Cytokines & Chemokines

The Indian Hedgehog protein (IHH) is one of three proteins in the mammalian hedgehog family, the others being desert hedgehog (DHH) and Sonic hedgehog (SHH). Hedgehog proteins are important signaling molecules during embryonic development and are highly conserved across species. Mouse and human IHH share 100% amino acid identity in the signaling domain, while mouse IHH and SHH share 90% amino acid identity in the N-terminal signaling domain. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.

Chemokine (C-C motif) ligand 2 (CCL2) is also referred to as monocyte chemotactic protein 1 (MCP1) and small inducible cytokine A2. CCL2 is a small cytokine that belongs to the CC chemokine family. CCL2 recruits monocytes, memory T cells, and dendritic cells to the sites of inflammation produced by either tissue injury or infection. CCL2 is implicated in the pathogeneses of several types of disease characterized by monocytic infiltrates, such as psoriasis, rheumatoid arthritis and atherosclerosis. CCL2 is anchored in the plasma membrane of endothelial cells by glycosaminoglycan side chains of proteoglycans. CCL2 is primarily secreted by monocytes, macrophages and dendritic cells. CCL2 can signal through the CCR2 receptor.

Chemokine (C-C motif) ligand 2 (CCL2) is also referred to as monocyte chemotactic protein 1 (MCP1) and small inducible cytokine A2. CCL2 is a small cytokine that belongs to the CC chemokine family. CCL2 recruits monocytes, memory T cells, and dendritic cells to the sites of inflammation produced by either tissue injury or infection. CCL2 is implicated in the pathogeneses of several types of disease characterized by monocytic infiltrates, such as psoriasis, rheumatoid arthritis and atherosclerosis. CCL2 is anchored in the plasma membrane of endothelial cells by glycosaminoglycan side chains of proteoglycans. CCL2 is primarily secreted by monocytes, macrophages and dendritic cells. CCL2 can signal through the CCR2 receptor.

Chemokine (C-C motif) ligand 2 (CCL2) is also referred to as monocyte chemotactic protein 1 (MCP1) and small inducible cytokine A2. CCL2 is a small cytokine that belongs to the CC chemokine family. CCL2 recruits monocytes, memory T cells, and dendritic cells to the sites of inflammation produced by either tissue injury or infection. CCL2 is implicated in the pathogeneses of several types of disease characterized by monocytic infiltrates, such as psoriasis, rheumatoid arthritis and atherosclerosis. CCL2 is anchored in the plasma membrane of endothelial cells by glycosaminoglycan side chains of proteoglycans. CCL2 is primarily secreted by monocytes, macrophages and dendritic cells. CCL2 can signal through the CCR2 receptor.

Vascular endothelial growth factor C (VEGF-C) is a member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family, is active in angiogenesis, lymphangiogenesis and endothelial cell growth and survival, and can also affect the permeability of blood vessels. VEGF-C is expressed in various tissues, however it is not produced in peripheral blood lymphocytes. It forms cell surface-associated non-covalent disulfide linked homodimers, and can bind and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4) receptors. The structure and function of VEGF-C is similar to those of vascular endothelial growth factor D (VEGF-D).

Vascular endothelial growth factor C (VEGF-C) is a member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family, is active in angiogenesis, lymphangiogenesis and endothelial cell growth and survival, and can also affect the permeability of blood vessels. VEGF-C is expressed in various tissues, however it is not produced in peripheral blood lymphocytes. It forms cell surface-associated non-covalent disulfide linked homodimers, and can bind and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4) receptors. The structure and function of VEGF-C is similar to those of vascular endothelial growth factor D (VEGF-D).

Vascular endothelial growth factor C (VEGF-C) is a member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family, is active in angiogenesis, lymphangiogenesis and endothelial cell growth and survival, and can also affect the permeability of blood vessels. VEGF-C is expressed in various tissues, however it is not produced in peripheral blood lymphocytes. It forms cell surface-associated non-covalent disulfide linked homodimers, and can bind and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4) receptors. The structure and function of VEGF-C is similar to those of vascular endothelial growth factor D (VEGF-D).

Fibroblast Growth Factor-16 (FGF-16) is a heparin binding growth factor, a member of the FGF family. All FGF family members are heparin­binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The rat homolog is predominantly expressed in embryonic brown adipose tissue and has significant mitogenic activity, which suggests a role in proliferation of embryonic brown adipose tissue. FGF-16 is most similar to FGF-9 (73 % amino acid identity). The protein sequence of human FGF-16 displays 98.6% identity with rat FGF-16. Chimpanzee FGF-16 (207 amino acids), chicken FGF-16 (207 amino acids), and zebrafish FGF-16 (203 amino acids) show 100 %, 89.9 %, and 79.2 % total amino acid identity with human FGF-16.

Fibroblast Growth Factor-16 (FGF-16) is a heparin binding growth factor, a member of the FGF family. All FGF family members are heparin­binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The rat homolog is predominantly expressed in embryonic brown adipose tissue and has significant mitogenic activity, which suggests a role in proliferation of embryonic brown adipose tissue. FGF-16 is most similar to FGF-9 (73 % amino acid identity). The protein sequence of human FGF-16 displays 98.6% identity with rat FGF-16. Chimpanzee FGF-16 (207 amino acids), chicken FGF-16 (207 amino acids), and zebrafish FGF-16 (203 amino acids) show 100 %, 89.9 %, and 79.2 % total amino acid identity with human FGF-16.