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|Title:||Insulin-like growth factor binding protein-6: the "forgotten" binding protein?||Austin Authors:||Bach, Leon A||Affiliation:||University of Melbourne, Department of Medicine, Austin & Repatriation Medical Centre, Heidelberg, Victoria, Australia||Issue Date:||3-Feb-1999||Publication information:||Hormone and Metabolic Research = Hormon- Und Stoffwechselforschung = Hormones Et Me´tabolisme; 31(2-3): 226-34||Abstract:||Insulin-like growth factor binding protein-6 (IGFBP-6) differs from IGFBPs 1-5 in that it binds IGF-II with marked preferential affinity over IGF-I. Human and rat IGFBP-6 lack 2 and 4 N-terminal cysteines and therefore the Gly-Cys-Gly-Cys-Cys motif present in IGFBPs 1-5. IGFBP-6 is O-glycolsylated, and five serine/threonine glycosylation sites in the non-conserved mid-region of human IGFBP-6 have been identified. O-Glycosylation inhibits proteolysis of IGFBP-6 by chymotrypsin and trypsin, but has no effect on high affinity IGF binding. IGFBP-6 is a relatively specific inhibitor of IGF-II actions; it has not been shown to potentiate IGF actions. IGFBP-6 is only cell-associated to a very limited extent, if at all. IGFBP-6 is often expressed in non-proliferative, quiescent states in vitro and differentiating agents increase its expression. IGFBP-6 expression is associated with inhibition of growth of tumour cells in vitro and in vivo. Although many questions remain regarding the biological role of IGFBP-6, its major function appears to be the regulation of IGF-II actions. This could be especially significant since IGF-II has been implicated as an autocrine tumour growth factor.||Gov't Doc #:||10226806||URI:||http://ahro.austin.org.au/austinjspui/handle/1/9151||DOI:||10.1055/s-2007-978723||URL:||https://pubmed.ncbi.nlm.nih.gov/10226806||Type:||Journal Article||Subjects:||Amino Acid Sequence
Insulin-Like Growth Factor Binding Protein 6.genetics.metabolism
Molecular Sequence Data
|Appears in Collections:||Journal articles|
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