Molecular and Cellular Biochemistry

, Volume 142, Issue 2, pp 117–124 | Cite as

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

  • Fu-Yue Zeng
  • Alberto Benguría
  • Sabine Kafert
  • Sabine André
  • Hans-J. Gabius
  • Antonio Villalobo


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 concanavalin 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 β-galactoside-binding 14 kDa lectin, isolated from bovine heart (14K-BHL), and the α/β-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. Although the response to binding of ConA and WGA was different to that of MBP or SAP with respect to the tyrosine kinase activity of the EGFR, it should be noted that the four lectins inhibited the binding of [125I]EGF to its receptor with similar efficiency.

Key Words

epidermal growth factor receptor tyrosine kinase lectin concanavalin A wheat germ agglutinin mannan-binding protein serum amyloid P component 



epidermal growth factor


epidermal growth factor receptor


concanavalin A


mannan-binding protein


serum amyloid P component


wheat germ agglutinin


bovine heart 14 kDa lectin


Viscum album L. (mistletoe) agglutinin


[ethylenebis(oxyethylenenitrilo)]-tetraacetic acid; poly(Glu:Tyr)-co-polymer of L-glutamic acid and L-tyrosine


4-(2-hydroxyethyl)-1-piperazinethanesulfonic acid




suberic acid bis(N-hydroxy-succinimide ester)


phenylmethanesulfonyl fluoride






bovine serum albumin


neoglycoprotein containing α-D-mannose


neoglycoprotein containing β-lactose


neoglycoprotein containing galactose


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Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • Fu-Yue Zeng
    • 2
  • Alberto Benguría
    • 1
  • Sabine Kafert
    • 1
  • Sabine André
    • 2
  • Hans-J. Gabius
    • 2
  • Antonio Villalobo
    • 1
  1. 1.Instituto de Investigaciones BiomédicasConsejo Superior de Investigaciones CientíficasMadridSpain
  2. 2.Institut für Physiologische Chemie der Tierärztlichen FakultätLudwig-Maximilians-UniversitätMünchenGermany

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