The Histochemical and Ultrastructural Structures of Avian Latissimus Dorsi Muscle Fiber Types and Changes in Them Caused by Water Copper Level

The histochemical and ultrastructural effects of water Cu on the anterior latissimus dorsi (ALD) muscle of 120 newly hatched broilers were investigated in a 45-day experiment. Two doses of water Cu (250 mg Cu/kg water and 500 mg Cu/kg water) were given to the poults. Two distinct categories (IIIA and IIIB) of slow tonic fibers in the control groups were detected by enzyme reactions. The ultrastructure of the Z-line, mitochondrial content and sarcotubular content differed between the 2 fiber types. In the application of 250 mg Cu/kg water, the histochemical characteristics of the IIIB fibers were clearly different from those observed in the control. In addition, a few IIIB fibers transformed to fast fiber types in their ultrastructure. No transformation of IIIA fiber type occurred, but a significant increase in fiber percentages (86.7%) was observed in the application of 500 mg Cu/kg water. In the application of 500 mg Cu/kg water, there was degeneration in IIIB fibers. Mitochondrial degeneration also occurred in both applications.

The Histochemical and Ultrastructural Structures of Avian Latissimus Dorsi Muscle Fiber Types and Changes in Them Caused by Water Copper Level

The histochemical and ultrastructural effects of water Cu on the anterior latissimus dorsi (ALD) muscle of 120 newly hatched broilers were investigated in a 45-day experiment. Two doses of water Cu (250 mg Cu/kg water and 500 mg Cu/kg water) were given to the poults. Two distinct categories (IIIA and IIIB) of slow tonic fibers in the control groups were detected by enzyme reactions. The ultrastructure of the Z-line, mitochondrial content and sarcotubular content differed between the 2 fiber types. In the application of 250 mg Cu/kg water, the histochemical characteristics of the IIIB fibers were clearly different from those observed in the control. In addition, a few IIIB fibers transformed to fast fiber types in their ultrastructure. No transformation of IIIA fiber type occurred, but a significant increase in fiber percentages (86.7%) was observed in the application of 500 mg Cu/kg water. In the application of 500 mg Cu/kg water, there was degeneration in IIIB fibers. Mitochondrial degeneration also occurred in both applications.

