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Immunohistochemical quantification of fast-myosin in frozen histological sections of goat limb muscles

  • N. Manabe (a1), Y Azuma (a2), Y. Furuya (a1), K. Kuramitsu (a1), Y. Kuribayashi (a1), N. Nagano (a3) and H. Miyamoto (a1)...

Abstract

Fast-myosin in frozen histological sections of eight, 10, 11 and nine muscles of the upper forelimb, lower forelimb, upper hindlimb and lower hindlimb, respectively, of goats was quantified by an immunohistochemical micromethod based on the enzyme-linked immunosorbent assay. The structure of the muscles is well preserved during the immunohistochemical measurement. High fast-myosin levels (more than 201 mg/g total protein) were observed in the triceps brachii (lateral head), rectus femoris, vastus lateralis, semitendinosus, semimembranosus, gastrocnemius (lateral head) and long digital extensor muscles. In contrast, low fast-myosin levels (less than 50 mg/g) were found in the triceps brachii (medial head), superficial digital flexor, vastus intermedialis, and soleus muscles. Fast-myosin-positive fibres (type II or fast-twitch type) were distributed more in the superficial regions than in the deeper regions in the triceps brachii (lateral and long heads), biceps brachii, brachialis, biceps femoris, vastus lateralis, vastus medialis, semimembranosus and gastrocnemius (lateral and medial heads) muscles. In contrast, type IIfibres were distributed more in the deeper regions than in the superficial regions in the extensor carpi radialis, deep digital flexor, cranial tibial, deep digital flexor and superficial digital flexor muscles. When the results obtained by the immunohistochemical micromethod were compared with those obtained by biochemical techniques and by histomorphometrical analyses, high correlations were noted. This technique could be used in research projects to study the muscle characteristics that determine meat quality.

