Insulin-like growth factor-binding protein

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
SCOPe1boe / SUPFAM

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:

gollark: u is just what people who can't type µ or μ say for micro.
gollark: It's consistently atrociously terrible, yes.
gollark: Having to multiply and divide by a thousand all the time for various units was so mildly annoying when I did chemistry last year.
gollark: A 1g reference would have been small and thus uncool.
gollark: Maybe because the kilogram was based on an actual physical object until recently.

See also

References

  1. Kalus W, Zweckstetter M, Renner C, et al. (November 1998). "Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions" (PDF). EMBO J. 17 (22): 6558–72. doi:10.1093/emboj/17.22.6558. PMC 1171003. PMID 9822601.
  2. Hwa V, Oh Y, Rosenfeld RG (December 1999). "The insulin-like growth factor-binding protein (IGFBP) superfamily". Endocr. Rev. 20 (6): 761–87. doi:10.1210/er.20.6.761. PMID 10605625.
  3. Clemmons DR, Busby WH, Arai T, Nam TJ, Clarke JB, Jones JI, Ankrapp DK (1995). "Role of insulin-like growth factor binding proteins in the control of IGF actions". Prog. Growth Factor Res. 6 (2–4): 357–66. doi:10.1016/0955-2235(95)00013-5. PMID 8817679.
  4. Stewart CE, Bates PC, Calder TA, Woodall SM, Pell JM (September 1993). "Potentiation of insulin-like growth factor-I (IGF-I) activity by an antibody: supportive evidence for enhancement of IGF-I bioavailability in vivo by IGF binding proteins". Endocrinology. 133 (3): 1462–5. doi:10.1210/en.133.3.1462. PMID 7689959.
  5. Gregory CW, DeGeorges A, Sikes RA (2001). "The IGF axis in the development and progression of prostate cancer". Recent Research Developments in Cancer: 437–462. ISBN 81-7895-002-2.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.