PMID- 10471394
OWN - NLM
STAT- MEDLINE
DCOM- 19991007
LR  - 20191210
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 262
IP  - 3
DP  - 1999 Sep 7
TI  - Characterization of the VEGF binding site on the Flt-1 receptor.
PG  - 731-8
AB  - The angiogenic growth factor VEGF binds to the receptor tyrosine kinases Flt-1
      and KDR/Flk-1. Immunoglobulin (Ig)-like loop-2 of Flt-1 is involved in binding
      VEGF, but the contribution of other Flt-1 Ig-loops to VEGF binding remains
      unclear. We tested the ability of membrane-bound chimeras between the
      extracellular domain of Flt-1 and the cell adhesion molecule embigin to bind
      VEGF. VEGF bound as well to receptors containing Flt-1 loops 1-2 or 2-3 as it did
      to the entire Flt-1 extracellular domain. Chimeras containing only loop-2 of
      Flt-1 bound VEGF with 22-fold lower affinity. We conclude that high-affinity VEGF
      binding requires Ig-like loop-2 plus either loop-1 or loop-3. In addition, Flt-1 
      amino acid residues Arg-224 and Asp-231 were not essential for high-affinity
      binding of VEGF to membrane-bound Flt-1.
CI  - Copyright 1999 Academic Press.
FAU - Herley, M T
AU  - Herley MT
AD  - Biochemistry Department, St. Jude Children's Research Hospital, Memphis,
      Tennessee, USA.
FAU - Yu, Y
AU  - Yu Y
FAU - Whitney, R G
AU  - Whitney RG
FAU - Sato, J D
AU  - Sato JD
LA  - eng
SI  - GENBANK/AF063657
SI  - GENBANK/AJ009698
GR  - DK38639/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (DNA Primers)
RN  - 0 (EMB protein, human)
RN  - 0 (Emb protein, rat)
RN  - 0 (Endothelial Growth Factors)
RN  - 0 (Glycoproteins)
RN  - 0 (Lymphokines)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Receptors, Growth Factor)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Vascular Endothelial Growth Factor A)
RN  - 0 (Vascular Endothelial Growth Factors)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
RN  - EC 2.7.10.1 (Receptors, Vascular Endothelial Growth Factor)
RN  - EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-1)
SB  - IM
MH  - Amino Acid Substitution
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Cloning, Molecular
MH  - DNA Primers
MH  - Endothelial Growth Factors/*metabolism
MH  - Glycoproteins/chemistry/metabolism
MH  - Humans
MH  - Kinetics
MH  - Lymphokines/*metabolism
MH  - Membrane Glycoproteins
MH  - Membrane Proteins
MH  - Molecular Chaperones
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Protein Structure, Secondary
MH  - Proto-Oncogene Proteins/chemistry/genetics/*metabolism
MH  - Rats
MH  - Receptor Protein-Tyrosine Kinases/chemistry/genetics/*metabolism
MH  - Receptors, Growth Factor/chemistry/genetics/*metabolism
MH  - Receptors, Vascular Endothelial Growth Factor
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Recombinant Proteins/metabolism
MH  - Restriction Mapping
MH  - Vascular Endothelial Growth Factor A
MH  - Vascular Endothelial Growth Factor Receptor-1
MH  - Vascular Endothelial Growth Factors
EDAT- 1999/09/02 00:00
MHDA- 1999/09/02 00:01
CRDT- 1999/09/02 00:00
PHST- 1999/09/02 00:00 [pubmed]
PHST- 1999/09/02 00:01 [medline]
PHST- 1999/09/02 00:00 [entrez]
AID - 10.1006/bbrc.1999.1282 [doi]
AID - S0006-291X(99)91282-2 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Sep 7;262(3):731-8. doi: 10.1006/bbrc.1999.1282.