Transferrin binds insulin‐like growth factors and affects binding properties of insulin‐like growth factor binding protein‐3

@article{Storch2001TransferrinBI,  title={Transferrin binds insulin‐like growth factors and affects binding properties of insulin‐like growth factor binding protein‐3},  author={Stephan Storch and Bernd Kübler and Stefan H{\"o}ning and Michael Ackmann and Jürgen Zapf and Werner F Blum and Thomas Braulke},  journal={FEBS Letters},  year={2001},  volume={509},  url={https://api.semanticscholar.org/CorpusID:22895295}}

34 Citations

Interaction of Insulin-like Growth Factor II (IGF-II) with Multiple Plasma Proteins

The present data indicate that IGFs, low and high affinity IGFBPs, several IGFBP-associated proteins, and IGFBP proteases can interact, which may result in the formation of binary, ternary, and higher molecular weight complexes capable of modulating IGF binding properties and the stability of IGFB Ps.

Cellular actions of the insulin-like growth factor binding proteins.

In addition to their roles in IGF transport, the six IGF-binding proteins (IGFBPs) regulate cell activity in various ways and manipulation of IGFBP-regulated pathways is speculated to offer therapeutic opportunities in cancer and other diseases.

The importance of metal ions for the formation and isolation of insulin-like growth factor-binding protein 3-transferrin (IGFBP-3-Tf) complexes, and the analysis of their physiological involvement.

IGBP-3 appears to be a member of a network of iron-binding proteins that participates in cell signaling that involves iron-associated response, and is inversely correlated with the concentration of ferritin.

Cellular Internalization of Insulin-like Growth Factor Binding Protein-3

Together, these data indicate that the actions of IGFBP-3 are mediated by internalization via distinct endocytic pathways.

Prevention of Fas-mediated hepatic failure by transferrin

It is shown in a murine model that transferrin interferes with Fas-mediated hepatocyte death and liver failure and the data suggest that Tf has broader functions than previously recognized and may serve as a cytoprotective agent.

18 References

Plasminogen binds the heparin-binding domain of insulin-like growth factor-binding protein-3.

Competitive binding studies suggest that the kringle 1, 4, and 5 domains of Glu-Pg and the heparin-binding domain of IGFBP-3 participate in forming the IGF BP-3/GLU-Pg complex, and other studies show that Glu -Pg in this complex is activated at a normal rate by tissue Pg activator.

Insulin-like growth factor (IGF)-binding proteins: interactions with IGFs and intrinsic bioactivities.

The regulation of cell sensitivity to inhibitory IGFBP signaling may play a role in the growth control of malignant cells.

Identification of novel high molecular weight insulin-like growth factor-binding protein-3 association proteins in human serum.

It is concluded that there are several serum proteins in addition to ALS and IGFs that bind IGFBP-3 with high affinity that may serve as an additional reservoir of IGF BP-3 or modulate its functions.

Insulin-like Growth Factor-binding Protein-3 Binds Fibrinogen and Fibrin*

It is suggested that IGF-I can concentrate at wound sites by binding to fibrin-immobilized IGFBP-3, and that the lower IGF affinity of fibr in-bound IGF BP-3 allows IGF- I release to type I IGF receptors of stromal cells migrating into the fibrIn clot.

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…

ADAM 12, a Disintegrin Metalloprotease, Interacts with Insulin-like Growth Factor-binding Protein-3*

The data suggest that ADAM 12-S has IGF BP-3 protease activity, and it may contribute to the IGFBP-3 proteolytic cleavage activity present in pregnancy serum.

Partial IGF affinity of circulating N- and C-terminal fragments of human insulin-like growth factor binding protein-4 (IGFBP-4) and the disulfide bonding pattern of the C-terminal IGFBP-4 domain.

This study provides the first molecular characterization of circulating human IGFBP-4 fragments formed in vivo exhibiting an at least 5-fold decrease in the affinity of the N-terminal IGF BP-4 fragment for the IGFs and a very low IGF binding capacity of the C-Terminal fragment.

Insulin‐Like Growth Factor‐I and Transferrin Mediate Growth and Survival of Chinese Hamster Ovary Cells

Results indicate that IGF‐I alone is able to maintain the viability of CHO cells for an extended length of time in the absence of serum, and IGF-I alone does not stimulate cell proliferation but is a requirement for growth in serum‐free medium in cooperation with transferrin.

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