Skeletal muscle fiber type and myofibrillar proteins in relation to meat quality

Meat Science

Volumn 86, Issue 1, 2010, Pages 166-170

  Lee, S H ^a   Joo, S T ^b   Ryu, Y C ^c  

^a Korea University   (South Korea)

^b Gyeongsang National University   (South Korea)

^c Jeju National University   (South Korea)

Author keywords

Meat quality; Muscle fiber type; Myofibrillar protein; Proteasome

Indexed keywords

ISOPROTEIN; MUSCLE PROTEIN; PROTEASOME;

ANIMAL; CLASSIFICATION; DOMESTIC ANIMAL; MEAT; METABOLISM; MUSCLE FIBRIL; PHYSIOLOGY; QUALITY CONTROL; REVIEW; SKELETAL MUSCLE;

ANIMALS; ANIMALS, DOMESTIC; MEAT; MUSCLE FIBERS, SKELETAL; MUSCLE PROTEINS; MYOFIBRILS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN ISOFORMS; QUALITY CONTROL;

ANIMALIA;

EID: 77954385411     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2010.04.040     Document Type: Review

References (76)

1. Baker D.M., Santer R.M. Development of a quantitative histochemical method for determination of succinate-dehydrogenase activity in autonomic neurons and its application to the study of aging in the autonomic nervous-system. Journal of Histochemistry & Cytochemistry 1990, 38:525-531.
2. Bee G. Effect of early gestation feeding, birth weight, and gender of progeny on muscle fiber characteristics of pigs at slaughter. Journal of Animal Science 2004, 82:826-836.
3. Bond J.J., Warner R.D. Ion distribution and protein proteolysis affect water holding capacity of longissimus thoracis et lumborum in meat of lamb subjected to antemortem exercise. Meat Science 2007, 75:406-414.
4. Bottinelli R. Functional heterogeneity of mammalian single muscle fibres: Do myosin isoforms tell the whole story?. Pflugers Arch 2001, 443:6-17.
5. Bottinelli R., Reggiani C. Human skeletal muscle fibres: Molecular and functional diversity. Progress in Biophysics & Molecular Biology 2000, 73:195-262.
6. Brocks L., Klont R.E., Buist W., de Greef K., Tieman M., Engel B. The effects of selection of pigs on growth rate vs leanness on histochemical characteristics of different muscles. Journal of Animal Science 2000, 78:1247-1254.
7. Brooke M.H., Kaiser K.K. Muscle fiber types - How many and what kind. Archives of Neurology 1970, 23:369-379.
8. Candek-Potokar M., Lefaucheur L., Zlender B., Bonneau M. Effect of slaughter weight and/or age on histological characteristics of pig longissimus dorsi muscle as related to meat quality. Meat Science 1999, 52:195-203.
9. Candek-Potokar M., Zlender B., Lefaucheur L., Bonneau M. Effects of age and/or weight at slaughter on longissimus dorsi muscle: Biochemical traits and sensory quality in pigs. Meat Science 1998, 48:287-300.
10. Cerisuelo A., Sala R., Nurnberg G., Baucells M., Rehfeldt C. How many muscle samples are required to obtain reliable estimations of muscle fibre characteristics from pig longissimus muscle?. Meat Science 2007, 76:583-587.
11. Chang K.C., da Costa N., Blackley R., Southwood O., Evans G., Plastow G., et al. Relationships of myosin heavy chain fibre types to meat quality traits in traditional and modern pigs. Meat Science 2003, 64:93-103.
12. Choe J.H., Choi Y.M., Lee S.H., Shin H.G., Ryu Y.C., Hong K.C., et al. The relation between glycogen, lactate content and muscle fiber type composition, and their influence on postmortem glycolytic rate and pork quality. Meat Science 2008, 80:355-362.
13. Choi Y.M., Kim B.C. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality. Livestock Science 2009, 122:105-118.
14. Choi Y.M., Ryu Y.C., Kim B.C. Influence of myosin heavy- and light chain isoforms on early postmortem glycolytic rate and pork quality. Meat Science 2007, 76:281-288.
