Immunohistochemical analysis of bFGF, TGF-β1 and catalase in rectus abdominis muscle from cattle foetuses at 180 and 260 days post-conception

Tissue and Cell

Volumn 34, Issue 6, 2002, Pages 416-426

  Orzechowski, Arkadiusz ^a   Gajkowska, B ^b   Wojewodzka U ^b   Cassar Malek, I ^c   Picard, B ^c   Hocquette, J F ^c  

^a WARSAW UNIVERSITY OF LIFE SCIENCES   (Poland)

^b POLISH ACADEMY OF SCIENCES   (Poland)

^c UMR1213 HERBIVORES   (France)

Author keywords

bFGF; Catalase; Cattle; Muscle growth; TGF 1

Indexed keywords

ANTIOXIDANT; BASIC FIBROBLAST GROWTH FACTOR; CATALASE; GROWTH FACTOR; TRANSFORMING GROWTH FACTOR BETA1;

AGE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BIRTH; BLOOD VESSEL; CATTLE; CELL DIFFERENTIATION; CELL PROLIFERATION; CONCEPTION; ENZYME ACTIVITY; FETUS; FETUS GROWTH; GENOTYPE; GROWTH REGULATION; IMMUNOHISTOCHEMISTRY; MATURATION; MUSCLE GROWTH; MUSCLE MITOCHONDRION; MYOBLAST; NONHUMAN; PROTEIN CONTENT; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; QUANTITATIVE ANALYSIS; RECTUS ABDOMINIS MUSCLE; ROUGH ENDOPLASMIC RETICULUM; SKELETAL MUSCLE; SMOOTH ENDOPLASMIC RETICULUM;

BOS TAURUS; FELIS CATUS;

EID: 0036908127     PISSN: 00408166     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0040816602000824     Document Type: Article

References (47)

1. Bae, Y.S., Sung, J.-Y., Kim, O.-S., Kim, Y.-J., Hur, K.-C., Kazlaukas, A. and Rhee, S.G. 2000. Platelet-derived growth factor-induced Ho(2)O(2) requires the activation of phosphatidylinositol 3-kinase. J. Biol. Chem., 275, 10527-10531.
2. Blachowski, W., Motyl, T., Orzechowski, A., Grzelkowska, K. and Interewicz, B. Comparison of metabolic effects of EGF, TGFα, and TGFβ1 in primary culture of foetal bovine myoblasts and rat L6 myoblasts. Int. J. Biochem., 25, 1571-1577.
3. Clarke, M.S., Khakee, R. and McNeil, P.L. 1993. Loss of cytoplasmic basic fibroblast growth factor from physiologically wounded myofibers of normal and dystrophic muscle. J. Cell Sci., 106, 121-133.
4. Czubryt M.P., Austria, J.A. and Pierce, G.N. 2000. Hydrogen peroxide inhibition of nuclear protein import is mediated by the mitogen-activated protein kinase, ERK2. J. Cell Biol., 148, 7-15.
5. Elsasser T.H., Kahl, S., Rumsey, T.S. and Blum, J.W. 2000. Modulation of growrth performance in disease: Reactive nitrogen compounds and their impact on cell proteins. Domest. Anim. Endocrinol., 19, 75-84.
6. Fahimi, H.D. and Baumgart, E. 1999. Current cytochemical techniques for the investigation of peroxisomes: A review. J. Histochem. Cytochem., 47, 1219-1232.
7. Florini, J.R. 1987. Hormonal control of muscle growth. Muscle Nerve, 7, 577-612.
8. Gagniere, H., Ménissier, F., Geay, Y. and Picard, B. 2000. Influence of genotype on contractile protein differentiation in different bovine muscles during foetal life. Ann. Zootech., 49, 405-423.
9. Greene, E.A. and Allen, R.E. (1991). Growth factor regulation of bovine satellite cell growth in vitro. J. Anim. Sci. 69, 146-152.
10. Grobet, L., Poncelet, D., Royo, L., Brouwers, B., Pirottin, D., Michaux, C., Menissier, F., Zanotti, M., Dunner. S. and Geroges, M. 1998. Molecular definition of anallelic series of mutation disrupting the myostatin function and causing double muscling in cattle. Mamm. Genome, 9, 210-213.
11. Grobet, L., Royo, L., Poncelet, D., Pirottin, D., Brouwers, B., Riquet, J., Schoeberlein, A., Dunner, S., Ménissier, F., Masabanda, J., Fries, R., Hanset, R. and Georges, M. 1997. A deletion in the bovine Myostatin gene causes the double-muscled phenotype in cattle. Nat. Genet., 17, 71-74.
12. Hardy, S., Kong, Y. and Konieczny, S.F. 1993. Fibroblast growth factor inhibits MRF4 activity independently of the phosphorylation status of a conserved threonine residue within the DNA-binding domain. Mol. Cell. Biol., 13, 5943-5956.
13. Hocquette, J-F., Ortigues-Marty, I., Pethick, D.W., Herpin. P. and Fernandez, X. (1998). Nutritional and hormonal regulation of energy metabolism in skeletal muscles of meat-producing animals. Livest. Prod. Sci., 56, 115-143.
14. Hocquette, J-F., Piot, C. and Picard, B 2000. Metabolic differentiation of bovine cardiac and skeletal muscles during foetal development. In: International Congress of Myology. Nice, France.
15. Hong, Y.-H., Peng, H.-B., Fata, V.L. and Liao, J.K. 1997. Hydrogen peroxide-mediated transcriptional of macrophage colony-stimulating factor by TGF-β1. J. Immunol., 159, 2418-2423.
16. Irani, K., Xia, Y., Zweier, J.L., Sollott, S.J., Der, C.J., Fearon, E.R., Sundaresan, M., Finkel, T. and Goldschmidt-Clermont, P.J. 1997. Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts. Science, 275, 1649-1652.
17. Kazama, H. and Yonehara, S. 2000. Oncogenic K-Ras and basic fibroblast growth factor prevent Fas-mediated apoptosis in fibroblasts through activation of mitogen-activated protein kinase. J. Cell Biol., 148, 557-566.
18. Ko, T.-P., Safo, M.K., Musayev, F.N., Di Salvo, M.L., Wang, C., Wu, S.-H. and Abraham, D. (2000) Structure of human erythrocyte catalase. Biol. Cryst., 56, 241-245.
19. Liu, W., Zhu, X.-Z. and Ji, X.-Q. 1999. Effect of basic fibroblast growth factor on focal ischemic injury and antioxidant enzyme activities. Acta Pharmacol. Sin., 20, 227-231.
20. McPherron, A.C. and Lee, S.J. 1997. Double muscling in cattle due to mutations in the myostatin gene Proc. Natl. Acad. Sci. U.S.A., 94, 12457-12461.
21. McPherron, A., Lawler, A.M. and Lee S.-J. 1997. Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member. Nature, 387, 83-90.
22. Moore, J.W., Dionne, C., Jaye, M. and Swain, J.L. 1991. The mRNAs encoding acidic FGF, basic FGF and FGF receptor are coordinately downeregulated during myogenic differentiation. Development, 111, 741-748.
23. Oldham, J.M., Martyn, J.A.K., Sharma, M., Jeanplong, F., Kambadur, R. and Bass, J.J. 2001. Molecular expression of myostatin and MyoD is greater in double-muscled than normal-muscled cattle foetuses. Am. J. Physiol. Regul. Integr. Comp. Physiol. 280, R1488-R1493.
