Increased Pp60c-src Tyrosyl Kinase Activity in Human Neuroblastomas is Associated with Amino-terminal Tyrosine Phosphorylation of the Src Gene Product

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1985 Nov 1

PMID 2414774

Citations 41

Authors

J B Bolen

N Rosen

M A Israel

Affiliations

Soon will be listed here.

Abstract

We have observed a 20- to 40-fold increase in pp60c-src tyrosyl kinase activity in human neuroblastoma cell lines over that found in either human glioblastoma cells or human fibroblasts. The level of c-src gene transcripts and pp60c-src protein synthesis in the neuroblastoma cells was not significantly increased when compared to the levels found in glioblastoma cells. Approximately one-half of the pp60c-src molecules synthesized during a 4-hr [35S]methionine or [32P]orthophosphate labeling period in neuroblastoma cells were found to migrate more slowly on NaDodSO4/polyacrylamide gels than pp60c-src molecules labeled in glioblastoma cells. Peptide and phosphoamino acid analysis of the in vivo phosphorylated c-src molecules from these two cell types revealed that pp60c-src molecules from the neuroblastoma cells possess in the amino-terminal portion of the protein at least one unique tyrosine phosphorylation site not found in pp60c-src derived from glioblastoma cells.

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