15. Ciechanover A., Orian A., Schwartz A.L. Ubiquitin-mediated proteolysis: Biological regulation via destruction. Bioessays 2000, 22:442-451.
16. Dahlmann B., Kuehn L. The 20S/26S proteasomal pathway of protein degradation in muscle tissue. Molecular Biology Reports 1995, 21:57-62.
17. Dahlmann B., Ruppert T., Kloetzel P.M., Kuehn L. Subtypes of 20S proteasomes from skeletal muscle. Biochimie 2001, 83:295-299.
18. Depreux F.F.S., Grant A.L., Gerrard D.E. Influence of halothane genotype and body-weight on myosin heavy chain composition in pig muscle as related to meat quality. Livestock Production Science 2002, 73:265-273.
19. Dubowitz V., Pearse A.G.E. Reciprocal relationship of phosphorylase and oxidative enzymes in skeletal muscle. Nature 1960, 185:701-702.
20. Dwyer C.M., Fletcher J.M., Stickland N.C. Muscle cellularity and postnatal growth in the pig. Journal of Animal Science 1993, 71:3339-3343.
21. Ennion S., Sant' Ana Pereira J., Sargeant A.J., Young A., Goldspink G. Characterization of human skeletal muscle fibres according to the myosin heavy chains they express. Journal of Muscle Research and Cell Motility 1995, 16:35-43.
22. Fiedler I., Ender K., Wicke M., Maak S., von Lengerken G., Meyer W. Structural and functional characteristics of muscle fibres in pigs with different malignant hyperthermia susceptibility (MHS) and different meat quality. Meat Science 1999, 53:9-15.
23. Fiedler I., Kuchenmeister U., Ender K., Wicke M., Lengerken G. Fiber-type characteristics and meat quality in longissimus muscle of normal and halothane sensitive pigs. Journal of Muscle Research and Cell Motility 1994, 15:187-188.
24. Florini J.R., Ewton D.Z., Coolican S.A. Growth hormone and the insulin-like growth factor system in myogenesis. Endocrine Reviews 1996, 17:481-517.
25. Forster A., Hill C.P. Proteasome degradation: Enter the substrate. Trends in Cell Biology 2003, 13:550-553.
26. Fry A., Allemeier C., Staron R. Correlation between percentage fiber type area and myosin heavy chain content in human skeletal muscle. European Journal of Applied Physiology and Occupational Physiology 1994, 68:246-251.
27. Goll D.E., Neti G., Mares S.W., Thompson V.F. Myofibrillar protein turnover: The proteasome and the calpains. Journal of Animal Science 2008, 86:E19-E35.
28. Handel S.E., Stickland N.C. Catch-up growth in pigs - A relationship with muscle cellularity. Animal Production 1988, 47:291-295.
29. Henckel P., Oksbjerg N., Erlandsen E., Barton-Gade P., Bejerholm C. Histo- and biochemical characteristics of the longissimus dorsi muscle in pigs and their relationships to performance and meat quality. Meat Science 1997, 47:311-321.
30. Highley J.R., Esiri M.M., McDonald B., Roberts H.C., Walker M.A., Crow T.J. The size and fiber composition of the anterior commissure with respect to gender and schizophrenia. Biological Psychiatry 1999, 45:1120-1127.
31. Houbak M.B., Ertbjerg P., Therkildsen M. In vitro study to evaluate the degradation of bovine muscle proteins post-mortem by proteasome and [mu]-calpain. Meat Science 2008, 79:77-85.
32. Huff-Lonergan E., Mitsuhashi T., Beekman D.D., Parrish F.C., Olson D.G., Robson R.M. Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. Journal of Animal Science 1996, 74:993-1008.
33. Joo S.T., Kauffman R.G., Kim B.C., Park G.B. The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Science 1999, 52:291-297.
34. Jurie C., Picard B., Geay Y. Changes in the metabolic and contractile characteristics of muscle in male cattle between 10 and 16months of age. The Histochemical Journal 1999, 31:117-122.
35. Karlsson A., Enfalt A.C., Essengustavsson B., Lundstrom K., Rydhmer L., Stern S. Muscle histochemical and biochemical-properties in relation to meat quality during selection for increased lean tissue-growth rate in pigs. Journal of Animal Science 1993, 71:930-938.
