CD62E SELE (selection-E endothelial adhesion molecule 1), ELAM-1, LECAM-2
Molecule TypeAntigen ExpressionMolecular Weight
Min / Max
Non-lineage Restricted Molecule
Type 1 glycoprotein
Skin
Bone Marrow
Endothelium
Synovium
Placenta
97 / 97
107 / 107
115 / 115

Expression
CD62E is expressed on acutely activated endothelium and on the endothelium in chronic inflammatory lesions of the skin and synovium.  In addition, noninflammatory expression of CD62E has been observed on endothelium in placenta and bone marrow.

Structure
MOLECULAR FAMILY NAME: Belongs to the selectin C-type lectin family.

CD62E is a single-pass type-1 589 aa glycoprotein.  It contains a 535 aa extracellular domain which contains a N-terminus lectin C-type domain, a epidermal growth factor (EGF) domain, 6 complement control binding protein (CCP) domains and 11 N-linked glycosylation sites, a 22 aa transmembrane domain and a 32 aa intracellular cytoplasmic domain.  CD62E is a member of the selectin family of cell surface molecules and is structurally related to CD62L and CD62P.

MOLECULAR MASS
Cell Type Unreduced Reduced Comment
IL-1 treated endothelial cells (HEC, HUVEC) 115 kDa 115 kDa, 97 kDa
CD62E-transfected COS cells 107 kDa 107 kDa, 97 kDa

POST-TRANSCRIPTIONAL MODIFICATION: No information.

POST-TRANSLATIONAL MODIFICATION

CD62E has 11 possible N-linked glycosylation sites that are present in the extracellular region.

Ligands
CD62E recognizes carbohydrate ligands and like CD62L and CD62P, CD62E binds with a low affinity to oligosaccharide sequences related to sialylated Lewis x (sLe x, CD15s) through its C-type lectin domain.  The carbohydrate binding site on this domain has been localized to a region surrounding the Ca2+ binding site.  CD62E binds particularly well to 3-sialyl di-Le x, comprising sLe x followed by an additional Le x unit, which is an unusual structure found only on N-glycans.  CF62E has 1 glycoprotein ligand that is a particular glycoform of the ubiquitous protein ESL-1 which is restricted to myeloid cells.  Binding requires N-glycans on ESL-1 containing both sialic acid and fucose.  CD62E also binds to the CD62P ligand CD162 PSGL-1.  Activation of endothelial cells leads to association of CD62E with the actin cytoskeleton through its cytoplasmic portion.

LIGANDS AND MOLECULES ASSOCIATED WITH CD62E
Molecule Comment
Sialyl Lewis x
Sialyl Lewis a
ESL-1 (mouse)
CLA (cutaneous leukocyte antigen)
CD162 (PSGL-1)




Function
CD62E recognizes carbohydrate ligands like sialyl Lewis X (CD15s) on various molecules including GlyCAM1, CD34, CD107a, CD162 and ESL-1(mouse).  Like other selectins, CD62E is an adhesion molecule that contributes to the initial tethering and rolling of leukocytes on activated endothelium at inflammatory sites, a prerequisite for leukocyte extravasation into tissues.  CD62E, like CD62L, contributes to the later stages of leukocyte influx into inflamed tissues.  Although no abnormality has been detected in CD62E-deficient mice, these mice are unusually susceptible to the blocking of CD62P, suggesting overlapping but complementary roles for these molecules.  In support of this, mice deficient in both CD62E and CD62P have severe defects in leukocyte recruitment to inflammatory sites and are susceptible to opportunistic bacterial infections.  

BIOCHEMICAL ACTIVITY: No information.

DISEASE RELEVANCE AND FUNCTION OF CD62E IN INTACT ANIMAL

CD62E may also support tumor cell adhesion during hematogenous metastasis, and may play a role in angiogensis.  CD62E mediates adhesion of neutrophils to the blood vessel lining.  CD62E participates in the interaction between leukocytes and the endothelium and appears to be involved in the pathogenesis of atherosclerosis.  Function-blocking antibodies have been reported to decrease leukocyte-mediated damage in a rodent model of lung inflammation.  In CD62E KO mice, there are no significant changes in the recruitment of leukocytes in certain models of inflammation.  However, abnormalities are observed in CD62E KO mice when the function of CD62P is also blocked, and KO mice, CD62E + CD62P, do have reduced leukocyte recruitment to inflammatory sites and are less resistant to opportunistic infections.  Similarly, patients with LADII syndrome, who lack the sialyl Lewis x component of the selectin counter-receptors, suffer recurrent pyogenic infections.

Comments
MOLECULAR INTERACTIONS -
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD62E
Molecule Comment
AP-1
NF-kB
TF-2
HMGI (Y)

SUBSTRATES: No information.

ENZYMES WHICH MODIFY CD62E: No information.


Database accession numbers
AnimalPIRSWISSPROTEMGBL/GENBANK
 
HumanEntrezgene 6401P16581
MouseQ00690M80778
RatP98105L25527
Antibodies

Revised June 25, 2008


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