Cytokines & Chemokines

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, which also includes IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and shares a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

Insulin-like Growth Factor I (IGF-I) is a single chain 7 kDa growth-promoting polypeptide originally identified as somatomedin-c. It belongs to the IGF family of peptides, which also includes IGF-II and insulin. The gene expression of IGF-I is mainly regulated by Growth Hormone, and IGF-I executes its functions via signaling through transmembrane tyrosine receptors (IGF Receptors). Most circulating IFG-I is associated with the IGF Binding Protein 3 (IGFBP-3), and the IGFBPs may inhibit the actions of IGFs by competing against the IGF Receptors. IGF-I is active in post-natal and adult animals, and is crucial for somatic growth, as IGF-I null mice show marked retardation in utero. IGF-I is involved in the carcinogenesis, and related to the prostate cancer as well.

Insulin-like Growth Factor I (IGF-I) is a single chain 7 kDa growth-promoting polypeptide originally identified as somatomedin-c. It belongs to the IGF family of peptides, which also includes IGF-II and insulin. The gene expression of IGF-I is mainly regulated by Growth Hormone, and IGF-I executes its functions via signaling through transmembrane tyrosine receptors (IGF Receptors). Most circulating IFG-I is associated with the IGF Binding Protein 3 (IGFBP-3), and the IGFBPs may inhibit the actions of IGFs by competing against the IGF Receptors. IGF-I is active in post-natal and adult animals, and is crucial for somatic growth, as IGF-I null mice show marked retardation in utero. IGF-I is involved in the carcinogenesis, and related to the prostate cancer as well.

Insulin-like Growth Factor I (IGF-I) is a single chain 7 kDa growth-promoting polypeptide originally identified as somatomedin-c. It belongs to the IGF family of peptides, which also includes IGF-II and insulin. The gene expression of IGF-I is mainly regulated by Growth Hormone, and IGF-I executes its functions via signaling through transmembrane tyrosine receptors (IGF Receptors). Most circulating IFG-I is associated with the IGF Binding Protein 3 (IGFBP-3), and the IGFBPs may inhibit the actions of IGFs by competing against the IGF Receptors. IGF-I is active in post-natal and adult animals, and is crucial for somatic growth, as IGF-I null mice show marked retardation in utero. IGF-I is involved in the carcinogenesis, and related to the prostate cancer as well.

Insulin-like Growth Factor II (IGF-II) is a single chain 7 kDa polypeptide, and shares a high degree of homology with insulin. During circulation in vivo, IGF-II is complexed to high affinity binding proteins, IGF Binding Proteins (IGFBP), which act as circulating reservoirs, transport IGF-II, and prolong the half life of IGF-II. The receptors of IGF-II (IGFRs) are transmembrane tyrosine receptors, and are heterotetrameric consisting of two α-subunits and two β-subunits. IGFRs execute their role via intracellullar signaling molecules, such as IRS, shc, and PI3K. The functions of IGF-II include promoting cell survival, growth, proliferation, differentiation and motility. In particular, IGF-II promotes proliferation, inhibits death, and stimulates transformation in breast cancer cells.

Insulin-like Growth Factor II (IGF-II) is a single chain 7 kDa polypeptide, and shares a high degree of homology with insulin. During circulation in vivo, IGF-II is complexed to high affinity binding proteins, IGF Binding Proteins (IGFBP), which act as circulating reservoirs, transport IGF-II, and prolong the half life of IGF-II. The receptors of IGF-II (IGFRs) are transmembrane tyrosine receptors, and are heterotetrameric consisting of two α-subunits and two β-subunits. IGFRs execute their role via intracellullar signaling molecules, such as IRS, shc, and PI3K. The functions of IGF-II include promoting cell survival, growth, proliferation, differentiation and motility. In particular, IGF-II promotes proliferation, inhibits death, and stimulates transformation in breast cancer cells.

Insulin-like Growth Factor II (IGF-II) is a single chain 7 kDa polypeptide, and shares a high degree of homology with insulin. During circulation in vivo, IGF-II is complexed to high affinity binding proteins, IGF Binding Proteins (IGFBP), which act as circulating reservoirs, transport IGF-II, and prolong the half life of IGF-II. The receptors of IGF-II (IGFRs) are transmembrane tyrosine receptors, and are heterotetrameric consisting of two α-subunits and two β-subunits. IGFRs execute their role via intracellullar signaling molecules, such as IRS, shc, and PI3K. The functions of IGF-II include promoting cell survival, growth, proliferation, differentiation and motility. In particular, IGF-II promotes proliferation, inhibits death, and stimulates transformation in breast cancer cells.

Adiponectin is a hormone mainly produced by adipocytes. Adiponectin forms a homotrimer and exists as higher order multimers in vivo. The receptors of Adiponectin are seven transmembrane G protein coupled receptors: Receptor 1 is expressed in skeletal muscle and Receptor 2 in liver. Adiponectin receives a lot of attention because of its anti-diabetic, anti-atherosclerotic, and anti-inflammatory properties. Adiponectin increases the expression of molecules involved in fatty acid transport, combustion of fatty acid, and energy dissipation, and increases insulin sensitivity of the body. Decreased levels of Adiponectin are associated with hypertension, cardiovascular diseases, and metabolic syndromes. Therefore, Adiponectin has promising potential as a pharmacological agent.

Adiponectin is a hormone mainly produced by adipocytes. Adiponectin forms a homotrimer and exists as higher order multimers in vivo. The receptors of Adiponectin are seven transmembrane G protein coupled receptors: Receptor 1 is expressed in skeletal muscle and Receptor 2 in liver. Adiponectin receives a lot of attention because of its anti-diabetic, anti-atherosclerotic, and anti-inflammatory properties. Adiponectin increases the expression of molecules involved in fatty acid transport, combustion of fatty acid, and energy dissipation, and increases insulin sensitivity of the body. Decreased levels of Adiponectin are associated with hypertension, cardiovascular diseases, and metabolic syndromes. Therefore, Adiponectin has promising potential as a pharmacological agent.