Cytokines & Chemokines

Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, GRO-α, KC, neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-α). Human GRO-α, GRO-β (MIP2α),and GRO-γ (MIP2β)are products of three distinct, nonallelichuman genes. GRO-β and GRO-γ share 90% and 86% amino acid sequence homology with GROα, respectively. All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. GRO expression is inducible by serum or PDGF and/or by a variety of inflammatory mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In certain tumor cell lines, GRO is expressed constitutively. Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. Additionally, these chemokines are also active toward basophils.All three GROs can bind with high affinity to the IL-8

Human GRO-α, GRO-β (MIP-2α), and GRO-γ (MIP-2β) are products of three distinct, nonallelichuman genes. GRO-β and GRO-γ share 90% and 86% amino acid sequence homology, respectively, with GROα. All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors.GRO expression is inducible by serum or PDGF and/or by a variety of inflammatory mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In certain tumor cell lines, GRO is expressed constitutively.Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. In addition, these chemokines are also active toward basophils.

Human GRO-α, GRO-β (MIP-2α), and GRO-γ (MIP-2β) are products of three distinct, nonallelichuman genes. GRO-β and GRO-γ share 90% and 86% amino acid sequence homology, respectively, with GROα. All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors.GRO expression is inducible by serum or PDGF and/or by a variety of inflammatory mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In certain tumor cell lines, GRO is expressed constitutively.Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. In addition, these chemokines are also active toward basophils.

Human GRO-α, GRO-β (MIP-2α), and GRO-γ (MIP-2β) are products of three distinct, nonallelichuman genes. GRO-β and GRO-γ share 90% and 86% amino acid sequence homology, respectively, with GROα. All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors.GRO expression is inducible by serum or PDGF and/or by a variety of inflammatory mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In certain tumor cell lines, GRO is expressed constitutively.Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. In addition, these chemokines are also active toward basophils.

Chemokine (C-X3-C motif) ligand 1 (CX3CL1) is a known member of the CX3C chemokine family. It is also commonly known under the names fractalkine (in humans) and neurotactin (in mice). The polypeptide structure of CXC3L1 differs from the typical structure of other chemokines. For example, the spacing of the characteristic N-terminal cysteines is different; there are three amino acids separating the initial pair of cysteines in CX3CL1, while there are none in CC chemokines and only one in CXC chemokines. CX3CL1 is produced as a long protein (with 373-amino acid in humans) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk allows it to bind to the surface of certain cells. Soluble CX3CL1 potently chemoattracts T cells and monocytes, while the cell-bound chemokine promotes strong adhesion of leukocytes to activated endothelial cells, where it is primarily expressed. CX3CL1 can signal through the chemokine receptor CX3CR1.

Chemokine (C-X3-C motif) ligand 1 (CX3CL1) is a known member of the CX3C chemokine family. It is also commonly known under the names fractalkine (in humans) and neurotactin (in mice). The polypeptide structure of CXC3L1 differs from the typical structure of other chemokines. For example, the spacing of the characteristic N-terminal cysteines is different; there are three amino acids separating the initial pair of cysteines in CX3CL1, while there are none in CC chemokines and only one in CXC chemokines. CX3CL1 is produced as a long protein (with 373-amino acid in humans) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk allows it to bind to the surface of certain cells. Soluble CX3CL1 potently chemoattracts T cells and monocytes, while the cell-bound chemokine promotes strong adhesion of leukocytes to activated endothelial cells, where it is primarily expressed. CX3CL1 can signal through the chemokine receptor CX3CR1.

Chemokine (C-X3-C motif) ligand 1 (CX3CL1) is a known member of the CX3C chemokine family. It is also commonly known under the names fractalkine (in humans) and neurotactin (in mice). The polypeptide structure of CXC3L1 differs from the typical structure of other chemokines. For example, the spacing of the characteristic N-terminal cysteines is different; there are three amino acids separating the initial pair of cysteines in CX3CL1, while there are none in CC chemokines and only one in CXC chemokines. CX3CL1 is produced as a long protein (with 373-amino acid in humans) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk allows it to bind to the surface of certain cells. Soluble CX3CL1 potently chemoattracts T cells and monocytes, while the cell-bound chemokine promotes strong adhesion of leukocytes to activated endothelial cells, where it is primarily expressed. CX3CL1 can signal through the chemokine receptor CX3CR1.

Stromal-Cell Derived Factor-1 alpha/ CXCL12 (SDF-1α) and SDF-1β, members of the chemokine α subfamily that lack the ELR domain, were initially identified using the signal sequence trap cloning strategy from a mouse bone-marrow stromal cell line. These proteins were subsequently also cloned from a human stromal cell line as cytokines that supported the proliferation of a stromal cell-dependent pre-B-cell line. SDF-1α and SDF-1β cDNAs encode precursor proteins of 89 and 93 amino acid residues, respectively. Both SDF-1α and SDF-1β are encoded by a single gene and arise by alternative splicing. The two proteins are identical except for the four amino acid residues that are present in the carboxy-terminus of SDF-1β and absent from SDF-1α. SDF-1/PBSF is highly conserved between species, with only one amino acid substitution between the mature human and mouse proteins. SDF-1/PBSF acts via the chemokine receptor CXCR4 and has been shown to be a chemoattractant for T-lymphocytes, monocytes, pro

Stromal-Cell Derived Factor-1 alpha/ CXCL12 (SDF-1α) and SDF-1β, members of the chemokine α subfamily that lack the ELR domain, were initially identified using the signal sequence trap cloning strategy from a mouse bone-marrow stromal cell line. These proteins were subsequently also cloned from a human stromal cell line as cytokines that supported the proliferation of a stromal cell-dependent pre-B-cell line. SDF-1α and SDF-1β cDNAs encode precursor proteins of 89 and 93 amino acid residues, respectively. Both SDF-1α and SDF-1β are encoded by a single gene and arise by alternative splicing. The two proteins are identical except for the four amino acid residues that are present in the carboxy-terminus of SDF-1β and absent from SDF-1α. SDF-1/PBSF is highly conserved between species, with only one amino acid substitution between the mature human and mouse proteins. SDF-1/PBSF acts via the chemokine receptor CXCR4 and has been shown to be a chemoattractant for T-lymphocytes, monocytes, pro