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. Feline TNF-α consists of a 35 amino acid
(aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 177 aa extracellular
domain (ECD). Within the ECD, feline TNF-α shares 85% 94% aa sequence identity with
canine, equine, human, porcine, and rhesus and 69% 77% with bovine, cotton rat, mouse,
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 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. Feline TNF-α consists of a 35 amino acid
(aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 177 aa extracellular
domain (ECD). Within the ECD, feline TNF-α shares 85% 94% aa sequence identity with
canine, equine, human, porcine, and rhesus and 69% 77% with bovine, cotton rat, mouse,
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 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.
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