Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/9932
Title: IGF-binding proteins--the pieces are falling into place.
Authors: Bach, Leon A;Headey, Stephen J;Norton, Raymond S
Affiliation: University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg 3084, Australia. l.bach@unimelb.edu.au
Issue Date: 1-Jul-2005
Citation: Trends in Endocrinology and Metabolism: Tem; 16(5): 228-34
Abstract: The six insulin-like growth factor (IGF)-binding proteins (IGFBPs) are important regulators of IGF actions. IGF-independent actions of several IGFBPs have also been described. IGFBPs contain highly conserved N- and C-terminal domains, both of which are important for high-affinity IGF binding. The C-domain also binds a large number of other biomolecules, thereby modulating IGF binding and mediating IGF-independent effects. The 3D structures of the IGF-binding region of the N-domain of IGFBP-5 and the entire C-domain of IGFBP-6 have been solved recently, providing new insights into IGFBP modulation of IGF actions, and structural studies might be expected to do the same for IGF-independent actions. IGFBP-based therapies for diseases such as cancer are promising, and this recent progress will enhance their development.
Internal ID Number: 15935690
URI: http://ahro.austin.org.au/austinjspui/handle/1/9932
DOI: 10.1016/j.tem.2005.05.005
URL: http://www.ncbi.nlm.nih.gov/pubmed/15935690
Type: Journal Article
Subjects: Animals
Humans
Insulin-Like Growth Factor Binding Proteins.chemistry.genetics.physiology
Models, Molecular
Appears in Collections:Journal articles

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