Essential roles of IGFBP-3 and IGFBP-rP1 in breast cancer

• Published in: European journal of cancer (1990) Vol. 41; no. 11; pp. 1515 - 1527
• Main Authors: Burger, Angelika M., Leyland-Jones, Brian, Banerjee, Kris, Spyropoulos, Demetri D., Seth, Arun K.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.07.2005; Elsevier
• Subjects: Biological and medical sciences; Breast cancer; Breast Neoplasms - etiology; Breast Neoplasms - therapy; Cell Communication - physiology; Female; Humans; IGFBP-related protein 1; Insulin-Like Growth Factor Binding Protein 3 - metabolism; Insulin-Like Growth Factor Binding Protein 3 - physiology; Insulin-Like Growth Factor Binding Protein 3 - therapeutic use; Insulin-Like Growth Factor Binding Proteins - metabolism; Insulin-Like Growth Factor Binding Proteins - physiology; Insulin-Like Growth Factor Binding Proteins - therapeutic use; Insulin-like growth factor-binding protein 3; Medical sciences; Pharmacology. Drug treatments; Recombinant Proteins - therapeutic use; Therapeutic possibilities; Tumors; Insulin-like growth factor-binding protein 3; Breast cancer; IGFBP-related protein 1; Therapeutic possibilities; Mammary gland diseases; Insulin-like growth factor binding protein-3; Cancerology; Treatment; Insulin like growth factor binding protein 1; Pharmacology; Malignant tumor; Essential
• ISSN: 0959-8049; 1879-0852
• DOI: 10.1016/j.ejca.2005.04.023

Insulin and insulin-like growth factors (IGFs) have critical functions in growth regulatory signalling pathways. They are part of a tightly controlled network of ligands, receptors, binding proteins and their proteases. However, the system becomes uncontrolled in neoplasia. The insulin-like growth factor binding protein 3 (IGFBP-3) and the insulin-like growth factor binding protein-related protein 1 (IGFBP-rP1) have unique properties among the sixteen known members of the IGFBP superfamily. IGFBP-3 has very high affinity for IGFs ( k d ∼ 10 −10 M), it transports > 75% of serum IGF-I and -II, whereas it’s affinity for insulin is very low. On the other hand, IGFBP-rP1 binds insulin with very high affinity (500-fold higher compared to other IGFBPs), but has low affinity for IGF-I and -II proteins ( k d = 3 × 10 −8 M). In this review, we have examined the roles of IGFBP-3 and IGFBP-rP1 in breast cancer, and discuss the potential impact of these two proteins in mammary carcinoma risk assessment and the development of treatments for breast cancer.