Insulin-Like Growth Factor-Binding Protein 5

IGFBP5 contains a thyroglobulin type-I domain and belongs to the IGFBP family. IGFBPs display strong sequence homologies. IGFBPs contain three distinct domains. N-terminal domain 1 and C-terminal domain 3 contain invariant cysteine residues and are thought to be the IGF binding domains. Domain 2 generally lacks sequence identity among the IGFBPs. Domain 3 is homologous to the thyroglobulin type I repeat. IGF-I and IGF-II circulate in plasma tightly bound to IGFBPs. IGFs, IGFRs, and IGFBPs regulate cell proliferation and apoptosis; the primary effect of IGFBPs appears to be modulation of IGF activity and control of IGF-mediated cell growth and metabolism. Secreted IGF-binding proteins prolong the half-life of IGFs (somatomedins) and either inhibit or stimulate the growth promoting effects of IGFs; they alter the interaction of IGFs with cell surface receptors. (from OMIM 146734, SWISS-PROT P22692, and NCI) (NCI Thesaurus)

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