Insulin-like growth factor binding proteins (IGFBPs ) contain insulin-like growth factor (IGF) binding domain and play an important role in the regulation of numerous metabolic and proliferative processes mainly through interaction with IGF1 and IGF2, their cell surface receptors as well as insulin receptor, alter the half-life of the IGFs, modifying their biological activity. It is well known that insulin-like growth factors and the signal transduction networks play important roles in tumorigenesis and metastasis as well as in metabolic diseases [1,2]. IGFBPs participate in endoplasmic reticulum stress, which is an important factor of tumor growth, insulin resistance, and obesity [3][4][5]. It is interesting to note that there is the cross talk between IGF and insulin receptor signaling pathways at the receptor level or at downstream signaling level. This cross talk significantly changed a variety of cancers as a result of insulin receptor isoform. A formation of hybrid receptor isoforms between receptors for IGF1 and insulin, which are sensitive to the stimulation of all three IGF axis ligands, as well as hybrid receptors of IGF1/insulin receptor with other tyrosine kinase potentiate the transformation of cells, tumorigenesis, and tumor neovascularization [6].The IGFBPs have different affinity for insulin-like growth factors. They bind and regulate the availability of both insulin-like growth factors and inhibit or stimulate the growth promoting effects of the IGFs through IGF/INS receptors and through other signaling pathways and regulate cell proliferation and survival as well as angiogenesis and cancer експериментальні роботи doi: http://dx