A calcium-dependent 35-kilodalton substrate for epidermal growth factor receptor/kinase isolated from normal tissue

B. K. De, K. S. Misono, T. J. Lukas, B. Mroczkowski, S. Cohen

Research output: Contribution to journalArticlepeer-review

115 Scopus citations

Abstract

We have previously reported the isolation of a 35-kDa protein from A-431 cells that, in the presence of Ca2+, can serve as a substrate for the epidermal growth factor (EGF) receptor/tyrosine kinase. We now report the detection of an antigenically related 35-kDa protein in a number, but not all, of rat, pig, and human tissues. These antigenically related proteins also can serve as substrates for the EGF receptor/kinase in the presence of Ca2+. All of these proteins share the property of reversible, Ca2+-dependent binding to the particulate fraction (presumably membranes) of cell homogenates. We have isolated the 35-kDa substrate from porcine lung and have demonstrated that it is a Ca2+-binding protein. The amino-terminal sequence and the site of tyrosine phosphorylation therein have been determined. The positions of the acidic amino acid residues amino-terminal to the tyrosine phosphorylation site bear a distinct resemblance to the sequence in the homologous region of a number of other substrates for tyrosine kinases. Based on available data, the 35-kDa protein clearly differs from the protein I complex derived from intestinal mucosa and thought to be related to the proteins isolated herein. Finally, we report a striking sequence homology between the porcine 35-kDa described herein and human lipocortin, and phospholipase A2 inhibitor.

Original languageEnglish (US)
Pages (from-to)13784-13792
Number of pages9
JournalJournal of Biological Chemistry
Volume261
Issue number29
StatePublished - 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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