36. Karlsson A.H., Klont R.E., Fernandez X. Skeletal muscle fibres as factors for pork quality. Livestock Production Science 1999, 60:255-269.
37. Kim J.M., Lee Y.J., Choi Y.M., Kim B.C., Yoo B.H., Hong K.C. Possible muscle fiber characteristics in the selection for improvement in porcine lean meat production and quality. Asian-Australasian Journal of Animal Sciences 2008, 21:1529-1534.
38. Klont R.E., Brocks L., Eikelenboom G. Muscle fibre type and meat quality. Meat Science 1998, 49:S219-S229.
39. Koohmaraie M. Ovine skeletal-muscle multicatalytic proteinase complex (proteasome) - Purification, characterization, and comparison of its effects on myofibrils with mu-calpains. Journal of Animal Science 1992, 70:3697-3708.
40. Koohmaraie M. Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science 1996, 43:S193-S201.
41. Larzul C., Le Roy P., Gogue J., Talmant A., Jacquet B., Lefaucheur L., et al. Selection for reduced muscle glycolytic potential in Large White pigs. II. Correlated responses in meat quality and muscle compositional traits. Genetics, Selection, Evolution 1999, 31:61-76.
42. Larzul C., Lefaucheur L., Ecolan P., Gogue J., Talmant A., Sellier P., et al. Phenotypic and genetic parameters for longissimus muscle fiber characteristics in relation to growth, carcass, and meat quality traits in large white pigs. Journal of Animal Science 1997, 75:3126-3137.
43. Lefaucheur L. A second look into fibre typing - Relation to meat quality. Meat Science 2010, 84:257-270.
44. Li X., Yang X., Shan B., Shi J., Xia D., Wegner J., et al. Meat quality is associated with muscle metabolic status but not contractile myofiber type composition in premature pigs. Meat Science 2009, 81:218-223.
45. Lind A., Kernell D. Myofibrillar ATPase histochemistry of rat skeletal muscles: A "two-dimensional" quantitative approach. Journal of Histochemistry & Cytochemistry 1991, 39:589-597.
46. Maltin C., Balcerzak D., Tilley R., Delday M. Determinants of meat quality: Tenderness. The Proceedings of the Nutrition Society 2003, 62:337-347.
47. Maltin C.A., Sinclair K.D., Warriss P.D., Grant C.M., Porter A.D., Delday M.I., et al. The effects of age at slaughter, genotype and finishing system on the biochemical properties, muscle fibre type characteristics and eating quality of bull beef from suckled calves. Animal Science 1998, 66:341-348.
48. Maltin C.A., Warkup C.C., Matthews K.R., Grant C.M., Porter A.D., Delday M.I. Pig muscle fibre characteristics as a source of variation in eating quality. Meat Science 1997, 47:237-248.
49. Ouali A., Talmant A. Calpains and calpastatin distribution in bovine, porcine and ovine skeletal-muscles. Meat Science 1990, 28:331-348.
50. Ozawa S., Mitsuhashi T., Mitsumoto M., Matsumoto S., Itoh N., Itagaki K., et al. The characteristics of muscle fiber types of longissimus thoracis muscle and their influences on the quantity and quality of meat from Japanese Black steers. Meat Science 2000, 54:65-70.
51. Peter J.B., Gillespi.Ca, Barnard R.J., Stempel K.E., Edgerton V.R. Metabolic profiles of 3 fiber types of skeletal-muscle in guinea-pigs and rabbits. Biochemistry 1972, 11:2627-2633.
52. Pette D., Staron R.S. Transitions of muscle fiber phenotypic profiles. Histochemistry and Cell Biology 2001, 115:359-372.
53. Rahelic S., Puac S. Fiber types in longissimus-dorsi from wild and highly selected pig breeds. Meat Science 1981, 5:439-450.
54. Rechsteiner M., Hill C.P. Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors. Trends in Cell Biology 2005, 15:27-33.
