Cytokines & Chemokines

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, bFGF has the β trefoil structure. In vivo, bFGF is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. bFGF regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. bFGF can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of bFGF can produce beneficial cardioprotection during acute heart injury.

Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulat

Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulat

Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulat

Adiponectin is an important adipokine involved in the control of fat metabolism and insulin sensitivity. It is synthesized exclusively by adipocytes and secreted into plasma. It antagonizes THF-alpha by negatively regulating its expression. It also inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. Adiponectin can form low molecular weight complexes (LMW), middle molecular weight complexes (MMW) and higher molecular weight complexes (HMW). These bind to various growth factors, such as HBEGF, PDGFB and FGF2, and play a role in cell growth, angiogenesis and tissue remodeling.

Adiponectin is an important adipokine involved in the control of fat metabolism and insulin sensitivity. It is synthesized exclusively by adipocytes and secreted into plasma. It antagonizes THF-alpha by negatively regulating its expression. It also inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. Adiponectin can form low molecular weight complexes (LMW), middle molecular weight complexes (MMW) and higher molecular weight complexes (HMW). These bind to various growth factors, such as HBEGF, PDGFB and FGF2, and play a role in cell growth, angiogenesis and tissue remodeling.

Adiponectin is an important adipokine involved in the control of fat metabolism and insulin sensitivity. It is synthesized exclusively by adipocytes and secreted into plasma. It antagonizes THF-alpha by negatively regulating its expression. It also inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. Adiponectin can form low molecular weight complexes (LMW), middle molecular weight complexes (MMW) and higher molecular weight complexes (HMW). These bind to various growth factors, such as HBEGF, PDGFB and FGF2, and play a role in cell growth, angiogenesis and tissue remodeling.

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 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 produced by activated macrophages and Th2 cells. It also displays 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 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 produced by activated macrophages and Th2 cells. It also displays 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.