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, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

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, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

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, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

PDGF-DD, also known as platelet-derived growth factor D, IEGF and SCDGFB, is asecreted growth factor belonging to the PDGF/VEGFfamily. It is highly expressed in the heart, pancreas, adrenal glands and ovary. PDGF-DD forms functional homodimers that bind and induce PDGF Rβ homodimers and PDGF Rα/β heterodimers that promote intracellular signaling. This plays an important role in the regulation of cell differentiation, migration and survival. It has also been reported that PDGF-DD can induce monocyte and macrophage recruitment, increase interstitial pressure and facilitate wound healing.

PDGF-DD, also known as platelet-derived growth factor D, IEGF and SCDGFB, is asecreted growth factor belonging to the PDGF/VEGFfamily. It is highly expressed in the heart, pancreas, adrenal glands and ovary. PDGF-DD forms functional homodimers that bind and induce PDGF Rβ homodimers and PDGF Rα/β heterodimers that promote intracellular signaling. This plays an important role in the regulation of cell differentiation, migration and survival. It has also been reported that PDGF-DD can induce monocyte and macrophage recruitment, increase interstitial pressure and facilitate wound healing.

Interleukin-33 (IL-33) is a proinflammatory cytokine that belongs to the IL-1 family. IL-33 is expressed in a variety of cells, including epithelial and endothelial cells, smooth muscle cells, macrophages and fibroblasts. The primary receptors for IL-33 are ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which belong to the IL-1 receptor family. IL-33 is localized to the nucleus of resting cells where it binds to chromatin in the H2A-H2B histone complex as a transcriptional suppressor. IL-33 is secreted by cells during injury which induces a T-helper 2 type inflammatory response. Evidence suggests IL-33 plays a role in autoimmune disease. IL-33’s interaction with ST2 can drive allergic pathology and IL-33 has been reported to play a role in the development of rheumatoid arthritis and systemic lupus erythematosus.

Interleukin-33 (IL-33) is a proinflammatory cytokine that belongs to the IL-1 family. IL-33 is expressed in a variety of cells, including epithelial and endothelial cells, smooth muscle cells, macrophages and fibroblasts. The primary receptors for IL-33 are ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which belong to the IL-1 receptor family. IL-33 is localized to the nucleus of resting cells where it binds to chromatin in the H2A-H2B histone complex as a transcriptional suppressor. IL-33 is secreted by cells during injury which induces a T-helper 2 type inflammatory response. Evidence suggests IL-33 plays a role in autoimmune disease. IL-33’s interaction with ST2 can drive allergic pathology and IL-33 has been reported to play a role in the development of rheumatoid arthritis and systemic lupus erythematosus.

Interleukin-33 (IL-33) is a proinflammatory cytokine that belongs to the IL-1 family. IL-33 is expressed in a variety of cells, including epithelial and endothelial cells, smooth muscle cells, macrophages and fibroblasts. The primary receptors for IL-33 are ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which belong to the IL-1 receptor family. IL-33 is localized to the nucleus of resting cells where it binds to chromatin in the H2A-H2B histone complex as a transcriptional suppressor. IL-33 is secreted by cells during injury which induces a T-helper 2 type inflammatory response. Evidence suggests IL-33 plays a role in autoimmune disease. IL-33’s interaction with ST2 can drive allergic pathology and IL-33 has been reported to play a role in the development of rheumatoid arthritis and systemic lupus erythematosus.

IGF-BP-2, also known as Insulin-like growth factor-binding protein 2, IBP-2 and BP-2, is a cysteine-rich secreted protein belonging to the IGF-binding protein superfamily. It is expressed by the central nervous system, bone cells and reproductive tissues. IGF-BP-2 binds to both IGF-I and IGF-II, with a much higher binding affinity to IGF-II than IGF-I. IGF-BP-2 has been shown to inhibitand stimulate the growth promoting effects of IGFs, thus serving as a regulator for IGF distribution, function and activity.