55. Rehfeldt C., Fiedler I., Dietl G., Ender K. Myogenesis and postnatal skeletal muscle cell growth as influenced by selection. Livestock Production Science 2000, 66:177-188.
56. Rehfeldt C., Kuhn G. Consequences of birth weight for postnatal growth performance and carcass quality in pigs as related to myogenesis. Journal of Animal Science 2006, 84:E113-E123.
57. Rehfeldt C., Tuchscherer A., Hartung M., Kuhn G. A second look at the influence of birth weight on carcass and meat quality in pigs. Meat Science 2008, 78:170-175.
58. Rivero J.L.L., Talmadge R.J., Edgerton V.R. A sensitive electrophoretic method for the quantification of myosin heavy chain isoforms in horse skeletal muscle: Histochemical and immunocytochemical verifications. Electrophoresis 1997, 18:1967-1972.
59. Robert N., Briand M., Taylor R., Briand Y. The effect of proteasome on myofibrillar structures in bovine skeletal muscle. Meat Science 1999, 51:149-153.
60. Ruusunen M., Puolanne E. Comparison of histochemical properties of different pig breeds. Meat Science 1997, 45:119-125.
61. Ryu Y.C., Choi Y.M., Lee S.H., Shin H.G., Choe J.H., Kim J.M., et al. Comparing the histochemical characteristics and meat quality traits of different pig breeds. Meat Science 2008, 80:363-369.
62. Ryu Y.C., Kim B.C. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Science 2005, 71:351-357.
63. Ryu Y.C., Lee M.H., Lee S.K., Kim B.C. Effect of muscle mass and fiber type composition of longissimus dorsi muscle on postmortem metabolic rate and meat quality in pigs. Journal of Muscle Foods 2006, 17:343-353.
64. Schiaffino S., Gorza L., Sartore S., Saggin L., Ausoni S., Vianello M., et al. Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. Journal of Muscle Research and Cell Motility 1989, 10:197-205.
65. Schiaffino S., Reggiani C. Molecular diversity of myofibrillar proteins: Gene regulation and functional significance. Physiological Reviews 1996, 76:371-423.
66. Seideman S.C., Crouse J.D. The effects of sex condition, genotype and diet on bovine muscle fiber characteristics. Meat Science 1986, 17:55-72.
67. Sentandreu M.A., Coulis G., Ouali A. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends in Food Science & Technology 2002, 13:400-421.
68. Smerdu V., Karsch-Mizrachi I., Campione M., Leinwand L., Schiaffino S. Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle. The American Journal of Physiology 1994, 267:C1723-C1728.
69. Solomon V., Goldberg A.L. Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. The Journal of Biological Chemistry 1996, 271:26690-26697.
70. Stephenson G.M. Hybrid skeletal muscle fibres: A rare or common phenomenon? Clinical and Experimental Pharmacology & Physiology 2001, 28:692-702.
71. Taber L.A. Biomechanical growth laws for muscle tissue. Journal of Theoretical Biology 1998, 193:201-213.
72. Talmadge R.J. Myosin heavy chain isoform expression following reduced neuromuscular activity: Potential regulatory mechanisms. Muscle & Nerve 2000, 23:661-679.
73. Talmadge R.J., Roy R.R., Edgerton V.R. Prominence of myosin heavy-chain hybrid fibers in soleus muscle of spinal cord-transected rats. Journal of Applied Physiology 1995, 78:1256-1265.
74. Taylor R.G., Geesink G.H., Thompson V.F., Koohmaraie M., Goll D.E. Is Z-disk degradation responsible for postmortem tenderization. Journal of Animal Science 1995, 73:1351-1367.
75. Taylor R.G., Tassy C., Briand M., Robert N., Briand Y., Ouali A. Proteolytic activity of proteasome on myofibrillar structures. Molecular Biology Reports 1995, 21:71-73.
76. Xiong Y.L., Mullins O.E., Stika J.F., Chen J., Blanchard S.P., Moody W.G. Tenderness and oxidative stability of post-mortem muscles from mature cows of various ages. Meat Science 2007, 77:105-113.