Tissue-dependent regulation of protein tyrosine kinase activity during embryonic development.
作者： P A Maher
关键词:
摘要: Protein tyrosine kinase activity was assayed in a variety of chicken tissues during embryonic development and the adult. In some protein decreased development; however, other it remained high throughout development, contrast to level phosphorylation, which development. The highest levels were detected 17-d brain although only low phosphorylation observed this tissue. Several alternatives examined an effort determine mechanism responsible for phosphorylated proteins most older adult despite presence highly active kinases. results show that regulation is complex varies from tissue Furthermore, suggest phosphatases play important role regulating phosphotyrosine many tissues.
core.ac.uk
rupress.org
jcb.org参考文章(23)
C. Bordier, Phase separation of integral membrane proteins in Triton X-114 solution. Journal of Biological Chemistry. ,vol. 256, pp. 1604- 1607 ,(1981) , 10.1016/S0021-9258(19)69848-0
P. A. Maher, S. J. Singer, Anomalous interaction of the acetylcholine receptor protein with the nonionic detergent Triton X-114. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 82, pp. 958- 962 ,(1985) , 10.1073/PNAS.82.4.958
Yehiel ZICK, George GRUNBERGER, Robert W. REES-JONES, Richard J. COMI, Use of tyrosine-containing polymers to characterize the substrate specificity of insulin and other hormone-stimulated tyrosine kinases. FEBS Journal. ,vol. 148, pp. 177- 182 ,(1985) , 10.1111/J.1432-1033.1985.TB08822.X
K L Gould, J A Cooper, A Bretscher, T Hunter, The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein. Journal of Cell Biology. ,vol. 102, pp. 660- 669 ,(1986) , 10.1083/JCB.102.2.660
D. E. Cool, N. K. Tonks, H. Charbonneau, K. A. Walsh, E. H. Fischer, E. G. Krebs, cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family Proceedings of the National Academy of Sciences of the United States of America. ,vol. 86, pp. 5257- 5261 ,(1989) , 10.1073/PNAS.86.14.5257
Nicholas K. Tonks, Harry Charbonneau, Protein tyrosine dephosphorylation and signal transduction Trends in Biochemical Sciences. ,vol. 14, pp. 497- 500 ,(1989) , 10.1016/0968-0004(89)90184-9
E. B. Pasquale, S. J. Singer, Identification of a developmentally regulated protein-tyrosine kinase by using anti-phosphotyrosine antibodies to screen a cDNA expression library. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 86, pp. 5449- 5453 ,(1989) , 10.1073/PNAS.86.14.5449
Nihal S. De Silva, James W. Gurd, Charles Schwartz, Developmental alteration of rat brain synaptic membranes. Reaction of glycoproteins with plant lectins. Brain Research. ,vol. 165, pp. 283- 293 ,(1979) , 10.1016/0006-8993(79)90560-2
Tony Hunter, Protein-tyrosine phosphatases: the other side of the coin. Cell. ,vol. 58, pp. 1013- 1016 ,(1989) , 10.1016/0092-8674(89)90496-0
M E Greenberg, R Brackenbury, G M Edelman, Changes in the distribution of the 34-kdalton tyrosine kinase substrate during differentiation and maturation of chicken tissues. Journal of Cell Biology. ,vol. 98, pp. 473- 486 ,(1984) , 10.1083/JCB.98.2.473