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Current IssueEditorial BoardOnline First ArticlesArchive

Research Article

volume 53 issue 7 (july 2019) : 852-855,   Doi: 10.18805/ijar.B-3596

Expression profile of the myoglobin gene in indigenous native chicken

A
Athe Rajendra Prasad
N
N. Govardhana Sagar
R
R.N. Chatterjee
C
Chandan Paswan
S
S.P. Yadav
T
T.K. Bhattacharya
1ICAR-Directorate of Poultry Research, Hyderabad-500 030, Telangana, India.
Cite article:- Prasad Rajendra Athe, Sagar Govardhana N., Chatterjee R.N., Paswan Chandan, Yadav S.P., Bhattacharya T.K. (2018). Expression profile of the myoglobin gene in indigenous native chicken. Indian Journal of Animal Research. 53(7): 852-855. doi: 10.18805/ijar.B-3596.

ABSTRACT

In the present study, we quantified myoglobin (Mb) gene expression in two different indigenous chicken breeds, namely Ghagus and Aseel to discern tissue specific expression pattern in different age groups. Quantitative real-time PCR assay was developed for measurement of the Mb mRNA expression in different tissues in chickens of different age groups (day old and day 28). Overall, the Mb mRNA level displayed a significant difference among all the tissues investigated in the study. Results exhibited that, bursa and heart tissues relatively had the highest expression of Mb related to the other tissues (P<0.05). Further, in gizzard and bursa, a significant difference was found in the expression between both the breeds studied. It is concluded that the expression of Mb gene varied significantly among different tissues and between age groups in chicken.

REFERENCES

  1. Blessing, M.H. and Muller, G. (1974). Myoglobin concentration in the chicken, especially in the gizzard (a biochemical, light and electron  microscopic study). Comparative Biochemistry and Physiology Part A: Physiology, 47(2): 535-540.
  2. de Koning, J., Hoofd, L.J.C. and Kreuzer, F. (1981). Oxygen transport and the function of myoglobin. Pflügers Archiv, 389(3): 211-217.
  3. Fraser, J., de Mello, L.V., Ward, D., Rees, H.H., Williams, D.R., Fang, Y., Brass, A., Gracey, A.Y. and Cossins, A.R. (2006). Hypoxia-    inducible myoglobin expression in nonmuscle tissues. Proceedings of the National Academy of Sciences of the United States of America, 103(8): 2977-2981.
  4. Graber, S.G. and Woodworth, R.C. (1986). Myoglobin expression in L6 muscle cells. Role of differentiation and heme. Journal of Biological Chemistry, 261: 9150-9154.
  5. Groschel-Stewart, U., Jaroschik, U. and Schwalm, H. (1971). Chicken gizzard, a myoglobin-containing smooth muscle.Cellular and Molecular Life Sciences, 27: 512.
  6. Hochachka, P. and Somero, G. (2002). Biochemical Adaptation: Mechanism and process in physiological evolution. University Press, Oxford:
  7. Livak, K.J. and Schmittgen, T.D. (2001). Analysis of relative gene expression data using real-time quantitative PCR and the 2-DDCT method. Methods, 25(4): 402–408.
  8. Millikan, G.A. (1937). Experiments on muscle haemoglobin in vivo; the instantaneous measurement of muscle metabolism. Proceedings of the Royal Society of London. Series B, Biological sciences, 123: 218-241.
  9. Millikan, G.A. (1939). Muscle hemoglobin. Physiological Reviews, 19: 503–523.
  10. Takahashi, E., Sato, K., Endoh, H., Xu, Z.L. and Doi, K. (1998). Direct observation of radial intracellular PO2 gradients in a single cardiomyocyte of the rat. American Journal of Physiology-Heart and Circulatory Physiology, 275: H225-H233.
  11. Underwood, L.E. and Williams, R.S. (1987). Pre-translational regulation of myoglobin gene expression. American Journal of Physiology-    Cell Physiology, 252: C450-C453.
  12. Williams, R.S. and Neufer, P.D. (1996). Regulation of gene expression in skeletal muscle by contractile activity. Comprehensive Physiology. American Physiological Society, Bethesda, MD:
  13. Wittenberg, J.B. (1970). Myoglobin facilitated oxygen diffusion and the role of myoglobin in oxygen entry into muscle.Physiological Reviews, 50: 559-636.
  14. Wittenberg, B.A. and Wittenberg, J.B. (1989). Transport of oxygen in muscle. Annual Review of Physiology, 51(1): 857-878.
  15. Wittenberg, J.B. and Witternberg, B.A. (2003). Myoglobin function reassessed. Journal of Experimental Biology, 206: 2011-2020.
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Indian Journal of Animal Research
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    Research Article

