Effects of a myostatin mutation in Japanese quail (Coturnix japonica) on the physicochemical and histochemical characteristics of the pectoralis major muscle

The aim of this study was to compare the carcass, meat quality, and histochemical characteristics of pectoralis major (PM) muscle between wild type (WT) and myostatin (Mstn) homozygous mutant (HO) quail lines. The HO quail line exhibited significantly heavier body weight (HO vs. WT, 115.7 g vs. 106.2 g, approximately 110%) and PM muscle weight (HO vs. WT, 18.0 g vs. 15.2 g, approximately 120%) compared to the WT (p < 0.001). However, the two groups had similar traits (pH, redness, yellowness, and drip loss) for meat quality, although slightly higher lightness and cooking loss were observed in the mutant quail (103% and 141%, respectively, p < 0.05). For histochemical traits of PM muscle, Mstn mutant quail exhibited lower type IIA and higher type IIB percentage in the deep region than WT quail (p < 0.05), indicating a fiber conversion from the type IIA to IIB. However, the two quail lines had comparable histochemical traits in the superficial region (p > 0.05). These data suggest that Mstn mutation greatly increases muscle mass without significantly affecting meat quality.

[1]  Kichoon Lee,et al.  Differential Expression of MSTN Isoforms in Muscle between Broiler and Layer Chickens , 2022, Animals : an open access journal from MDPI.

[2]  Bo-Su Lee,et al.  Research Note: Comparison of histochemical characteristics, chicken meat quality, and heat shock protein expressions between PSE-like condition and white-stripping features of pectoralis major muscle , 2021, Poultry science.

[3]  Gap-Don Kim,et al.  Generation of myostatin‐knockout chickens mediated by D10A‐Cas9 nickase , 2020, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[4]  Kichoon Lee,et al.  Muscle Hyperplasia in Japanese Quail by Single Amino Acid Deletion in MSTN Propeptide , 2020, International journal of molecular sciences.

[5]  J. Burek,et al.  A retrospective analysis of the United States poultry industry: 1965 compared with 2010 , 2017 .

[6]  B. Vernus,et al.  Myostatin deficiency is associated with lipidomic abnormalities in skeletal muscles. , 2017, Biochimica et biophysica acta. Molecular and cell biology of lipids.

[7]  Kui Li,et al.  Loss-of-function myostatin mutation increases insulin sensitivity and browning of white fat in Meishan pigs , 2017, Oncotarget.

[8]  L. Laghi,et al.  Functional property issues in broiler breast meat related to emerging muscle abnormalities , 2016 .

[9]  Kui Li,et al.  Targeted mutations in myostatin by zinc-finger nucleases result in double-muscled phenotype in Meishan pigs , 2015, Scientific Reports.

[10]  R. H. Carvalho,et al.  The incidence of pale, soft, and exudative (PSE) turkey meat at a Brazilian commercial plant and the functional properties in its meat product , 2014 .

[11]  A. Fouad,et al.  Nutritional Factors Affecting Abdominal Fat Deposition in Poultry: A Review , 2014, Asian-Australasian journal of animal sciences.

[12]  Kichoon Lee,et al.  Skeletal Muscle Characterization of Japanese Quail Line Selectively Bred for Lower Body Weight as an Avian Model of Delayed Muscle Growth with Hypoplasia , 2014, PloS one.

[13]  L. Fiems Double Muscling in Cattle: Genes, Husbandry, Carcasses and Meat , 2012, Animals : an open access journal from MDPI.

[14]  Byoung-Chul Kim,et al.  Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality , 2009 .

[15]  P. O’Callaghan,et al.  Myostatin regulates fiber-type composition of skeletal muscle by regulating MEF2 and MyoD gene expression. , 2009, American journal of physiology. Cell physiology.

[16]  M. Georges,et al.  Characterization of the complete porcine MSTN gene and expression levels in pig breeds differing in muscularity. , 2008, Animal genetics.

[17]  S. Velleman,et al.  Genetics of growth and reproduction in the Turkey. 17. Changes in genetic parameters over forty generations of selection for increased sixteen-week body weight. , 2008, Poultry science.

[18]  E. Huff-Lonergan,et al.  Progress in reducing the pale, soft and exudative (PSE) problem in pork and poultry meat. , 2008, Meat science.

[19]  J. E. Edwards,et al.  Evidence for multiple alleles effecting muscling and fatness at the Ovine GDF8 locus , 2007, BMC Genetics.

[20]  S. F. Bilgili,et al.  Comparison of chicken genotypes: myofiber number in pectoralis muscle and myostatin ontogeny. , 2004, Poultry science.

[21]  Se-Jin Lee,et al.  Suppression of body fat accumulation in myostatin-deficient mice. , 2002, The Journal of clinical investigation.

[22]  K. Honikel,et al.  Reference methods for the assessment of physical characteristics of meat. , 1998, Meat science.

[23]  Se-Jin Lee,et al.  Double muscling in cattle due to mutations in the myostatin gene. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[24]  Se-Jin Lee,et al.  Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member , 1997, nature.

[25]  K. Nestor,et al.  Genetics of growth and reproduction in the turkey. 13. Effects of repeated backcrossing of an egg line to two sire lines. , 1997, Poultry science.

[26]  T. Art,et al.  Muscle fibre type and size, and muscle capillary density in young double-muscled blue Belgian cattle. , 1994, Zentralblatt fur Veterinarmedizin. Reihe A.

[27]  J. C. George,et al.  Architecture of the pectoralis muscle of the Japanese quail (Coturnix japonica): histochemical and ultrastructural characterization, and distribution of muscle fiber types , 1987 .