Differential response of the epidermal growth factor receptor tyrosine kinase activity to several plant and mammalian lectins

Mol Cell Biochem. 1995 Jan 26;142(2):117-24. doi: 10.1007/BF00928932.


Biosignalling via lectins may involve modulation of protein kinase activities. This aspect of the biological action of mammalian and plant lectins has been investigated for their effect on the activity of the isolated epidermal growth factor receptor (EGFR). The constitutive tyrosine kinase activity of the epidermal growth factor receptor from rat liver, isolated by calmodulin-affinity chromatography, was activated by concanvalin A (ConA), and wheat germ agglutinin (WGA) to a similar extent as the measured enhancement induced by EGF. In contrast, two mannose-specific lectins, the mannan-binding protein (MBP) and serum amyloid P component (SAP), isolated from human serum, have inhibitory effects, both in the absence and presence of EGF. The differential effects of these lectins were tested using as phosphorylatable substrates a co-polymer of glutamic acid-tyrosine, as well as calmodulin. However, two galactoside-specific lectins, the laminin-binding beta-galactoside-binding 14 kDa lectin, isolated from bovine heart (14K-BHL), and the alpha/beta-galactoside-binding lectin, isolated from mistletoe (Viscum album L.) leaves (VAA), do not inhibit the EGFR tyrosine kinase activity. The sugar dependence of the lectin-mediated action was studied by inhibition assays. Mannose and a mannose-containing neoglycoprotein prevent the activating effect of ConA, and N-acetyl-D-glucosamine partially prevents the activation produced by WGA. However, mannose and mannose-containing neoglycoprotein were ineffective to reduce the inhibitory effect of MBP or SAP.(ABSTRACT TRUNCATED AT 250 WORDS)

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / pharmacology
  • Adenosine Triphosphate / metabolism
  • Animals
  • Calmodulin / metabolism
  • Carrier Proteins / metabolism
  • Carrier Proteins / pharmacology
  • Collectins
  • Concanavalin A / metabolism
  • Concanavalin A / pharmacology
  • Enzyme Activation
  • Epidermal Growth Factor / metabolism*
  • ErbB Receptors / antagonists & inhibitors
  • ErbB Receptors / metabolism*
  • Lectins / metabolism
  • Lectins / pharmacology*
  • Liver / enzymology
  • Liver / metabolism
  • Male
  • Mannose / pharmacology
  • Protein-Tyrosine Kinases / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Serum Amyloid P-Component / metabolism
  • Serum Amyloid P-Component / pharmacology
  • Signal Transduction / physiology
  • Wheat Germ Agglutinins / metabolism
  • Wheat Germ Agglutinins / pharmacology


  • Calmodulin
  • Carrier Proteins
  • Collectins
  • Lectins
  • Serum Amyloid P-Component
  • Wheat Germ Agglutinins
  • Concanavalin A
  • Epidermal Growth Factor
  • Adenosine Triphosphate
  • ErbB Receptors
  • Protein-Tyrosine Kinases
  • Mannose
  • Acetylglucosamine