CD270 

TNFRSF14 (tumor necrosis factor receptor superfamily, member 14), HVEM, LIGHT-R

Molecule TypeAntigen ExpressionMolecular Weight
Min / Max
Non-lineage Restricted Molecule
Type 1 glycoprotein
Thymus
Spleen
Lung
T Cell
Monocyte
Dendritic Cell
30 / 30

Expression

CD270 is expressed on resting T cells, monocytes and immature dendritic cells.  T cell activation and CD258 (LIGHT) binding both downregulate CD270 expression.  CD270 is widely expressed with the highest expression in lung, spleen and thymus.



Structure
MOLECULAR FAMILY NAME: Belongs to the tumor necrosis factor receptor family.

CD270 is a single-pass type-1 283 aa glycoprotein.  It contains a 38 aa signal sequence, an extracellular domain which contains 4 tumor necrosis factor receptor  cysteine-rich domains, (CRD1-4) , a transmembrane domain and cytoplasmic domain.  CD270 is the receptor for CD258.  The binding site for CD258 maps to CRD2 and CRD3 of CD270 and is known as the DARC site.  CRD1 contains the distinct but overlapping binding sites for CD272 (BTLA) and herpes virus glycoprotein D (gD).  gD contacts CRD2 as well as CRD1 but on the opposite side to the CD258 binding site.  The cysteine-rich repeat regions are characteristic of TNFR family members and shares 17-25% aa identity with other TNFRs.  Ligand binding to CD258 induces CD270 trimerization.

MOLECULAR MASS

POST-TRANSCRIPTIONAL MODIFICATION: No information.

POST-TRANSLATIONAL MODIFICATION

CD270 is N-glycosylated.

Ligands
LIGANDS AND MOLECULE ASSOCIATED WITH CD270

CD270 binds CD258 (LIGHT), CD272 (BTLA) and glycoprotein D of h
erpes simplex viruses HSV-1 and HSV-2.

Function
Ligation of CD270 with a monoclonal antibody stimulates in an IFN-γ-dependent manner the secretion of TNFα and the angiogenic factor IL-8 by the THP-1 monocytic cell line.  Furthermore, the THP-1 monocytes produced interstitial collagenase (MMP-1), interstitial collagenase-3 (MMP-13) and gelatinase B (MMP-9).  CD270 expression correlated with expression of the matrix metalloproteases in foam rich regions of human atherosclerotic lesions.  In contrast to the positive signaling when bound to CD258 binding of CD270 to CD272 does not trigger CD270 but does provide an inhibitory signal to T cells via CD272.  Binding of HSV viral envelope glycoprotein D to this receptor has been shown to be part of the viral entry mechanism.  CD258/ CD270 has been identified as a cellular mediator of herpes simplex virus (HSV) entry and plays a role in HSV pathogenesis because it enhances the entry of several wild-type HSV strains into CHO cells and mediates HSV entry into activated human T cells. The cytoplasmic region of this receptor was found to bind to several TRAF family members, which may mediate the signal transduction pathways that activate the immune response.

BIOCHEMICAL ACTIVITY: No information.

DISEASE RELEVANCE AND FUNCTION OF CD270 IN INTACT ANIMAL

CD258/CD270 signaling is implicated in macrophage- and macrophage-derived foam cell-mediated development of atherosclerotic lesions.  CD270 expression correlated with the expression of the matrix metalloproteases in foam rich regions of human lesions.

Comments
MOLECULAR INTERACTIONS-
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD270: No information.

SUBSTRATES: No information.

ENZYMES WHICH MODIFY CD270: No information.

Database accession numbers
AnimalPIRSWISSPROTEMGBL/GENBANK
 
HumanEntrezgene 8764Q92956
Antibodies

Revised June 25, 2008


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