CD144 CDH5 (cadherin 5, type2 VE-cadherin vascular epithelium),
Molecule TypeAntigen ExpressionMolecular Weight
Min / Max
Non-lineage Restricted Molecule
Type 1 glycoprotein
Endothelial Cell
Brain
Stem Cell
130 / 130
135 / 135

Expression
CD144 is expressed on stem cell subsets, endothelial cells, endothelia tissues and brain but is not expressed on any other cell types. 



Structure
MOLECULAR FAMILY Belongs to the cadherin superfamily.

CD144 is a type-1 784 aa glycoprotein.  It contains an 593 aa extracellular region which contains 5 cadherin homologous repeats that form a rigid rod-like structure stabilized by the binding of Ca2+ ions between the repeats and contains 7 potential N-linked glycosylation sites, a transmembrane region and a highly conserved 164 aa cytoplasmic tail which has at the distal end a catenin-binding domain.  It is a calcium-dependent cell-cell adhesion glycoprotein. 

MOLECULAR MASS
Cell Type Unreduced Reduced
Endothelial cells 135 kDa 130 kDa

POST-TRANSCRIPTIONAL MODIFICATION: No information.

POST-TRANSLATIONAL MODIFICATION

CD144 has 7 potential N-glycosylation sites and 9 tyrosines in the cytoplasmic domain.  The molecule can be phosphorylated on tyrosine.


Ligands
CD144 displays homotypic binding only.

LIGANDS AND MOLECULES ASSOCIATED WITH CD144
Molecule Comment
VE-cadherin Homotypic adhesion, mediates adhesion
b catenin
Plakoglobin
P120 CAS



Function
CD144 is a Ca++-dependent homophilic cell adhesion molecule found in adherens junctions in endothelial cells.   Adherens junctions control endothelial cell-cell adhesion and migration of vascular endothelial cells as well as the permeability of microvascular endothelium.  CD144 plays a role in the contact inhibition of endothelial cell growth.  The functions of CD144 are modulated by various catenins, which are critical to its interaction with the cell cytoskeleton and its own intracellular trafficking.  β-catenin and γ-catenin (plakoglobin) associate direcetly with catenin binding domain of the CD144 cytoplasmic domain and via α-catenin link the cadherin to the actin cytoskeleton.  Plakoglobin can bind desmoplakin, which in turn mediates associates with the vimentin/intermediate filament cytoskeleton.  p120-catenin associates with the juxtamembrane region of the cytoplasmic domain and plays a regulatory role in cadherin trafficking.  Another catenin, p0071 (plakophilin-4) binds the same region of CD144 as p120-catenin and can bind desmoplakin and the ultimate link CD144 to the intermediate filament cytoskelton.  CD144 functions by impairing to cells the ability to adhere in a homophilic manner and may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. 

BIOCHEMICAL ACTIVITY

CD144 has homotypic binding and VE-cadherin only binds to VE-cadherin.

DISEASE RELEVANCE AND FUNCTION OF CD144 IN INTACT ANIMAL

CD144 is involved in the loss of heterozgosity events in breast and prostate cancer.  Expression is reduced in human angiosarcomas.

Comments
MOLECULAR INTERACTIONS -
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD144: No information.

SUBSTRATES: No information.

ENZYMES WHICH MODIFY CD144
Molecule Comment
Tyrosine kinases


Database accession numbers
AnimalPIRSWISSPROTEMGBL/GENBANK
 
HumanEntrezgene 1003P33151
Antibodies
I23   View Reactivity

Revised June 25, 2008


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