Insulin-like growth factor-binding protein

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The insulin-like growth factor-binding protein (IGFBP) serves as a transport protein for insulin-like growth factor 1 (IGF-1).[2]

Insulin-like growth factor
binding protein
Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5)[1]
Identifiers
SymbolIGFBP
PfamPF00219
InterProIPR000867
SMARTSM00121
PROSITEPDOC00194
SCOP21boe / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1boe​, 1h59

Function

Approximately 98% of IGF-1 is always bound to one of six binding proteins (IGF-BP). IGFBP-3, the most abundant protein, accounts for 80% of all IGF binding. IGF-1 binds to IGFBP-3 in a 1:1 molar ratio. IGF-BP also binds to IGF-1 inside the liver, allowing growth hormone to continuously act upon the liver to produce more IGF-1.

IGF binding proteins (IGFBPs) are proteins of 24 to 45 kDa. All six IGFBPs share 50% homology with each other and have binding affinities for IGF-I and IGF-II at the same order of magnitude as the ligands have for the IGF-IR.[3]

The IGFBPs help to lengthen the half-life of circulating IGFs in all tissues, including the prostate.[4] Individual IGFBPs may act to enhance or attenuate IGF signaling depending on their physiological context (i.e. cell type). Even with these similarities, some characteristics are different: chromosomal location, heparin binding domains, RGD recognition site, preference for binding IGF-I or IGF-II, and glycosylation and phosphorylation differences.[5] These structural differences can have a tremendous impact on how the IGFBPs interact with cellular basement membranes.

Family members

In humans, IGFBPs are transcribed from the following seven genes:

See also

References