Suppression of Growth-Associated Phosphorylation of Proteins of Fibroblasts by Collagen Fibrils

作者: Norimasa Kosekt , Hajime Sato , Katsutoshi Yoshizato

DOI: 10.3109/15419069609081023

关键词:

摘要: Collagen fibrils suppressed serum- or epidermal growth factor (EGF)-inducible DNA synthesis of human fibroblasts. The phosphorylation cellular proteins upon these mitogenic stimulation was analyzed by two-dimensional polyacrylamide gel electrophoresis in order to reveal a possible interference collagen with the signal transduction pathway coupled protein phosphorylation-dephosphorylation reaction. Spots phosphorylated numbered 192 on plain plastic which were reduced 143 fibrils. More than half them matched between two substrates, most much more weakly EGF stimulated cells plastic. Among an approximate molecular weight 27K and isoelectric point 5.3 early highly responsive EGF, seemed be catalyzed mainly kinase C tyrosine kinase. significantly this phosphorylation. present study demonstrates that modulate growth-associated cells, seems lead suppression synthesis.

参考文章(45)
Alain Colige, Betty Nusgens, C. M. Lapiere, Effect of EGF on human skin fibroblasts is modulated by the extracellular matrix. Archives of Dermatological Research. ,vol. 280, ,(1988)
P J Blackshear, L A Witters, P R Girard, J F Kuo, S N Quamo, Growth factor-stimulated protein phosphorylation in 3T3-L1 cells. Evidence for protein kinase C-dependent and -independent pathways. Journal of Biological Chemistry. ,vol. 260, pp. 13304- 13315 ,(1985) , 10.1016/S0021-9258(17)38870-1
C. Faucher, J. Capdevielle, I. Canal, P. Ferrara, H. Mazarguil, W.L. McGuire, J.M. Darbon, The 28-kDa protein whose phosphorylation is induced by protein kinase C activators in MCF-7 cells belongs to the family of low molecular mass heat shock proteins and is the estrogen-regulated 24-kDa protein. Journal of Biological Chemistry. ,vol. 268, pp. 15168- 15173 ,(1993) , 10.1016/S0021-9258(18)82451-6
L King, S Cohen, G Carpenter, Rapid enhancement of protein phosphorylation in A-431 cell membrane preparations by epidermal growth factor. Journal of Biological Chemistry. ,vol. 254, pp. 4884- 4891 ,(1979) , 10.1016/S0021-9258(17)30094-7
L Kornberg, H.S. Earp, J.T. Parsons, M Schaller, R.L. Juliano, Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. Journal of Biological Chemistry. ,vol. 267, pp. 23439- 23442 ,(1992) , 10.1016/S0021-9258(18)35853-8
S.M. Bockholt, K. Burridge, Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin. Journal of Biological Chemistry. ,vol. 268, pp. 14565- 14567 ,(1993) , 10.1016/S0021-9258(18)82365-1
T Kadowaki, S Koyasu, E Nishida, K Tobe, T Izumi, F Takaku, H Sakai, I Yahara, M Kasuga, Tyrosine phosphorylation of common and specific sets of cellular proteins rapidly induced by insulin, insulin-like growth factor I, and epidermal growth factor in an intact cell. Journal of Biological Chemistry. ,vol. 262, pp. 7342- 7350 ,(1987) , 10.1016/S0021-9258(18)48242-7
J. Sinnett-Smith, I. Zachary, A.M. Valverde, E. Rozengurt, Bombesin stimulation of p125 focal adhesion kinase tyrosine phosphorylation. Role of protein kinase C, Ca2+ mobilization, and the actin cytoskeleton. Journal of Biological Chemistry. ,vol. 268, pp. 14261- 14268 ,(1993) , 10.1016/S0021-9258(19)85236-5
C.E. Somers, D.F. Mosher, Protein kinase C modulation of fibronectin matrix assembly. Journal of Biological Chemistry. ,vol. 268, pp. 22277- 22280 ,(1993) , 10.1016/S0021-9258(18)41525-6