24. Olwin, B.B. and Hauschka, S.D. 1988. Cell surface fibroblast growth factor and epidermal growth factor receptors are permanently lost during skeletal muscle terminal differentiation. J. Cell Biol., 107, 761-769.
25. Orzechowski, A. and Grzelkowska, K. 2000. Apoptotic effect of reactive oxygen/nitrogen species (ROS/RNS) in rat L6 satellite cells. Pol. J. Vet. Sci., 3, 195-205.
26. Orzechowski, A., Grzelkowska, K., Skierski, J., Poszaj, T. and Motyl, T. 1996. Resistance of L6 myoblasts to TGF-(1 induced apoptosis). J. Physiol. Pharmacol. 47 (3 Suppl 2). 152.
27. Orzechowski, A., Czerwińska, I. and Ostaszewski, P. 2001. Growth promoting effect of SOD-1 or catalase on skeletal myogenesis from C2C12 myoblasts treated with insulin, PDGF, EGF, TGF-α, TNF-α and TGF-β1. In: Fifth Winter Research Conferences, CERLIB. Val Cenis. France.
28. Pena, T.L., Chen, S.H., Konieczny, S.F. and Ranen, S.G. 2000. Ras/MEK/ERK up-regulation of the fibrobalst KCa channel FIK is a common mechanism for basic fibroblast growth factor and transforming growth factor-β suppression of myogenesis. J. Biol. Chem., 275, 13677-13682.
29. Picard, B., Gagniere, H., Robelin, J. and Geay, Y. Comparison of the foetal development of muscle in normal and double-muscled cattle. J. Muscle Res. Cell Motil., 16, 629-639.
30. Picard, B., Depreux, F. and Geay, Y. 1998. Muscle differentiation of normal and double-muscled bovine foetal myoblasts in primary culture. Basic Appl. Myol., 8, 197-203.
31. Picard, B., Duclos, M.,Lefaucheur, L. and Berri, C. 2002. Myogenesis in farm animal species. Reprod. Nutr. Dev. (in press).
32. Pruddhome, G.J. and Piccirillo, C.A. 2000. The inhibitory effects of transforming growth factor-beta-1 (TGF-β1) in autoimmune diseases. J. Autoimmun., 14, 23-42.
33. Rochard, P., Rodier, A., Casas, F., Cassar-Malek, I., Marchal-Victorion, S.,Daury, L., Wrutniak, C. and Cabello, G. 2000. Mitochondrial activity is involveld in the regulation of myoblast differentiatioon through myogenin expression and activity of myogenic factors. J. Biol. Chem., 275, 2733-2744.
34. Roymans, D. and Slegers, H. 2001. Phosphatidylinositol 3-kinases in tumor progression. Eur. J. Biochem., 268, 487-498.
35. Sakuma, K., Watanabe, K., Sano, M., Uramotop, I. and Totsuka, T. 2000. Postnatal profiles of myogenic regulatory factors and the receptors of TGF-β2, LIF and IGF-I in the gastrocnemius and rectus femoris muscles of dy mouse. Acta Neuropathol., 99, 169-176.
36. Scata, K.A., Bernard, D.W., Fox, J. and Swain, J.L. 1999. FGF receptor availability regulates skeletal myogenesis. Exp. Cell Res., 250, 10-21.
37. Schlessinger, J. 2000. Cell signalling by receptor tyrosine kinases. Cell 103, 211-225.
38. Sheehan, S.M. and Allen, R.E. 1999. Skeletal muscle satellite cell proliferation in response to members of the firblast growth factors family and hepatocyte growth factor. J. Cell Physiol., 181, 499-506.
39. Solanes, G., Pedraza, N., Iglesias, R., Giralt, M. and Villaroya, F. 2000. The human uncoupling protein-3 gene promoter requires MyoD and is induced by retinoic acid in muscle cells. FASEB J., 14, 2141-2143.
40. 2 and nitric-oxide-mediated oxidative stress induce apoptosis in rat skeletal muscle myoblasts. J. Neuropathol. Exp. Neurol., 55, 36-43.
41. 2 for platelet-derived growth factor signal transduction. Science, 270, 296-299.
42. Sundaresan, M., Yu, Z.X., Ferrans, V.J., Sulciner, D.J., Gutkind, J.S., Irani, K., Goldschmidt-Clermont, P.J. and Finkel, T. 1996. Regulation of reactive-oxygen-species generation in fibroblasts by Racl. Biochem. J., 318, 379-382.
43. Taylor, W.R., Bhasin, S., Artaza, J., Byhower, F., Azam, M.,Willard, D.H., Kull, F.C. and Gonzalez-Cadavid, N. 2001. Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells. Am. J. Physiol. Endocrinol. Metab., 280, E221-E228.
44. 2-terminal kinase). Eur. J. Biochem., 244, 587-595.
45. Vaidya, T.B., Rhodes, S.J., Taparowsky, E.J. and Konieczny, S.R. 1989. Fibroblast growth factor and transforming growth factor β repress transcription of the myogenic regulatory gene MyoD. Mol. Cell. Biol., 9, 3576-3579.
46. Westermarck, J., Li, S.-P., Kallunki, T., Han, J. and Kahario, V.-M. 2001. p38 mitogen activated protein kinase-dependent activation of protein phosphatases 1 and 2a inhibits MEK1 and MEK2 activity and collagenase 1 (MMP-1) gene expression. Mol. Cell. Biol., 21, 2373-2383.
47. Zamocky, M. and Koller, F. (1999). Understanding the structure and function of catalases: Clues form molecular evolution and in vitro mitogenesis. Prog. Biophys. Mol. Biol., 72, 19-66.