Cytokines & Chemokines

Interleukin-2 (IL-2) is a Oglycosylated, four α-helix bundle cytokine that has potent stimulatory activity for antigen-activated T cells. It is expressed by CD4+ and CD8+ T cells, γδ T cells, B cells, dendritic cells, and eosinophils. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions which are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine activated killer cells, monocytes, macrophages and oligodendrocytes.

Interleukin-21 (IL-21) belongs to the Type I four helix bundle cytokines, and shares the common cytokine receptor γ chain with IL-2, IL-4, IL-7, IL-9, and IL-15. IL-21 is expressed by CD4+ T cells, natural killer (NK) T cells, and Th17 cells, and the IL-21 receptor is highly expressed on CD4+ and CD8+ B cells; indeed, IL-21 plays a pivotal role in the survival and proliferation of B cells, and their differentiation to immunoglobulin (Ig) producing cells. IL-21 up-regulates and down-regulates the production of IgG1 and IgE by B cells, respectively, and diminishes the severity of allergy and asthma. In some case, IL-21 also induces the apoptosis of B cells. The other roles of IL-21 include regulation of innate immune systems, implication on autoimmunity, and antitumor actions.

Interleukin-21 (IL-21) belongs to the Type I four helix bundle cytokines, and shares the common cytokine receptor γ chain with IL-2, IL-4, IL-7, IL-9, and IL-15. IL-21 is expressed by CD4+ T cells, natural killer (NK) T cells, and Th17 cells, and the IL-21 receptor is highly expressed on CD4+ and CD8+ B cells; indeed, IL-21 plays a pivotal role in the survival and proliferation of B cells, and their differentiation to immunoglobulin (Ig) producing cells. IL-21 up-regulates and down-regulates the production of IgG1 and IgE by B cells, respectively, and diminishes the severity of allergy and asthma. In some case, IL-21 also induces the apoptosis of B cells. The other roles of IL-21 include regulation of innate immune systems, implication on autoimmunity, and antitumor actions.

Interleukin-21 (IL-21) belongs to the Type I four helix bundle cytokines, and shares the common cytokine receptor γ chain with IL-2, IL-4, IL-7, IL-9, and IL-15. IL-21 is expressed by CD4+ T cells, natural killer (NK) T cells, and Th17 cells, and the IL-21 receptor is highly expressed on CD4+ and CD8+ B cells; indeed, IL-21 plays a pivotal role in the survival and proliferation of B cells, and their differentiation to immunoglobulin (Ig) producing cells. IL-21 up-regulates and down-regulates the production of IgG1 and IgE by B cells, respectively, and diminishes the severity of allergy and asthma. In some case, IL-21 also induces the apoptosis of B cells. The other roles of IL-21 include regulation of innate immune systems, implication on autoimmunity, and antitumor actions.

Leukemia Inhibitory Factor (LIF) is a pleiotropic cytokine belonging to the long four-helix bundle cytokine superfamily. LIF shares tertiary structure with several other cytokines, including Interleukin-6 (IL-6), Oncostatin M, ciliary neurotropic factor, and cardiotrophin-1, and their functions in vivo are also redundant to some extent. LIF can bind to the common receptor of IL-6 subfamily, gp130, and then recruit its own receptor LIF Receptor to form a ternary complex. The basal expression of LIF in vivo is low; and its expression is induced by pro-inflammatory factors, including lipopolysaccharide, IL-1, and IL-17, and inhibited by anti-inflammatory agents, including IL-4 and IL-13. The functions of LIF include proliferation of primordial germ cells, regulation in blastocyst implantation and early pregnancy, and maintenance of pluripotent embryonic stem cells.

Leukemia Inhibitory Factor (LIF) is a pleiotropic cytokine belonging to the long four-helix bundle cytokine superfamily. LIF shares tertiary structure with several other cytokines, including Interleukin-6 (IL-6), Oncostatin M, ciliary neurotropic factor, and cardiotrophin-1, and their functions in vivo are also redundant to some extent. LIF can bind to the common receptor of IL-6 subfamily, gp130, and then recruit its own receptor LIF Receptor to form a ternary complex. The basal expression of LIF in vivo is low; and its expression is induced by pro-inflammatory factors, including lipopolysaccharide, IL-1, and IL-17, and inhibited by anti-inflammatory agents, including IL-4 and IL-13. The functions of LIF include proliferation of primordial germ cells, regulation in blastocyst implantation and early pregnancy, and maintenance of pluripotent embryonic stem cells.

Leukemia Inhibitory Factor (LIF) is a pleiotropic cytokine belonging to the long four-helix bundle cytokine superfamily. LIF shares tertiary structure with several other cytokines, including Interleukin-6 (IL-6), Oncostatin M, ciliary neurotropic factor, and cardiotrophin-1, and their functions in vivo are also redundant to some extent. LIF can bind to the common receptor of IL-6 subfamily, gp130, and then recruit its own receptor LIF Receptor to form a ternary complex. The basal expression of LIF in vivo is low; and its expression is induced by pro-inflammatory factors, including lipopolysaccharide, IL-1, and IL-17, and inhibited by anti-inflammatory agents, including IL-4 and IL-13. The functions of LIF include proliferation of primordial germ cells, regulation in blastocyst implantation and early pregnancy, and maintenance of pluripotent embryonic stem cells.

Platelet-Derived Growth Factor (PDGF) is a potent mitogen for a wide range of cell types including fibroblasts, smooth muscle, connective tissue, bone and cartilage cells, and some blood cells. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. The PDGF family consists of proteins derived from four genes (PDGF -A, -B, -C, and -D) that form four disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and one heterodimer (PDGF-AB).

Platelet-Derived Growth Factor (PDGF) is a potent mitogen for a wide range of cell types including fibroblasts, smooth muscle, connective tissue, bone and cartilage cells, and some blood cells. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. The PDGF family consists of proteins derived from four genes (PDGF -A, -B, -C, and -D) that form four disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and one heterodimer (PDGF-AB).