Modulation of p36 phosphorylation in human cells: studies using anti-p36 monoclonal antibodies

Mol Cell Biol. 1986 Jul;6(7):2745-51. doi: 10.1128/mcb.6.7.2745-2751.1986.

Abstract

We have characterized two monoclonal antibodies which recognize human p36. These have been used to examine the sites and extent of serine and tyrosine phosphorylation of p36 in human cells treated with epidermal growth factor and platelet-derived growth factor and in human cells transformed with viruses whose oncogenes encode protein-tyrosine kinases.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Annexins
  • Antibodies, Monoclonal*
  • Cell Transformation, Viral
  • Epidermal Growth Factor / pharmacology
  • Humans
  • Membrane Proteins / immunology
  • Membrane Proteins / metabolism*
  • Oncogene Protein pp60(v-src)
  • Oncogenes
  • Phosphorylation
  • Platelet-Derived Growth Factor / pharmacology
  • Protein-Tyrosine Kinases / genetics
  • Retroviridae Proteins / metabolism
  • Serine / metabolism
  • Tyrosine / metabolism

Substances

  • Annexins
  • Antibodies, Monoclonal
  • Membrane Proteins
  • Platelet-Derived Growth Factor
  • Retroviridae Proteins
  • Tyrosine
  • Serine
  • Epidermal Growth Factor
  • Protein-Tyrosine Kinases
  • Oncogene Protein pp60(v-src)