Nima Naseri,1,*
1. Department of Clinical Biochemistry, Hamadan University of Medical Science, Hamadan, Iran
Introduction: IGFBP-3 is a member of the six binding protein family, which is known to be the major carrier of insulin-like growth factors 1 and 2 in serum. Through its N and C-terminal domains, IGFBP-3 involves binding to insulin-like growth factors and regulating the function of insulin-like growth factors in cell proliferation and differentiation, and regulates their function and bioavailability that is associated with the pathophysiology of several illnesses like Cancers and Diabetes. In the IGFBP-3 structure, certain amino acid domains and sequences are involved in binding to IGFs, which are highly conserved among the IGFBPs family. A recent study in 2020 showed that IGFBP-3 C- terminal domain-derived peptides in both Wild and Mutant forms, with significant potency similar to IGFBP-3, were able to bind to hyaluronans and like domain-derived peptides, binds to metalloproteinases. Therefore, by binding to extracellular matrix components such as heparin, hyaluronan, and proteases, this peptide prevents the binding of IGFBP-3 to the extracellular matrix, increases the free form of IGFBP-3, and the resistance of this protein to proteases.
Methods: The different articles associated with IGFBP-3 C-terminal peptide were searched and collected base on Mesh word advanced search in Pubmed.
Results: A recent study in 2020 showed that IGFBP-3 C- terminal domain-derived peptides in both Wild and Mutant forms, with significant potency similar to IGFBP-3, were able to bind to hyaluronans and like domain-derived peptides, binds to metalloproteinases.
Conclusion: Therefore, by binding to extracellular matrix components such as heparin, hyaluronan, and proteases, this peptide prevents the binding of IGFBP-3 to the extracellular matrix, increases the free form of IGFBP-3, and the resistance of this protein to proteases.