Literature DB >> 1709017

Isolation of a novel insulin-like growth factor (IGF) binding protein from human bone: a potential candidate for fixing IGF-II in human bone.

C M Bautista1, D J Baylink, S Mohan.   

Abstract

Insulin-like growth factor-II (IGF-II) is the most abundant growth factor stored in human bone. Upon release from this storage depot, IGF-II could act in bone repair and in the coupling of bone formation to bone resorption, a process inherent to bone which is a key regulatory process for maintenance of bone tissue. In this study, we report the isolation and characterization of a novel IGF binding protein (IGFBP) from human bone and describe how this IGFBP may be involved in the fixation of IGF-II in human bone. This new IGFBP has an apparent molecular weight of 29 kDa and has several fold higher affinity for IGF-II than IGF-I which could explain the much greater abundance of IGF-II than IGF-I in human bone. In terms of biological activity, this IGFBP was found to potentiate the proliferative actions of IGF-II on bone cells. This work raises the possibility that this IGFBP may participate in mediating some of the actions of IGF-II.

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Year:  1991        PMID: 1709017     DOI: 10.1016/s0006-291x(05)80249-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  18 in total

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5.  Effects of systemic and local administration of recombinant human IGF-I (rhIGF-I) on de novo bone formation in an aged mouse model.

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7.  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.

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Review 8.  Non-Canonical (RANKL-Independent) Pathways of Osteoclast Differentiation and Their Role in Musculoskeletal Diseases.

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