描述:
Tumor necrosis factor alpha (TNFα), also known as cachectin and TNFSF1A, is the
prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a
central role in inflammation, apoptosis, and immune system development. TNFα
is produced by a wide variety of immune and epithelial cell types. Rhesus
TNFα consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane
segment, and a 177 aa extracellular domain (ECD). Within the ECD, rhesus
TNFα shares 97% aa sequence identity with human and 71%92% with bovine,
canine, cotton rat, equine, feline, mouse, porcine, and rat TNFα. The 26 kDa type 2
transmembrane protein is assembled intracellularly to form a noncovalently linked
homotrimer. Ligation of this complex induces reverse signaling that promotes
lymphocyte costimulation but diminishes monocyte responsiveness. Cleavage of
membrane bound TNFα by TACE/ADAM17 releases a 55 kDa soluble trimeric
form of TNFα. TNFα trimers bind the ubiquitous TNF RI and the hematopoietic
cellrestricted TNF RII, both of which are also expressed as homotrimers.
TNFα regulates lymphoid tissue development through control of apoptosis.
It also promotes inflammatory responses by inducing the activation of vascular
endothelial cells and macrophages. TNFα is a key cytokine in the development
of several inflammatory disorders. It contributes to the development of type 2
diabetes through its effects on insulin resistance and fatty acid metabolism.
原厂资料:
Tumor necrosis factor alpha (TNFα), also known as cachectin and TNFSF1A, is the
prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a
central role in inflammation, apoptosis, and immune system development. TNFα
is produced by a wide variety of immune and epithelial cell types. Rhesus
TNFα consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane
segment, and a 177 aa extracellular domain (ECD). Within the ECD, rhesus
TNFα shares 97% aa sequence identity with human and 71%92% with bovine,
canine, cotton rat, equine, feline, mouse, porcine, and rat TNFα. The 26 kDa type 2
transmembrane protein is assembled intracellularly to form a noncovalently linked
homotrimer. Ligation of this complex induces reverse signaling that promotes
lymphocyte costimulation but diminishes monocyte responsiveness. Cleavage of
membrane bound TNFα by TACE/ADAM17 releases a 55 kDa soluble trimeric
form of TNFα. TNFα trimers bind the ubiquitous TNF RI and the hematopoietic
cellrestricted TNF RII, both of which are also expressed as homotrimers.
TNFα regulates lymphoid tissue development through control of apoptosis.
It also promotes inflammatory responses by inducing the activation of vascular
endothelial cells and macrophages. TNFα is a key cytokine in the development
of several inflammatory disorders. It contributes to the development of type 2
diabetes through its effects on insulin resistance and fatty acid metabolism.