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Association of functional sequence variants of the myosin heavy chain 3 gene with muscle collagen content in pigs

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주제분류축산학

초록

This study examined the association between functional sequence variants (FSVs) of myosin heavy chain 3 (MYH3) genotypes and collagen content in a Landrace and Jeju native pig (JNP) crossbred population. Four muscles (Musculus longissimus dorsi, Musculus semimembranosus, Musculus triceps brachii, and Musculus biceps femoris) were used for the analysis of meat collagen content, and the same animals were genotyped for the FSVs of the MYH3 gene by using PCR-RFLP (polymerase chain reaction-restriction fragment length polymorphism). Three FSVs of MYH3 genotypes were identified and had genotype frequencies of 0.358, 0.551, and 0.091 for QQ, Qq, and qq, respectively. QQ animals for the FSVs of the MYH3 genotypes showed higher collagen content in their M. longissimus dorsi (p < 0.001), M. semimembranosus (p < 0.001), M. triceps brachii (p < 0.001), and M. biceps femoris (p < 0.001) than qq homozygous animals. After the validation of this result in other independent populations, the FSVs of MYH3 genotypes can be a valuable genetic marker for improving collagen content in porcine muscles and can also be applied to increase the amount of collagen for biomedical purposes.

Abstract

This study examined the association between functional sequence variants (FSVs) of myosin heavy chain 3 (MYH3) genotypes and collagen content in a Landrace and Jeju native pig (JNP) crossbred population. Four muscles (Musculus longissimus dorsi, Musculus semimembranosus, Musculus triceps brachii, and Musculus biceps femoris) were used for the analysis of meat collagen content, and the same animals were genotyped for the FSVs of the MYH3 gene by using PCR-RFLP (polymerase chain reaction-restriction fragment length polymorphism). Three FSVs of MYH3 genotypes were identified and had genotype frequencies of 0.358, 0.551, and 0.091 for QQ, Qq, and qq, respectively. QQ animals for the FSVs of the MYH3 genotypes showed higher collagen content in their M. longissimus dorsi (p < 0.001), M. semimembranosus (p < 0.001), M. triceps brachii (p < 0.001), and M. biceps femoris (p < 0.001) than qq homozygous animals. After the validation of this result in other independent populations, the FSVs of MYH3 genotypes can be a valuable genetic marker for improving collagen content in porcine muscles and can also be applied to increase the amount of collagen for biomedical purposes.

참고문헌 (20)

  1. Andersson L, "Molecular consequences of animal breeding", Curr Opin Genet Dev, 23, pp.295~301 (2013)[DOI]
  2. Cho IC, "A functional regulatory variant of MYH3 influences muscle fiber-type composition and intramuscular fat content in pigs", PLOS Genet, 15, pp.e1008279~ (2019)[DOI]
  3. Jongjareonrak A, "Isolation and characterization of collagen from bigeye snapper(Priacanthus macracanthus)skin", J Sci Food Agric, 85, pp.1203~1210 (2005)[DOI]
  4. McCormick RJ, "The flexibility of the collagen compartment of muscle", Meat Sci, 36, pp.79~91 (1994)[DOI]
  5. Nalinanon S, "Use of pepsin for collagen extraction from the skin of bigeye snapper(Priacanthus tayenus)", Food Chem, 104, pp.593~601 (2007)[DOI]
  6. Ogawa M, "Biochemical properties of black drum and sheepshead seabream skin collagen", J Agric Food Chem, 51, pp.8088~8092 (2003)[DOI]
  7. Woo JW, "Extraction optimization and properties of collagen from yellowfin tuna (Thunnus albacares) dorsal skin", Food Hydrocoll, 22, pp.879~887 (2008)[DOI]
  8. Nakamura YN, "Relationship among collagen amount, distribution and architecture in the M. longissimus thoracis and M. pectoralis profundus from pigs", Meat Sci, 64, pp.43~50 (2003)[DOI]
  9. Liu X, "Type III collagen is crucial for collagen I fibrillogenesis and for normal cardiovascular development", Proc Natl Acad Sci, 94, pp.1852~1856 (1997)[DOI]
  10. Maffulli N, "Tenocytes from ruptured and tendinopathic achilles tendons produce greater quantities of Type III collagen than tenocytes from normal achilles tendons : an in vitro model of human tendon healing", Am J Sports Med, 28, pp.499~505 (2000)[DOI]
  11. Ran XG, "Use of ultrasonic and pepsin treatment in tandem for collagen extraction from meat industry by-products", J Sci Food Agric, 94, pp.585~590 (2014)[DOI]
  12. Rizk MA, "Extraction and characterization of collagen from buffalo skin for biomedical applications", Orient J Chem, 32, pp.1601~1609 (2016)[DOI]
  13. Coelho NM, "Discoidin domain receptor 1 interactions with myosin motors contribute to collagen remodeling and tissue fibrosis", Biochim Biophys Acta Mol Cell Res, 1866, pp.118510~ (2019)[DOI]
  14. 서수영, "제주재래흑돼지와 Landrace 교잡돈의 부위별 육질 특성", 농업생명과학연구, 49(5), pp.211~223 (2015), 농업생명과학연구원[DOI]
  15. Sambrook J, "Molecular cloning: a laboratory manual" (1989), Cold Spring Harbor Laboratory
  16. 최영석, "Comparison of Meat Quality and Fatty Acid Composition of Longissimus Muscles from Purebred Pigs and Three-way Crossbred LYD Pigs", 한국축산식품학회지, 36(5), pp.689~696 (2016), 한국축산식품학회
  17. Kalinowski ST, "Revising how the computer program CERVUS accommodates genotyping error increases success in paternity assignment", Mol Ecol, 16, pp.1099~1106 (2007)[DOI]
  18. Kang YJ, "The MYH3 gene variant(g. -1805_-1810, ACGT)affects endophenotypes of myoglobin oxidation–reduction states in porcine muscles", Anim Genet, 53, pp.532~533 (2022)[DOI]
  19. Agarwal M, "Myosin heavy chain-embryonic regulates skeletal muscle differentiation during mammalian development", Development, 147, pp.dev184507~ (2020)[DOI]
  20. Normal probability plots and tests for normality, "Ryan TA Jr", Statistics Department, The Pennsylvania State University, ~ (1976)

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