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

FEBS Letters

Reisinger, R.³  Vargas, G.A.⁴  Hoeflich, A.³  Renner-Müller, I.³  Lahm, H.³  Elmlinger, M.W.²  Wolf, E.³  Russo, V.C.¹  Schuett, B.²  Jehle, P.M.⁴ 

[1] Centre for Hormone Research, Murdoch Childrens Research Institute, Parkville, Vic. 3052, Australia;University of Tübingen, 72076 Tübingen, Germany;Institute of Molecular Animal Breeding, Gene Center, Ludwig-Maximilian University, Feodor-Lynen-Str. 25, 81377 Munich, Germany;Department of Internal Medicine, 89081 Ulm, Germany

关键词: Insulin-like growth factor-binding protein-2;    Overexpression;    Transgenic mouse;    Cell surface association;    RGD sequence;   

DOI  :  10.1016/S0014-5793(02)02935-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown