Analogs of human epidermal growth factor which partially inhibit the growth factor-dependent protein-tyrosine kinase activity of the epidermal growth factor receptor.

Abstract:

:Three site-directed mutants of human epidermal growth factor, Leu-26----Gly, Leu-47----Ala, and Ile-23----Thr, were examined for their ability to stimulate the protein-tyrosine kinase activity of the epidermal growth factor receptor. The receptor binding affinities of the mutant growth factors were 20- to 50-fold lower, as compared to wild-type growth factor. At saturating concentrations of growth factor, the velocities of the phosphorylation of exogenously added substrate and receptor autophosphorylation were significantly lower with the mutant analogs, suggesting a partial 'uncoupling' of signal transduction. The mutant analogs were shown to compete directly with the binding of wild-type, resulting in a decrease in growth factor-stimulated kinase activity.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Matsunami RK,Campion SR,Niyogi SK,Stevens A

doi

10.1016/0014-5793(90)80776-f

subject

Has Abstract

pub_date

1990-05-07 00:00:00

pages

105-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)80776-F

journal_volume

264

pub_type

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