. DOI: 10.1074/jbc.M102344200 Zhang WG, Lonergan SM, Gardner MA, Huff-Lonergan E: Contribution of postmortem changes of integrin, desmin and μ-calpain to variation in water holding capacity of pork. Meat Sci, 74, 578-585, 2006. DOI: 10.1016/j.meatsci.2006.05.008 Van de Wiel DFM, Zhang WL: Identification of pork quality parameters byproteomics. Meat Sci, 77, 46-54, 2007. DOI: 10.1016/j.meatsci. 2007.04.017 Canto AC, Suman SP, Nair MN, Li S, Rentfrow G, Beach CM, Silva TJ, Wheeler TL, Shackelford SD, Grayson A, McKeith RO, King DA: Differential abundance of sarcoplasmic proteome explains animal effect on beef Longissimus lumborum color stability. Meat Sci, 102, 90-98, 2015. DOI: 10.1016/j.meatsci.2014.11.011 Bouley J, Chambon C, Picard B: Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics, 4, 1811-1824, 2004. DOI: 10.1002/pmic.200300688 Jia X, Ekman M, Grove H, Faergestad EM, Aass L, Hildrum KI, Hollung K: Proteome changes in bovine longissimus thoracis muscle during the early postmortem storage period. J Proteome Res, 6, 2720- 2731, 2007. DOI: 10.1021/pr070173o Au Y: The muscle ultrastructure: A structural perspective of the sarcomere. Cell Mol Life Sci, 61, 3016-3033, 2004. DOI: 10.1007/s00018- 004-4282-x Marino R, Albenzio M, della Malva A, Caroprese M, Santillo A, Sevi A: Changes in meat quality traits and sarcoplasmic proteins during aging in three differen