IGFBPs and cancer

Peng Fang, Vivian Hwa, Ronald (Ron) Rosenfeld

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The proposed insulin-like growth factor binding protein (IGFBP) superfamily are a group of secreted proteins that are structurally, functionally and evolutionarily related, and include six IGFBPs and over 10 IGFBP-related proteins. The IGFBPs have high affinities for insulin-like growth factors (IGFs), thereby modulating the mitogenic, anti-apoptotic and metabolic actions of IGFs. In addition, IGFBPs, particularly IGFBP-3, also have IGF-independent, anti-proliferative and pro-apoptotic functions. The IGFBPs are, in turn, modulated by proteolysis. Epidemiological data correlating serum IGF/ IGFBP levels with the risk of several human cancers suggest a possible protective role for IGFBP-3. In vitro studies suggest that the potential protective effects of IGFBP-3 involve both IGF-dependent and IGF-independent mechanisms. Further studies are necessary to demonstrate whether the ability of IGFBPs to inhibit the proliferation of cancer cells under in vitro conditions has significant clinical implications.

Original languageEnglish (US)
Title of host publicationBiology of IGF-1
Subtitle of host publicationIts Interaction with Insulin in Health and Malignant States
Publisherwiley
Pages215-230
Number of pages16
Volume262
ISBN (Electronic)9780470869970
ISBN (Print)9780470869987
DOIs
StatePublished - Oct 7 2008
Externally publishedYes

Keywords

  • Altered serum IGFs and IGFBP-3 concentrations
  • Conserved N-terminal domain
  • IGF-binding affinity of IGFBPs
  • IGF-dependent and IGF-independent mechanisms
  • IGFBP inhibitory effects regulation
  • IGFBP superfamily
  • IGFBP-3 and antitumorigenesis
  • IGFBPs and human cancer
  • Insulin-like growth factor binding protein (IGFBP)
  • Matrix metalloproteinases (MMPs)

ASJC Scopus subject areas

  • Medicine(all)

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  • Cite this

    Fang, P., Hwa, V., & Rosenfeld, R. R. (2008). IGFBPs and cancer. In Biology of IGF-1: Its Interaction with Insulin in Health and Malignant States (Vol. 262, pp. 215-230). wiley. https://doi.org/10.1002/0470869976.ch14