Cytokines & Chemokines

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.

Interleukin-4 Receptor, also known as IL-4RA and CD124, is a transmembrane glycoprotein belonging to the class I receptor family. It is highly expressed by activated T-cells. IL-4RA couples with γ chain to form the type I receptor for IL-4. The extracellular domain of IL-4RA binds to IL-4 and antagonizes its activity. IL-4RA plays an important role in Th2 cell differentiation, Ig class switching and alternative macrophage activation. It has also been implicated in allergic inflammation, tumor progression and atherogenesis.

Interleukin-4 Receptor, also known as IL-4RA and CD124, is a transmembrane glycoprotein belonging to the class I receptor family. It is highly expressed by activated T-cells. IL-4RA couples with γ chain to form the type I receptor for IL-4. The extracellular domain of IL-4RA binds to IL-4 and antagonizes its activity. IL-4RA plays an important role in Th2 cell differentiation, Ig class switching and alternative macrophage activation. It has also been implicated in allergic inflammation, tumor progression and atherogenesis.

Interleukin-4 Receptor, also known as IL-4RA and CD124, is a transmembrane glycoprotein belonging to the class I receptor family. It is highly expressed by activated T-cells. IL-4RA couples with γ chain to form the type I receptor for IL-4. The extracellular domain of IL-4RA binds to IL-4 and antagonizes its activity. IL-4RA plays an important role in Th2 cell differentiation, Ig class switching and alternative macrophage activation. It has also been implicated in allergic inflammation, tumor progression and atherogenesis.

Protransforming Growth Factor-alpha (TGF-alpha), also known as sarcoma growth factor, TGF-type I and ETGF, is a member of the EGF family of cytokines. It is expressed in monocytes, brain cells, keratinocytes and various tumor cells. ProTGF-alpha signals through EGFR and acts synergistically with TGF-beta to promote the proliferation of a wide range of epidermal and epithelial cells. It may function as either a membrane-bound ligand or a soluble ligand. Membrane-bound proTGF-alpha plays a role in cell-cell adhesion and juxtacrine stimulation of adjacent cells. The soluble form of the cytokine is released from the membrane-bound form by proteolytic cleavage and acts as a mitogen for cell proliferation.

Protransforming Growth Factor-alpha (TGF-alpha), also known as sarcoma growth factor, TGF-type I and ETGF, is a member of the EGF family of cytokines. It is expressed in monocytes, brain cells, keratinocytes and various tumor cells. ProTGF-alpha signals through EGFR and acts synergistically with TGF-beta to promote the proliferation of a wide range of epidermal and epithelial cells. It may function as either a membrane-bound ligand or a soluble ligand. Membrane-bound proTGF-alpha plays a role in cell-cell adhesion and juxtacrine stimulation of adjacent cells. The soluble form of the cytokine is released from the membrane-bound form by proteolytic cleavage and acts as a mitogen for cell proliferation.

Keratinocyte Growth Factor (KGF) is a highly specific epithelial mitogen produced by fibroblasts and mesenchymal stem cells. KGF belongs to the heparin binding Fibroblast Growth Factor (FGF) family, and is known as FGF-7. However, in contrast to FGF-1, which binds to all known FGF receptors with high affinity, KGF only binds to a splice variant of the FGF receptor, FGFR2-IIIb. FGFR2-IIIb is expressedby most epithelial cells, indicating KGF’s roleas a paracrine mediator. KGF induces the differentiation and proliferation of various epithelial cells such as keratinocytes in the epidermis, hair follicles and sebaceous glands., KGF is also responsible for wound repair of various tissuesincluding lung, bladder, and kidney.

Keratinocyte Growth Factor (KGF) is a highly specific epithelial mitogen produced by fibroblasts and mesenchymal stem cells. KGF belongs to the heparin binding Fibroblast Growth Factor (FGF) family, and is known as FGF-7. However, in contrast to FGF-1, which binds to all known FGF receptors with high affinity, KGF only binds to a splice variant of the FGF receptor, FGFR2-IIIb. FGFR2-IIIb is expressedby most epithelial cells, indicating KGF’s roleas a paracrine mediator. KGF induces the differentiation and proliferation of various epithelial cells such as keratinocytes in the epidermis, hair follicles and sebaceous glands., KGF is also responsible for wound repair of various tissuesincluding lung, bladder, and kidney.

Keratinocyte Growth Factor (KGF) is a highly specific epithelial mitogen produced by fibroblasts and mesenchymal stem cells. KGF belongs to the heparin binding Fibroblast Growth Factor (FGF) family, and is known as FGF-7. However, in contrast to FGF-1, which binds to all known FGF receptors with high affinity, KGF only binds to a splice variant of the FGF receptor, FGFR2-IIIb. FGFR2-IIIb is expressedby most epithelial cells, indicating KGF’s roleas a paracrine mediator. KGF induces the differentiation and proliferation of various epithelial cells such as keratinocytes in the epidermis, hair follicles and sebaceous glands., KGF is also responsible for wound repair of various tissuesincluding lung, bladder, and kidney.