Increased pp60(c-src) tyrosyl kinase activity in human neuroblastomas is associated with amino-terminal tyrosine phosphorylation of the src gene product Academic Article uri icon

Overview

MeSH Major

  • Neoplasm Proteins
  • Neuroblastoma
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins

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.

publication date

  • December 1985

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC390832

PubMed ID

  • 2414774

Additional Document Info

start page

  • 7275

end page

  • 9

volume

  • 82

number

  • 21