Mutation of the RGD sequence does not affect plasma membrane association and growth inhibitory effects of elevated IGFBP-2 in vivo

FEBS Lett. 2002 Jul 17;523(1-3):63-7. doi: 10.1016/s0014-5793(02)02935-6.

Abstract

Using insulin-like growth factor-binding protein-2 (IGFBP-2) transgenic mice (D mice) as a model of elevated IGFBP-2 expression, which is often found in unphysiological conditions, we found association of IGFBP-2 to purified plasma membranes of many organs. To determine whether the RGD (Arg-Gly-Asp) motif of IGFBP-2 mediates cell surface binding in vivo, we mutated the RGD motif of IGFBP-2 into an RGE (Arg-Gly-Glu) sequence and produced transgenic mice (E mice) which express elevated amounts of mutated IGFBP-2. Our data demonstrate that in vivo IGFBP-2 cell surface association is not dependent on the RGD motif and that mutation of this sequence does not alter growth inhibitory effects of IGFBP-2.

MeSH terms

  • Amino Acid Motifs / genetics
  • Amino Acid Motifs / physiology
  • Animals
  • Body Weight / genetics
  • Body Weight / physiology*
  • Cell Membrane / metabolism
  • Insulin-Like Growth Factor Binding Protein 2 / blood
  • Insulin-Like Growth Factor Binding Protein 2 / genetics
  • Insulin-Like Growth Factor Binding Protein 2 / metabolism*
  • Insulin-Like Growth Factor I / analysis
  • Insulin-Like Growth Factor I / metabolism
  • Insulin-Like Growth Factor II / analysis
  • Insulin-Like Growth Factor II / metabolism
  • Membrane Proteins / blood
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Transgenic / growth & development
  • Mice, Transgenic / physiology
  • Oligopeptides / genetics
  • Oligopeptides / metabolism*
  • Organ Size / genetics
  • Organ Size / physiology
  • Point Mutation

Substances

  • Insulin-Like Growth Factor Binding Protein 2
  • Membrane Proteins
  • Oligopeptides
  • Insulin-Like Growth Factor I
  • Insulin-Like Growth Factor II
  • arginyl-glycyl-aspartic acid