Key result
Affinity chromatography demonstrated that most circulating IGFBP-1 exists in complexes with α2-macroglobulin, which can be differentiated from dimers and multimers using lectin-affinity methods.
Affinity chromatography methods can successfully separate different molecular forms of IGFBP-1, revealing that most circulating IGFBP-1 exists in complexes with α2-macroglobulin.
Hypothesis-generating in animal models; human cardiovascular studies required before any clinical measurement or mechanistic inferences.
Insulin-like growth factor-binding protein 1 (IGFBP-1) is a member of a family of six homologous proteins that regulate the action of the insulin-like growth factors. IGFBP-1 is a 25 kDa protein that beside its native form, may exist in several phosphoforms (30 kDa), which are predominant in the circulation of humans. Phosphorylation of IGFBP-1 is a post-translational modification that has a great influence on the IGF-I action. IGFBP-1 forms multimers and complexes with ?2-macroglobulin (?2M). Polymerisation of IGFBP-1 was also reported. In order to analyse and separate these IGFBP-1 molecular species, affinity chromatography methods were used in this study. The results demonstrated that most of the IGFBP-1 circulates in complexes with ?2M, which can be isolated by affinity chromatography using immobilised anti-?2M antibodies. IGFBP- 1/?2M complexes may be differentiated from IGFBP-1 dimer and multimers using lectin-affinity chromatography, since the latter do not interact with lectins. It seems that the complexes contain not only monomeric IGFBP-1, but also its multimers. Dimer and multimers are stable under reducing conditions, suggesting covalent linkage between units. Free IGFBP-1 monomer can be separated from multimers using Con A-affinity chromatography. The concentration of free IGFBP-1 is relatively low in the circulation.
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Lagundžin et al. (2010) studied this question. Affinity chromatography methods was evaluated on Separation and analysis of IGFBP-1 molecular species. Affinity chromatography demonstrated that most circulating IGFBP-1 exists in complexes with α2-macroglobulin, which can be differentiated from dimers and multimers using lectin-affinity methods.
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