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Ariano, M. A., Armstrong, R. B. and Edgerton, V. R. 1973. Hindlimb muscle fiber populations of five mammals. journal of Histochemistry and Cytochemistry 21: 5155.
Armstrong, R. B. and Phelps, R. O. 1984. Muscle fiber type composition of the rat hindlimb. American journal of Anatomy 171: 256272.
Armstrong, R. B., Saubert, C. W., Seeherman, H. J. and Taylor, C. R. 1982. Distribution of fiber types in locomotory muscles of dogs. American journal of Anatomy 163: 8798.
Azuma, Y., Manabe, N., Kawai, F., Kanamori, M. and Miyamoto, H. 1994a. Phosphorus-31 nuclear magnetic resonance study of energy metabolism in intact slow- and fast-twitch muscles of rats. journal of Animal Science 72: 103108.
Azuma, Y., Manabe, N., Kawai, F., Kanamori, M. and Miyamoto, H. 1994b. Phosphorus-31 nuclear magnetic resonance study of postmortem changes in the intact tissue of goat muscles. Animal Science and Technology 65: 416422.
Bàràny, M., Bàràny, K., Reckard, T. and Volpe, A. 1965. Myosin of fast and slow muscles of the rabbit. Archives of Biochemistry and Biophysics 109: 185191.
Cassens, R. G., Marple, D. N. and Eikelenboom, G. 1975. Animal physiology and meat quality. Advanced Food Research 21: 71155.
d'Albis, A., Panaloni, C. and Bechet, J.-J. 1979a. An electrophoretic study of native myosin isozymes and their subunit content. European journal Biochemistry 99: 261272.
d'Albis, A., Janmot, C. and Bechet, J.-J. 1979b. Comparison of myosins from the masseter muscle of adult rat, mouse and guinea-pig. European journal of Biochemistry 156: 291296.
d'Albis, A., Couteaux, R., Janmot, C. and Roulet, A. 1989. Specific programs of myosin expression in the postnatal development of rat muscles. European journal of Biochemistry 183: 583590.
Essèn-Gustavsson, B., Karlsson, A., Lundström, K. and Enfält, A.-C. 1994. Intramuscular fat and muscle fibre lipid contents in halothane-gene-free pigs fed high or low protein diets and its relations to meat quality. Meat Science 38: 269277.
Goto, T., Iwamoto, H., Ono, Y., Nishimura, S., Matsuo, K., Nakanishi, Y., Umetsu, R. and Takahara, H. 1994. Comparative study on the regional composition of fiber types in M. Longissimus thoracis with different marbling scores for Japanese Black steers. Animal Science and Technology 65: 454463.
Greaser, M. L. 1986. Conversion of muscle to meat. In Muscle as food (ed. Bechtel, P. J.), pp. 37102. Academic Press, Orlando.
Guerret, S., Rojkind, M., Druguet, M., Chevallier, M. and Grimaud, J.-A. 1988. Immunohistochemical micromethods for the measurement of specific collagen types in human liver biopsies. Collagen and Related Research 8: 249258.
Harrington, W. F. and Rogers, M. E. 1984. Myosin. Annual Review of Biochemistry 53: 3573.
Havenith, M. G., Visser, R., Schrijversvanschendel, J. M. C. and Bosman, F. T. 1990. Muscle fiber typing in routinely processed skeletal muscle with monoclonal antibodies. Histochemistry 93: 497499.
Hoh, J. F. Y. 1979. Developmental changes in chicken skeletal muscle myosin isozymes. FEBS Letters 98: 267270.
Hoh, J. F. Y., McGrath, P. A. and White, R. I. 1976. Electrophoretic analysis of multiple forms of myosis in fast-twitch and slow-twitch muscles of the chick. Biochemical Journal 157: 8795.
Karlsson, A., Enfält, A.-C., Essèn-Gustavsson, B., Lundström, K., Rydhmer, L. and Stern, S. 1993. Muscle histochemical and biochemical properties in relation to meat quality during selection for increased lean tissue growth rate in pigs. journal of Animal Science 71: 930938.
Klosowski, B., Bidwell, P. K., Klosowska, D. and Piotrowski, J. 1992. Microstructure of skeletal muscles of growing calves fed silage-based vs hay-based diets. II. Fibre type distribution. Reproduction, Nutrition, Development 32: 257263.
Kyoto University Animal Care Committee. 1990. Guide for the care and use of animals. Kyoto University, Japan.
Lamed, R., Levin, Y. and Oplatka, A. 1973. Enzymatic mechanochemistry. 1. The interaction of heavy meromyosin with “immobilized adenosine triphosphate”. Biochemica el Biophysica Acta 305: 163171.
Lamed, R. and Oplatka, A. 1974. Application of immobilized adenosine triphosphate in the study of myosin. Biochemistry 13: 31373142.
Lòpez de Leòn, A. and Rojkind, M. 1985. A simple micromethod for collagen and total protein determination in formalin-fixed paraffin-embedded sections. journal of Histochemistry and Cytochemistry 33: 737743.
Lowry, O. H., Resebrough, J., Farr, A. L. and Randall, R. J. 1951. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193: 265275.
Manabe, N., Azuma, Y., Furuya, Y., Kuramitsu, K., Nagano, N. and Miyamoto, H. 1995a. Immunohistochemical Microquantification of Fast-Myosin in Frozen Histological Sections of Mammalian Skeletal Muscles. Journal of Animal Science 73: 8895.
Manabe, N., Azuma, Y., Furuya, Y., Kuramitsu, K., Nagano, N. and Miyamoto, H. 1995b. Immunohistochemical quantitation for extracellular matrix proteins in rats with glomerulonephritis induced by monoclonal anti-Thy 1.1 antibody. Nephron 71: 7986.
Manabe, N., Azuma, Y., Furuya, Y., Nagano, N. and Miyamoto, H. 1994a. A new immunohistochemical method for quantification of fast-myosin in frozen histologic sections of the rat skeletal muscles. journal of Veterinary Medical Science 56: 713.
Manabe, N., Chevallier, M., Chossgros, P., Causse, X., Guerret, S., Trèpo, C. and Grimaud, J.-A. 1993b. Interferon-α2b therapy reduces liver fibrosis in chronic nonA, non-B hepatitis: A quantitative histological evaluation. Hepatology 18: 13441349.
Manabe, N., Furuya, Y., Nagano, N. and Miyamoto, H. 1994b. Immunohistochemical microquantitation method for type I collagen in kidney histological section of the rats. Journal of Veterinary Medical Science 56: 147150.
Manabe, N., Ishibashi, T. and Miyamoto, H. 1993a. Slow-twitch myofibers are observed in masseter muscle of the hypothalamic obese rat. Animal Science and Technology 64: 440447.
Manabe, N., Ishii, T. and Ishibashi, T. 1982. pH stability of myosin adenosine triphosphatase activity of the muscle fibers in the growing cattle, sheep and swine. Japanese Journal of Zootechnical Science 53: 6466.
Manabe, N., Ishii, T. and Ishibashi, T. 1988. Histochemical fiber type composition and fiber size in skeletal muscles of the growing cattle, sheep and swine. Memories of College of Agriculture Kyoto University 131: 2736.
Manabe, N., Sato, E., Watanabe, S. and Ishibashi, T. 1980. The skeletal muscle fiber types of the mammals. 1. Nyctereus procynoides, Mustela itatsi, Canis familiaris, Rhinolophus ferrumequinum, Crocidula dsinezumi, Journal of Mammalian Science 40: 8994.
Pette, D. and Staron, R. S. 1990. Cellular and molecular diversities of mammalian skeletal muscle fibers. Review of Physiology Biochemistry and Pharmacology 116: 176.
Picard, B., Leger, J. and Robelin, J. 1994. Quantitative determination of type I myosin heavy chain in bovine muscle with antimyosin monoclonal antibodies. Meat Science 36: 333343.
Pullen, A. H. 1977. The distribution and relative sizes of fibre types in the extensor digitorum longus and soleus muscles of the adult rat. Journal of Anatomy 123: 467486.
Reiser, P. J., Moss, R. L., Giulian, G. G. and Greaser, M. L. 1985. Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition. Journal of Biological Chemistry 260: 90779080.
Robe, G. H. and Xiong, Y. L. 1992. Phosphates and muscle fiber type influence thermal transitions in porcine salt-soluble protein aggregation. Journal of Food Science 57: 13041307.
Staron, R. S. and Pette, D. 1986. Correlation between myofibrillar ATPase activity and myosin heavy chain comoposition in rabbit muscle fibers. Histochemistry 86: 1923.
Suzuki, A. 1971a. Histochemical classification of individual skeletal muscle fibers in the sheep. I. On M. semitendinosus, M. longissimus dorsi, M. psoas major, M. latissimus dorsi and M. gastrocnemius. Japanese Journal of Zootechnical Science 42: 3954.
Suzuki, A. 1971b. Histochemical classification of individual skeletal muscle fibers in the sheep. II. On M. serratus ventralis, M. supraspinatus, M. infraspinatus, M. semimembranosus and M. triceps brachii (Caput longum). Japanese Journal of Zootechnical Science 42: 463473.
Suzuki, A. 1973. Histochemical observations of individual skeletal muscle fibers in starved sheep. Japanese Journal of Zootechnical Science 44: 5058.
Suzuki, A. and Tamate, H. 1988. Distribution of myofiber types in the hip and thigh musculature of sheep. Anatomical Record 221: 494502.
Termin, A., Staron, R. S. and Pette, D. 1989a. Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle. Histochemistry 92: 453457.
Termin, A., Staron, R. S. and Pette, D. 1989b. Changes in myosin heavy chain isoforms during chronic low-frequency stimulation of rat fast hindlimb muscles — a single fibre study. European Journal of Biochemistry 186: 749754.

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Immunohistochemical quantification of fast-myosin in frozen histological sections of goat limb muscles

  • N. Manabe (a1), Y Azuma (a2), Y. Furuya (a1), K. Kuramitsu (a1), Y. Kuribayashi (a1), N. Nagano (a3) and H. Miyamoto (a1)...

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