Purification and characterization of the insulin-like growth factor-binding protein-1 phosphoform found in normal plasma.

@article{Westwood1997PurificationAC,
  title={Purification and characterization of the insulin-like growth factor-binding protein-1 phosphoform found in normal plasma.},
  author={Melissa Westwood and J Martin Gibson and A. White},
  journal={Endocrinology},
  year={1997},
  volume={138 3},
  pages={
          1130-6
        }
}
Our previous work has shown that, in the normal circulation, insulin-like growth factor-binding protein-1 (IGFBP-1) is present as a single highly phosphorylated species. In this study, we have purified this previously uncharacterized isoform of IGFBP-1 to determine its ligand-binding affinity and the potential significance of highly phosphorylated IGFBP-I. Immunoaffinity chromatography was used to isolate IGFBP-1 from normal human plasma and from human hepatoma (Hep G2) cell medium as an… 
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Specific cleavage of insulin-like growth factor-binding protein-1 by a novel protease activity
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It is concluded that specific cleavage of IGF BP-1 at target tissues is important in cellular growth and metabolism and opens novel strategies for targeting IGFBP-1 in treatment of disease.
Phosphorylation of rat insulin-like growth factor binding protein-1 does not affect its biological properties.
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Rat IGF BP-1 is phosphorylated on two sites by reactions that occur in different secretory organelles and that similar to human IGFBP-3, but unlike human IGFbp-1, phosphorylation does not affect its affinity for IGF-I.
Functional and Complementary Phosphorylation State Attributes of Human Insulin-like Growth Factor-Binding Protein-1 (IGFBP-1) Isoforms Resolved by Free Flow Electrophoresis
TLDR
The data demonstrate that phosphorylation at Ser119 plays a significant role in modulating affinity of IGFBP-1 for IGF-I, and an altered profile of IGF BP-1 phosphoisoforms was revealed between FGR and healthy pregnancies that may result from potential site-specific phosphorylated.
Separation of the molecular forms of the insulin-like growth factor (IGF)-Binding proteins by affinity chromatography.
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Insulin-Like Growth Factor Binding Protein-6: Posttranslational modifications and sorting in polarized MDCK cells
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The present study indicates that the complex regulation of IGF actions in MDCK cells involve IGFBPs and IGFBP-proteases and suggests that mIGFBP-6 is capable of modulating important physiological processes like proliferation and migration.
Physiological differences in insulin-like growth factor binding protein-1 (IGFBP-1) phosphorylation in IGFBP-1 transgenic mice.
TLDR
The phosphorylation state of human IGFBP-1 may account for part of the phenotypic differences noted in the two studies of transgenic mice, and it is an important determinant of the capacity of human insulin-like growth factor binding protein (IGFBP) to inhibit IGF-1 actions in vivo.
The role of placental alkaline phosphatase in the regulation of insulin-like growth factor binding protein-1 in pregnancy complicated by diabetes.
TLDR
Fetal overgrowth in pregnancy with diabetes may be a consequence of elevated IGF-I action at the placenta secondary to increased PLAP activity, and this process is catalyzed by placental alkaline phosphatase (PLAP).
The insulin-like growth factor-binding protein (IGFBP) superfamily.
Over the last decade, the concept of an IGFBP family has been well accepted, based on structural similarities and on functional abilities to bind IGFs with high affinities. The existence of other…
Placental alkaline phosphatase de-phosphorylates insulin-like growth factor (IGF)-binding protein-1.
Multiple post-translational modifications of mouse insulin-like growth factor binding protein-6 expressed in epithelial Madin–Darby canine kidney cells
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References

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TLDR
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TLDR
Competitive binding curves using pure BP and human IGF-I and IGF-II as both labeled and unlabeled ligands indicated association constants of 2-3 X 10(10) liters/mol for both peptides, with a slightly higher affinity for IGF- II than IGF- I, and 0.9 binding sites for either peptide per 53-kDa protein.
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TLDR
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TLDR
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TLDR
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TLDR
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