___

  • Dove, C.R.: Effect of adding copper and various fat sources to the diets of weanling swine on growth performance and serum fatty acid profiles. J. Anim. Sci., 1993; 71: 2187-2192.
  • Weeks, R.C., Sullivan, T.W.: Influence of copper sulphate on the “Growth Promoting” effect of penicillin and streptomycin in turkey diets. Poult. Sci., 1972; 51: 475-480.
  • Guenthner, E., Carlson, CW., Emerick, R.J.: Copper salts for growth stimulation and alleviation of aortic rupture losses in turkeys. Poult. Sci., 1978; 57: 1313-1324.
  • Kashani, A.B., Samie, H., Emerick, R.J., Carlson, C.: Effect of copper with three levels of sulfur containing amino acid in diet for turkeys. Poult. Sci., 1986; 665: 1754-1759. 5. Christmas, R.B., Harms, R.M.: The effect of supplemental copper and methionine on the performance of the poultry turkeys. Poult. Sci., 1979; 58: 382-384. 6. Harms, R.H., Buresh, R.E.: Influence of three levels of copper on the performance of turkey poults with diets containing two sources of methionine. Poult. Sci., 1987; 66: 721-724.
  • Rimer, M., Rondall, W.R.: Denervation of chicken skeletal muscle causes an increase in acetylcholinesterase mRNA synthesis. Biochim. Biophys. Res. Com., 1999; 260: 251-255. 8. Nishida, J., Machida, N.W., Tagome, M., Kasugai, Y.: Distribution of parvalbumin in specific fibre types of chicken skeletal muscles. Brit. Poult. Sci., 1995; 36: 585-597.
  • Khan, M.A.: Unique ultrastructural characteristics of pigeon
  • anterior latissimus dorsi. Cell. Mol. Biol. Res., 1993; 39: 65-71.
  • Govind, C.K., Pearce, J.: Muscle remodeling in adult snapping shrimps via fast-fiber degeneration and slow-fiber genesis and transformation. Cell Tiss. Res., 1994; 276: 445-454.
  • Gardahaut, M.F., Rouaud, T.P., Renaud, D., Khaskiye, A., Le Douarin, G.H.: Role of nerve and tension in maturation of posthatching slow-tonic muscle in chicken. Muscle and Nerve, 1989; 12 : 943-952.
  • Dubowitz, V., Brooke, M.H.: Muscle biopsy : A modern approach. W.B. Saunders Co. Ltd. London. 1973; p: 5-73.
  • Bancroft, S.D., Stevens, A.: Theory and practice of histological techniques. Churchill Livingstone. Edinburgh (2nd ed.). 1982, p: 662.
  • Gleeson, T.T., Putnam, R.W., Bennet, A.F.: Histochemical, enzymatic, and contractile properties of skeletal muscle fibers in the lizard Dipsosaurus dorsalis. J. Exp. Zool., 1980; 214: 293- 302.
  • Sigel, P., Pette, D.: A gel film method for coupled enzyme reactions in histochemistry. J. Histochem. Cytochem., 1969; 17: 225-237.
  • Hooper, A.C.B.: Muscle fiber length and bone length in adult mice during dietary restriction and refeeding. Nutr. Res., 1986; 6: 415-420.
  • Ovalle, W.K.: Histochemical dichotomy of extrafusal and intrafusal fibers in an avian slow muscle. Am. J. Anat., 1978; 152: 587- 598.
  • Barnard, E.A., Lyles, J.M., Pizzey, J.A.: Fibre types in chicken skeletal muscles and their changes in muscular dystrophy. J. Physiol., 1982; 331: 333-354.
  • Huerta, M., Trujillo, X., Vasquez, C.: B-Adrenergic modulation of Ba2+currents and K+contracture in frog slow skeletal muscle fibres. Am. J. Physiol-Cell Physiol., 1997; 272 (141-1): C77- C81.
  • Shear, C.R., Goldspink, G.: Structural and physiological changes associated with the growth of avian fast and slow muscle. J. Morphol., 1971; 135: 351-372.
  • Zelena, J., Jirmanova, I.: Ultrastructure of chicken slow muscle after nerve cross union. Exp. Neurol., 1973; 38: 272-285.
  • Hikida, R.S.: Morphological transformation of slow to fast muscle fibers after tenotomy. Exp. Neurol., 1972; 35: 265-273.
  • Remignon, H., Gardahaut, M.F., Marche, G., Richard, F.H.: Selection for rapid growth increases the number and the size of muscle fibres without changing their typing in chickens. J. Muscle Res. Cell Mot., 1995; 16: 95-102.
  • Gordon, T., Perry, R., Srihari, T., Vrbova, G.: Differentiation of slow and fast muscles in chickens. Cell Tiss. Res., 1977; 180: 211-222.
  • Jensen, L.S., Maurice, D.V.: Effects of high dietary copper on the ceca of chicks. Poultry Sci., 1978; 57: 166-170.
  • Myers, B.M., Prendergast, F.G., Holman, R., Kuntz, S.M., Larusso, N.F.: Alterations in hepatocyte lysosomas in experimental hepatic copper overload in rats. Gastroenterology, 1993; 105: 1814-1823.
  • Obermann, W.M., Gautel, L., Steiner, F., van der Ven, P.F., Weber, K., Fürst, D.O.: The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxyterminal region of titin by immunoelectron microscopy. J. Cell Biol., 1996; 134: 1441-1453.
  • Luther, P.K., Squire, J.M.: Muscle Z-band ultrastructure: titin Z- repeats and Z-band periodicities do not match. J. Mol. Biol., 2002; 319: 1157-1164.
  • Masini, A., Scotti, C., Calligaro, A., Cazzalini, O., Stivala, L.A., Bianchi, L., Grovannini, F., Ceccarelli, D., Muscatello, Y., Tomasi, A., Vannini, V.: Zidovudine-induced experimental myopathy: dual mechanism of mitochondrial damage. J. Neurobiol. Sci., 1999; 166: 131-140.
  • Sokol, R.J., Twedt, D., McKim, J.M., Devereaux, M.W., Karrer, F.M., Kam, I., von Steigman, G., Narkewicz, M.R., Bacon, B.R., Britton, R.S., Neuschwandertetri, B.A.: Oxidant injury to hepatic mitochondria in patients with Wilson’s disease and Bedlington terriers with copper toxicosis. Gastroenterology, 1994; 107: 1788-1798.
  • Fry, T.G., Renken, C.W., Perkins, G.A.: Insight into mitochondrial structure and function from electron tomography. Biochem. Biophys. Acta (BBA)-Bioenerg., 2002; 1555: 196-203.