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Mutation of the RGD sequence does not affect plasma membrane association and growth inhibitory effects of elevated IGFBP‐2 in vivo
Author(s) -
Hoeflich A.,
Reisinger R.,
Vargas G.A.,
Elmlinger M.W.,
Schuett B.,
Jehle P.M.,
Renner-Müller I.,
Lahm H.,
Russo V.C.,
Wolf E.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02935-6
Subject(s) - in vivo , mutation , chemistry , inhibitory postsynaptic potential , sequence (biology) , cancer research , medicine , microbiology and biotechnology , endocrinology , biochemistry , biology , genetics , gene
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.