    volume 53 issue 7 (july 2019) : 852-855,   Doi: 10.18805/ijar.B-3596

    Expression profile of the myoglobin gene in indigenous native chicken

    A
    Athe Rajendra Prasad
    N
    N. Govardhana Sagar
    R
    R.N. Chatterjee
    C
    Chandan Paswan
    S
    S.P. Yadav
    T
    T.K. Bhattacharya
    1ICAR-Directorate of Poultry Research, Hyderabad-500 030, Telangana, India.
    Cite article:- Prasad Rajendra Athe, Sagar Govardhana N., Chatterjee R.N., Paswan Chandan, Yadav S.P., Bhattacharya T.K. (2018). Expression profile of the myoglobin gene in indigenous native chicken. Indian Journal of Animal Research. 53(7): 852-855. doi: 10.18805/ijar.B-3596.

    ABSTRACT

    In the present study, we quantified myoglobin (Mb) gene expression in two different indigenous chicken breeds, namely Ghagus and Aseel to discern tissue specific expression pattern in different age groups. Quantitative real-time PCR assay was developed for measurement of the Mb mRNA expression in different tissues in chickens of different age groups (day old and day 28). Overall, the Mb mRNA level displayed a significant difference among all the tissues investigated in the study. Results exhibited that, bursa and heart tissues relatively had the highest expression of Mb related to the other tissues (P<0.05). Further, in gizzard and bursa, a significant difference was found in the expression between both the breeds studied. It is concluded that the expression of Mb gene varied significantly among different tissues and between age groups in chicken.

    REFERENCES

    1. Blessing, M.H. and Muller, G. (1974). Myoglobin concentration in the chicken, especially in the gizzard (a biochemical, light and electron  microscopic study). Comparative Biochemistry and Physiology Part A: Physiology, 47(2): 535-540.
    2. de Koning, J., Hoofd, L.J.C. and Kreuzer, F. (1981). Oxygen transport and the function of myoglobin. Pflügers Archiv, 389(3): 211-217.
    3. Fraser, J., de Mello, L.V., Ward, D., Rees, H.H., Williams, D.R., Fang, Y., Brass, A., Gracey, A.Y. and Cossins, A.R. (2006). Hypoxia-    inducible myoglobin expression in nonmuscle tissues. Proceedings of the National Academy of Sciences of the United States of America, 103(8): 2977-2981.
    4. Graber, S.G. and Woodworth, R.C. (1986). Myoglobin expression in L6 muscle cells. Role of differentiation and heme. Journal of Biological Chemistry, 261: 9150-9154.
    5. Groschel-Stewart, U., Jaroschik, U. and Schwalm, H. (1971). Chicken gizzard, a myoglobin-containing smooth muscle.Cellular and Molecular Life Sciences, 27: 512.
    6. Hochachka, P. and Somero, G. (2002). Biochemical Adaptation: Mechanism and process in physiological evolution. University Press, Oxford:
    7. Livak, K.J. and Schmittgen, T.D. (2001). Analysis of relative gene expression data using real-time quantitative PCR and the 2-DDCT method. Methods, 25(4): 402–408.
    8. Millikan, G.A. (1937). Experiments on muscle haemoglobin in vivo; the instantaneous measurement of muscle metabolism. Proceedings of the Royal Society of London. Series B, Biological sciences, 123: 218-241.
    9. Millikan, G.A. (1939). Muscle hemoglobin. Physiological Reviews, 19: 503–523.
    10. Takahashi, E., Sato, K., Endoh, H., Xu, Z.L. and Doi, K. (1998). Direct observation of radial intracellular PO2 gradients in a single cardiomyocyte of the rat. American Journal of Physiology-Heart and Circulatory Physiology, 275: H225-H233.
    11. Underwood, L.E. and Williams, R.S. (1987). Pre-translational regulation of myoglobin gene expression. American Journal of Physiology-    Cell Physiology, 252: C450-C453.
    12. Williams, R.S. and Neufer, P.D. (1996). Regulation of gene expression in skeletal muscle by contractile activity. Comprehensive Physiology. American Physiological Society, Bethesda, MD:
    13. Wittenberg, J.B. (1970). Myoglobin facilitated oxygen diffusion and the role of myoglobin in oxygen entry into muscle.Physiological Reviews, 50: 559-636.
    14. Wittenberg, B.A. and Wittenberg, J.B. (1989). Transport of oxygen in muscle. Annual Review of Physiology, 51(1): 857-878.
    15. Wittenberg, J.B. and Witternberg, B.A. (2003). Myoglobin function reassessed. Journal of Experimental Biology, 206: 2011-2020.
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      Indian Journal of Animal Research

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