NDLI: Biochemical characterization of individual human glycosylated pro-insulin-like growth factor (IGF)-II and big-IGF-II isoforms associated with cancer.

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Biochemical characterization of individual human glycosylated pro-insulin-like growth factor (IGF)-II and big-IGF-II isoforms associated with cancer.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bentley, John D. Bartone, Nicola A. Cosgrove, Leah J. Baxter, Robert C. Pearce, Lesley A. Xiao, Xiaowen Scoble, Judith A. Adams, Timothy E. Sparrow, Lindsay G. Greenall, Sameer A.
Description	Author Affiliation: Greenall SA ( Division of Materials Science and Engineering, Commonwealth Scientific and Industrial Research Organisation, Parkville, Victoria 3052, Australia.)
Abstract	Insulin-like growth factor II (IGF-II) is a major embryonic growth factor belonging to the insulin-like growth factor family, which includes insulin and IGF-I. Its expression in humans is tightly controlled by maternal imprinting, a genetic restraint that is lost in many cancers, resulting in up-regulation of both mature IGF-II mRNA and protein expression. Additionally, increased expression of several longer isoforms of IGF-II, termed 'pro' and 'big' IGF-II, has been observed. To date, it is ambiguous as to what role these IGF-II isoforms have in initiating and sustaining tumorigenesis and whether they are bioavailable. We have expressed each individual IGF-II isoform in their proper O-glycosylated format and established that all bind to the IGF-I receptor and both insulin receptors A and B, resulting in their activation and subsequent stimulation of fibroblast proliferation. We also confirmed that all isoforms are able to be sequestered into binary complexes with several IGF-binding proteins (IGFBP-2, IGFBP-3, and IGFBP-5). In contrast to this, ternary complex formation with IGFBP-3 or IGFBP-5 and the auxillary protein, acid labile subunit, was severely diminished. Furthermore, big-IGF-II isoforms bound much more weakly to purified ectodomain of the natural IGF-II scavenging receptor, IGF-IIR. IGF-II isoforms thus possess unique biological properties that may enable them to escape normal sequestration avenues and remain bioavailable in vivo to sustain oncogenic signaling.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	1
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-01-04
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Insulin-Like Growth Factor II Chemistry Neoplasms Metabolism Animals Cell Proliferation Fibroblasts Cytology Gene Expression Regulation, Neoplastic Glycosylation HEK293 Cells Insulin-Like Growth Factor Binding Proteins Insulin-Like Growth Factor I Mass Spectrometry Mice Protein Binding Protein Isoforms Protein Structure, Tertiary Receptor Protein-Tyrosine Kinases Signal Transduction Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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