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Alternative Name
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Igf1 (IGF1 ELISA Kit Abstract)
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Background
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Insulin-like Growth Factor I (IGF-I), also known as somatomedin C, is a member of the insulin superfamily. It was originally discovered as a mediator of growth hormone actions on somatic cell growth, but has also been shown to be an important regulator of cell metabolism, differentiation and survival. IGF-I is synthesized as a preproprotein that is proteolytically cleaved to generate the mature protein linked by three disulfide bonds. Mature IGF-I is highly conserved among mammals, with 100% sequence identity between the Porcine, bovine, porcine, equine and canine proteins. IGF-I is synthesized in the liver and multiple other tissues. It is found in blood and other body fluids as a complex with specific high affinity IGF binding proteins (IGFBP-1to-6). The IGFBPs are expressed in specific patterns during development. They are modulators of IGF actions, which control IGF bioavailability to specific cell-surface receptors. Their functions are further regulated by IGFBP proteases, which proteolytically cleave the IGFBPs to lower the affinity with which they bind IGFs and increase IGF bioavailability. Some IGFBPs also have IGF-independent effects on cell functions. IGF-I circulates primarily as a ternary complex with IGFBP-3 or IGFBP-5 and the acid-labile subunit (ALS). Some IGF-I is also present in binary complexes with other IGFBPs. Whereas the ternary complexes are generally restricted to the vasculature, the binary complexes freely enter the tissues. IGF-I actions are mediated by two type I transmembrane receptor tyrosine kinases: the IGF-I receptor (IGF-I R), and the insulin receptor (INS R) that exists in two alternatively spliced isoforms (INS R-A and -B). Both IGF-I R and INS R share a highly homologous structure and are ubiquitously expressed. Functional IGF-I receptors are tetrameric glycoproteins composed of two disulfide-linked IGF-I Rs or disulfide-linked hybrids of one IGF-I R and one INS R. Whereas IGF-I binds with high-affinity to homodimeric IGF-I R and heterdimeric IGF-I R:INS R-A or – B hybrids, high-affinity binding of insulin is observed only with dimeric INS R or IGF-I R:INS R-A hybrid but not with IGF-I R:INS R-B hybrid. The signaling responses from the various receptors are different depending whether insulin or IGF-I is used as the activating ligand. 2
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Pathways
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RTK Signaling, Intracellular Steroid Hormone Receptor Signaling Pathway, Peptide Hormone Metabolism, Hormone Activity, Regulation of Intracellular Steroid Hormone Receptor Signaling, Regulation of Hormone Metabolic Process, Regulation of Hormone Biosynthetic Process, Stem Cell Maintenance, Glycosaminoglycan Metabolic Process, Regulation of Carbohydrate Metabolic Process, Autophagy, Smooth Muscle Cell Migration, Activated T Cell Proliferation, Positive Regulation of fat Cell Differentiation
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