Cytokines & Chemokines

Leptin is a cytokine belonging to the Interleukin 6 family, and has a four-helix bundle structure. Leptin is encoded by the ob gene, and produced and secreted by white adipose tissue. The receptors of Leptin are Type I cytokine receptors, which exist in two different forms: a short form expressed in multiple tissues, and a long form expressed exclusively in the central nervous system (CNS). Upon binding to Leptin, the receptors activate the JAK/STAT3 pathway and PI3K, and stimulate transcriptional programs that regulate feeding behavior, metabolic rate, endocrine axes, and glucose fluxes. The deficiency of Leptin in human and mouse causes morbid obesity, diabetes, and neuroendocrine anomalies. Leptin also has effects on reproduction and immunity. In summary, Leptin is a pivotal cytokine controlling energy balance, and as such has profound effects on human health.

Leptin is a cytokine belonging to the Interleukin 6 family, and has a four-helix bundle structure. Leptin is encoded by the ob gene, and produced and secreted by white adipose tissue. The receptors of Leptin are Type I cytokine receptors, which exist in two different forms: a short form expressed in multiple tissues, and a long form expressed exclusively in the central nervous system (CNS). Upon binding to Leptin, the receptors activate the JAK/STAT3 pathway and PI3K, and stimulate transcriptional programs that regulate feeding behavior, metabolic rate, endocrine axes, and glucose fluxes. The deficiency of Leptin in human and mouse causes morbid obesity, diabetes, and neuroendocrine anomalies. Leptin also has effects on reproduction and immunity. In summary, Leptin is a pivotal cytokine controlling energy balance, and as such has profound effects on human health.

Leptin is a cytokine belonging to the Interleukin 6 family, and has a four-helix bundle structure. Leptin is encoded by the ob gene, and produced and secreted by white adipose tissue. The receptors of Leptin are Type I cytokine receptors, which exist in two different forms: a short form expressed in multiple tissues, and a long form expressed exclusively in the central nervous system (CNS). Upon binding to Leptin, the receptors activate the JAK/STAT3 pathway and PI3K, and stimulate transcriptional programs that regulate feeding behavior, metabolic rate, endocrine axes, and glucose fluxes. The deficiency of Leptin in human and mouse causes morbid obesity, diabetes, and neuroendocrine anomalies. Leptin also has effects on reproduction and immunity. In summary, Leptin is a pivotal cytokine controlling energy balance, and as such has profound effects on human health.

Macrophage Migration Inhibitory Factor (MIF) is a pleiotropic cytokine, existing as a homotrimer in vivo. MIF was originally identified as a T cell derived factor responsible for the inhibition of macrophage migration. However, recently MIF has received much more attention because of its possible roles in angiogenesis and cancer development. MIF is over-expressed in various cancers, including pancreatic, breast, colon, brain, prostate, skin, and lung. The intratumoral expression of MIF is strongly correlated with angiogenic growth factor expression, such as the expression of Interleukin 8 (IL-8) and Vascular Endothelial Growth Factor (VEGF), and with risk of recurrence after resection.

Macrophage Migration Inhibitory Factor (MIF) is a pleiotropic cytokine, existing as a homotrimer in vivo. MIF was originally identified as a T cell derived factor responsible for the inhibition of macrophage migration. However, recently MIF has received much more attention because of its possible roles in angiogenesis and cancer development. MIF is over-expressed in various cancers, including pancreatic, breast, colon, brain, prostate, skin, and lung. The intratumoral expression of MIF is strongly correlated with angiogenic growth factor expression, such as the expression of Interleukin 8 (IL-8) and Vascular Endothelial Growth Factor (VEGF), and with risk of recurrence after resection.

Macrophage Migration Inhibitory Factor (MIF) is a pleiotropic cytokine, existing as a homotrimer in vivo. MIF was originally identified as a T cell derived factor responsible for the inhibition of macrophage migration. However, recently MIF has received much more attention because of its possible roles in angiogenesis and cancer development. MIF is over-expressed in various cancers, including pancreatic, breast, colon, brain, prostate, skin, and lung. The intratumoral expression of MIF is strongly correlated with angiogenic growth factor expression, such as the expression of Interleukin 8 (IL-8) and Vascular Endothelial Growth Factor (VEGF), and with risk of recurrence after resection.

Interleukin-10 (IL-10), initially known as Cytokine Synthesis Inhibitory Factor (CSIF), belongs to the IL-10 family and shares more than 80% sequence homology with the Epstein-Barr Virus protein BCRFI. It is produced by many immune cells, such as T-cells, macrophages, mast cells and dendritic cells. It is usually secreted as a homodimer and, upon binding to its receptor, inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF, by activated macrophages and Th2 cells. It also displays the ability to suppress Antigen-Presenting Cell (APC) function. The net effect of Interleukin-10 appears to be inhibitory; however, stimulatory effects, such as stimulation of B cell maturation and antibody production, are also reported.

Interleukin-10 (IL-10), initially known as Cytokine Synthesis Inhibitory Factor (CSIF), belongs to the IL-10 family and shares more than 80% sequence homology with the Epstein-Barr Virus protein BCRFI. It is produced by many immune cells, such as T-cells, macrophages, mast cells and dendritic cells. It is usually secreted as a homodimer and, upon binding to its receptor, inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF, by activated macrophages and Th2 cells. It also displays the ability to suppress Antigen-Presenting Cell (APC) function. The net effect of Interleukin-10 appears to be inhibitory; however, stimulatory effects, such as stimulation of B cell maturation and antibody production, are also reported.

Interleukin-10 (IL-10), initially known as Cytokine Synthesis Inhibitory Factor (CSIF), belongs to the IL-10 family and shares more than 80% sequence homology with the Epstein-Barr Virus protein BCRFI. It is produced by many immune cells, such as T-cells, macrophages, mast cells and dendritic cells. It is usually secreted as a homodimer and, upon binding to its receptor, inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF, by activated macrophages and Th2 cells. It also displays the ability to suppress Antigen-Presenting Cell (APC) function. The net effect of Interleukin-10 appears to be inhibitory; however, stimulatory effects, such as stimulation of B cell maturation and antibody production, are also reported.