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.

A Proliferation-inducing Ligand (April)) also known as TNSF13A, Tall-2, and TRDL-1, is a member of the TNF ligand (TNFL) superfamily. April is most similar to B-cell activation factor (BAFF) with which it shares 30% sequence identity, compete for two receptors, TACI and BCMA. APRIL is expressed at low levels in lymphoid tissue and is over-expressed by a number of tumors. April has a proliferative effect on both normal and tumor cell lines in vitro and in vivo. APRIL seems to be involved in the regulation of death and proliferation of tumor cells, but there are still contradictory findings regarding its overall biological effects.

A Proliferation-inducing Ligand (April)) also known as TNSF13A, Tall-2, and TRDL-1, is a member of the TNF ligand (TNFL) superfamily. April is most similar to B-cell activation factor (BAFF) with which it shares 30% sequence identity, compete for two receptors, TACI and BCMA. APRIL is expressed at low levels in lymphoid tissue and is over-expressed by a number of tumors. April has a proliferative effect on both normal and tumor cell lines in vitro and in vivo. APRIL seems to be involved in the regulation of death and proliferation of tumor cells, but there are still contradictory findings regarding its overall biological effects.

A Proliferation-inducing Ligand (April)) also known as TNSF13A, Tall-2, and TRDL-1, is a member of the TNF ligand (TNFL) superfamily. April is most similar to B-cell activation factor (BAFF) with which it shares 30% sequence identity, compete for two receptors, TACI and BCMA. APRIL is expressed at low levels in lymphoid tissue and is over-expressed by a number of tumors. April has a proliferative effect on both normal and tumor cell lines in vitro and in vivo. APRIL seems to be involved in the regulation of death and proliferation of tumor cells, but there are still contradictory findings regarding its overall biological effects.

IP-10/CXCL10 also known as CXCL10, is originally identified as an IFN-γ-inducible gene in monocytes, fibroblasts and endothelial cells. It has since been shown that IP-10 mRNA is also induced by LPS, IL-1β, TNF-α, IL-12 and viruses. Additional cell types that have been shown to express IP-10 include activated T-lymphocytes, splenocytes, keratinocytes, osteoblasts, astrocytes, and smooth muscle cells. IP-10 is also expressed in psoriatic and lepromatous lesions of skin. The mouse homologue of human IP-10, Crg-2, has been cloned and shown to share approximately 67% amino acid sequence identity with human IP-10.

IP-10/CXCL10 also known as CXCL10, is originally identified as an IFN-γ-inducible gene in monocytes, fibroblasts and endothelial cells. It has since been shown that IP-10 mRNA is also induced by LPS, IL-1β, TNF-α, IL-12 and viruses. Additional cell types that have been shown to express IP-10 include activated T-lymphocytes, splenocytes, keratinocytes, osteoblasts, astrocytes, and smooth muscle cells. IP-10 is also expressed in psoriatic and lepromatous lesions of skin. The mouse homologue of human IP-10, Crg-2, has been cloned and shown to share approximately 67% amino acid sequence identity with human IP-10.

IP-10/CXCL10 also known as CXCL10, is originally identified as an IFN-γ-inducible gene in monocytes, fibroblasts and endothelial cells. It has since been shown that IP-10 mRNA is also induced by LPS, IL-1β, TNF-α, IL-12 and viruses. Additional cell types that have been shown to express IP-10 include activated T-lymphocytes, splenocytes, keratinocytes, osteoblasts, astrocytes, and smooth muscle cells. IP-10 is also expressed in psoriatic and lepromatous lesions of skin. The mouse homologue of human IP-10, Crg-2, has been cloned and shown to share approximately 67% amino acid sequence identity with human IP-10.

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