[Comparison of the effect of the epidermal growth factor (EGF) and its cyanogen bromide derivative on EGF receptor phosphorylation and uridine uptake in a cell culture]. Tsitologiia 1987 Aug;29(8):911-6
Date
08/01/1987Pubmed ID
3500535Scopus ID
2-s2.0-0023393170 (requires institutional sign-in at Scopus site)Abstract
In contrast to the intact EGF, a cyanogen bromide derivative of EGF (EGF-CNBr) does not induce an increase in uridine phosphorylation rate in 3T3 cells, the ability of the EGF-CNBr to stimulate autophosphorylation of the EGF-receptor in A-431 cells being reserved. EGF and EGF-CNBr were used in concentrations promoting their equivalent binding with EGF receptor in both the series of experiments, which was necessary because of a decreased affinity to binding EGF-CNBr. Thus, the EGF-induced receptor autophosphorylation was not enough for uridine kinase activation. The differences between EGF and EGF-CNBr cellular processing made it possible to discuss potential ways of uridine-kinase activity regulation during the early period of stimulation of quiescent cell cultures.
Author List
Nesterov AM, Sorokin AB, Okulova AN, Nikol'skiĭ NNAuthor
Andrey Sorokin PhD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsCell Line
Cells, Cultured
Cyanogen Bromide
Enzyme Activation
Enzyme Induction
Epidermal Growth Factor
ErbB Receptors
Humans
Mice
Phosphorylation
Protein Kinases
Tumor Cells, Cultured
Uridine
Uridine Kinase