描述:
Tumor necrosis factor alpha (TNF-α), 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. TNF-α is produced by a wide
variety of immune and epithelial cell types. Canine TNF-α consisits of a 35 amino acid (aa)
cytoplasmic domain, a 21 aa transmembrane segment, and a 177 aa extracellular domain
(ECD). Within the ECD, canine TNFα shares 84%94% aa sequence identity with equine, feline,
human, porcine, and rhesus and 69%-77% with bovine, cotton rat, mouse, and rat with TNF-α.
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 TNF-α
by TACE/ADAM17 releases a 55 kDa soluble trimeric form of TNF-α. TNF-α trimers bind the
ubiquitous TNF RI and the hematopoietic cell-restricted TNF RII, both of which are also
expressed as homotrimers. TNF-α regulates lymphoid tissue development through control of
apoptosis. It also promotes inflammatory responses by inducing the activation of vascular
endothelial cells and macrophages.TNF-α 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 (TNF-α), 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. TNF-α is produced by a wide
variety of immune and epithelial cell types. Canine TNF-α consisits of a 35 amino acid (aa)
cytoplasmic domain, a 21 aa transmembrane segment, and a 177 aa extracellular domain
(ECD). Within the ECD, canine TNFα shares 84%94% aa sequence identity with equine, feline,
human, porcine, and rhesus and 69%-77% with bovine, cotton rat, mouse, and rat with TNF-α.
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 TNF-α
by TACE/ADAM17 releases a 55 kDa soluble trimeric form of TNF-α. TNF-α trimers bind the
ubiquitous TNF RI and the hematopoietic cell-restricted TNF RII, both of which are also
expressed as homotrimers. TNF-α regulates lymphoid tissue development through control of
apoptosis. It also promotes inflammatory responses by inducing the activation of vascular
endothelial cells and macrophages.TNF-α 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.