Differential processing and turnover of the oncogenically activated neu/erb B2 gene product and its normal cellular counterpart.

作者: S S Huang , H A Koh , Y Konish , L D Bullock , J S Huang

DOI: 10.1016/S0021-9258(19)39772-8

关键词:

摘要: In nontransformed DHFR/G-8 cells (NIH 3T3 transfected with normal rat neu gene), the gene product was initially synthesized as a 170-kDa protein bearing endoglycosidase H-sensitive oligosaccharide chains and then processed to 175-kDa mature form H-resistant, F-sensitive chains. Most of this appeared on cell surface 2 h following synthesis showed half-life approximately 3 h. presence growth factor(s) partially purified from bovine kidney, shortened less than 30 min. B104-1-1 activated oncogenically by point mutation that changes valine residue glutamic acid in putative transmembrane region), also precursor However, diminished very fast only 185-kDa which exhibited The possessed an unidentified post-translational modification addition N-linked Both forms mutationally increased tyrosine-specific phosphorylation compared those their counterparts cells. shared several features have been reported previously for ligand-activated platelet-derived factor receptor v-sis- or c-sis-transformed These properties include: 1) accelerated turnover rates its counterparts, 2) insensitivity rapid lysosomotropic amines, 3) vivo both forms. findings suggest may transform mimicking ligand-induced activation.

参考文章(35)
C. I. Bargmann, R. A. Weinberg, Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion. The EMBO Journal. ,vol. 7, pp. 2043- 2052 ,(1988) , 10.1002/J.1460-2075.1988.TB03044.X
L T Williams, P M Tremble, M F Lavin, M E Sunday, Platelet-derived growth factor receptors form a high affinity state in membrane preparations. Kinetics and affinity cross-linking studies. Journal of Biological Chemistry. ,vol. 259, pp. 5287- 5294 ,(1984) , 10.1016/S0021-9258(17)42987-5
J S Huang, S S Huang, M D Kuo, Bovine brain-derived growth factor. Purification and characterization of its interaction with responsive cells. Journal of Biological Chemistry. ,vol. 261, pp. 11600- 11607 ,(1986) , 10.1016/S0021-9258(18)67285-0
Jonathan A. Cooper, Bartholomew M. Sefton, Tony Hunter, [42] Detection and quantification of phosphotyrosine in proteins Methods in Enzymology. ,vol. 99, pp. 387- 402 ,(1983) , 10.1016/0076-6879(83)99075-4
Y. Yarden, W. J. Kuang, T. Yang-Feng, L. Coussens, S. Munemitsu, T. J. Dull, E. Chen, J. Schlessinger, U. Francke, A. Ullrich, Human proto-oncogene c-kit: a new cell surface receptor tyrosine kinase for an unidentified ligand. The EMBO Journal. ,vol. 6, pp. 3341- 3351 ,(1987) , 10.1002/J.1460-2075.1987.TB02655.X
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
J A Escobedo, P J Barr, L T Williams, Role of tyrosine kinase and membrane-spanning domains in signal transduction by the platelet-derived growth factor receptor. Molecular and Cellular Biology. ,vol. 8, pp. 5126- 5131 ,(1988) , 10.1128/MCB.8.12.5126
Charles J. Sherr, Carl W. Rettenmier, Rosalba Sacca, Martine F Roussel, A. Thomas Look, E. Richard Stanley, The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF 1 Cell. ,vol. 41, pp. 665- 676 ,(1985) , 10.1016/S0092-8674(85)80047-7