PMID- 16831875
OWN - NLM
STAT- MEDLINE
DCOM- 20061218
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 281
IP  - 36
DP  - 2006 Sep 8
TI  - Hybrid receptors formed by insulin receptor (IR) and insulin-like growth factor I 
      receptor (IGF-IR) have low insulin and high IGF-1 affinity irrespective of the IR 
      splice variant.
PG  - 25869-74
AB  - Insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) are both 
      from the same subgroup of receptor tyrosine kinases that exist as covalently 
      bound receptor dimers at the cell surface. For both IR and IGF-IR, the most 
      described forms are homodimer receptors. However, hybrid receptors consisting of 
      one-half IR and one-half IGF-IR are also present at the cell surface. Two splice 
      variants of IR are expressed that enable formation of two isoforms of the 
      IGF-IR/IR hybrid receptor. In this study, these two splice variants of hybrid 
      receptors were studied with respect to binding affinities of insulin, 
      insulin-like growth factor I (IGF-I), and insulin-like growth factor II (IGF-II). 
      Unlike previously published data, in which semipurified receptors have been 
      studied, we found that the two hybrid receptor splice variants had similar 
      binding characteristics with respect to insulin, IGF-I, and IGF-II binding. We 
      studied both semipurified and purified hybrid receptors. In all cases we found 
      that IGF-I had at least 50-fold higher affinity than insulin, irrespective of the 
      splice variant. The binding characteristics of insulin and IGF-I to both splice 
      variants of the hybrid receptors were similar to classical homodimer IGF-IR.
FAU - Slaaby, Rita
AU  - Slaaby R
AD  - Novo Nordisk A/S, Novo Alle, DK-2880 Bagsvaerd, Denmark. risl@novonordisk.com
FAU - Schaffer, Lauge
AU  - Schaffer L
FAU - Lautrup-Larsen, Inger
AU  - Lautrup-Larsen I
FAU - Andersen, Asser Sloth
AU  - Andersen AS
FAU - Shaw, Allan Christian
AU  - Shaw AC
FAU - Mathiasen, Ida Stenfeldt
AU  - Mathiasen IS
FAU - Brandt, Jakob
AU  - Brandt J
LA  - eng
PT  - Journal Article
DEP - 20060710
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Insulin)
RN  - 0 (Protein Isoforms)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 67763-96-6 (Insulin-Like Growth Factor I)
RN  - EC 2.7.10.1 (Receptor, IGF Type 1)
RN  - EC 2.7.10.1 (Receptor, Insulin)
SB  - IM
MH  - *Alternative Splicing
MH  - Animals
MH  - Cell Line
MH  - Cricetinae
MH  - Exons
MH  - Humans
MH  - Insulin/*metabolism
MH  - Insulin-Like Growth Factor I/*metabolism
MH  - Protein Binding
MH  - Protein Isoforms/genetics/*metabolism
MH  - Receptor, IGF Type 1/genetics/isolation & purification/*metabolism
MH  - Receptor, Insulin/genetics/isolation & purification/*metabolism
MH  - Recombinant Fusion Proteins/genetics/isolation & purification/*metabolism
EDAT- 2006/07/13 09:00
MHDA- 2006/12/19 09:00
CRDT- 2006/07/13 09:00
PHST- 2006/07/13 09:00 [pubmed]
PHST- 2006/12/19 09:00 [medline]
PHST- 2006/07/13 09:00 [entrez]
AID - S0021-9258(19)35114-2 [pii]
AID - 10.1074/jbc.M605189200 [doi]
PST - ppublish
SO  - J Biol Chem. 2006 Sep 8;281(36):25869-74. doi: 10.1074/jbc.M605189200. Epub 2006 
      Jul 10.