IGF I, also known as Mechano Growth Factor, somatomedin-C, IGF-I, and IGF1, is a secreted protein that belongs to the insulin family. The insulin family, comprised of insulin, relaxin, insulin-like growth factors I and II ( IGF-I and IGF-II ), and possibly the beta-subunit of 7S nerve growth factor, represents a group of structurally related polypeptides whose biological functions have diverged. The IGFs, or somatomedins, constitute a class of polypeptides that have a key role in pre-adolescent mammalian growth. IGF-I expression is regulated by GH and mediates postnatal growth, while IGF-II appears to be induced by placental lactogen during prenatal development. IGF1 / IGF-I may be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. IGF1 / IGF-I stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also about enhancing glucose uptake. Defects in IGF1 / IGF-I are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) which is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness, and mental retardation.
IGF I, also known as mechano growth factor, somatomedin-C, IGF-I and IGF1, is a secreted protein which belongs to the insulin family. The insulin family, comprised of insulin, relaxin, insulin-like growth factors I and II ( IGF-I and IGF-II ) and possibly the beta-subunit of 7S nerve growth factor, represents a group of structurally related polypeptides whose biological functions have diverged. The IGFs, or somatomedins, constitute a class of polypeptides that have a key role in pre-adolescent mammalian growth. IGF-I expression is regulated by GH and mediates postnatal growth, while IGF-II appears to be induced by placental lactogen during prenatal development. IGF1 / IGF-I may be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. IGF1 / IGF-I stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. Defects in IGF1 / IGF-I are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) which is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation.
nsulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mouse IGF-I is synthesized as two precursor isoforms with alternate N-and C-terminal propeptides. These isoforms are differentially expressed by various tissues. Mature mouse IGF-I shares 94% and 99% aa sequence identity with human and rat IGF-I, respectively, and exhibits cross-species activity. It shares 60% aa sequence identity with mature mouse IGF-II. IGF-I induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally. It plays an important role in muscle regeneration and tumor progression. IGF-I binds IGF-I R, IGF-II R, and the insulin receptor. IGF-I association with IGF binding proteins increases its plasma half-life and modulates its interactions with receptors.
Insulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mouse IGF-I is synthesized as two precursor isoforms with alternate N- and C-terminal propeptides. These isoforms are differentially expressed by various tissues. Mature mouse IGF-I shares 94% and 99% aa sequence identity with human and rat IGF-I, respectively, and exhibits cross-species activity. It shares 60% aa sequence identity with mature mouse IGF-II. IGF-I induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally. It plays an important role in muscle regeneration and tumor progression. IGF-I binds IGF-I R, IGF-II R, and the insulin receptor. IGF-I association with IGF binding proteins increases its plasma half-life and modulates its interactions with receptors.
Insulin-like growth factor I (also known as somatomedin C and somatomedin A) and insulin-like growth factor II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved (100% identity between human, bovine and porcine proteins) and exhibit cross-species activity. IGF-II is a potent mitogenic growth factor. However, unlike IGF-I which has important postnatal roles, the growth-promoting function of IGF-II is limited to embryonic development.
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