N-末端の細胞外領域にC型レクチンドメインを持つ。P-（血小板）L-（白血球）E-（内皮）の三種類のセレクチンが知られている。
P-セレクチンは血小板以外に血管内皮にも発現している。白血球の受容体（P-セレクチン糖タンパク質リガンド１、PSGL-1）と結合する。
PSGL-1は白血球に発現しており、ムチンリピートをもち、N-末端附近に硫酸化チロシン、ムチンリピートにシアリルルイス構造をもち、P-セレクチンのリガンドとなる。
P-selectin
Alternative name(s):
CD62 antigen-like family member P
Granule membrane protein 140
Short name=GMP-140
Leukocyte-endothelial cell adhesion molecule 3
Short name=LECAM3
Platelet activation dependent granule-external membrane protein
Short name=PADGEM
CD_antigen=CD62P
:Function
Ca2+-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1. Ref.7
Subunit structure
Interacts with SNX17. Interacts with PSGL1/SEPL and PODXL2 and mediates neutrophil adhesion and leukocyte rolling. This interaction requires the sialyl-Lewis X epitope of PSGL1 and PODXL2, and specific tyrosine sulfation on PSGL1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.15
Subcellular location
Membrane; Single-pass type I membrane protein.
Tissue specificity
Stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Upon cell activation by agonists, P-selectin is transported rapidly to the cell surface.
Involvement in disease
Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.20
Sequence similarities
Belongs to the selectin/LECAM family.
Contains 1 C-type lectin domain.
Contains 1 EGF-like domain.
Contains 9 Sushi (CCP/SCR) domains.
E-selectin
Alternative name(s):
CD62 antigen-like family member E
Endothelial leukocyte adhesion molecule 1
Short name=ELAM-1
Leukocyte-endothelial cell adhesion molecule 2
Short name=LECAM2
CD_antigen=CD62E
:Function
Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with PSGL1/SELPLG. May have a role in capillary morphogenesis. Ref.1
Subunit structure
Interacts with PSGL1/SELPLG and PODXL2 through the sialyl Lewis X epitope. PSGL1 sulfation appears not to be required for this interaction. Ref.9 Ref.12
Subcellular location
Membrane; Single-pass type I membrane protein.
Polymorphism
A polymorphism in position 149 is associated with a higher risk of coronary artery disease (CAD). A significantly higher mutation frequency (Arg-149) is observed in patients with angiographically proven severe atherosclerosis compared with an unselected population (Ser-149).
Sequence similarities
Belongs to the selectin/LECAM family.
Contains 1 C-type lectin domain.
Contains 1 EGF-like domain.
Contains 6 Sushi (CCP/SCR) domains.
L-selectin
Alternative name(s):
CD62 antigen-like family member L
Leukocyte adhesion molecule 1
Short name=LAM-1
Leukocyte surface antigen Leu-8
Leukocyte-endothelial cell adhesion molecule 1
Short name=LECAM1
Lymph node homing receptor
TQ1
gp90-MEL
CD_antigen=CD62L
:Function
Cell surface adhesion protein. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia. Ref.12
Subunit structure
Interaction with PSGL1/SELPLG and PODXL2 is required for promoting recruitment and rolling of leukocytes. This interaction is dependent on the sialyl Lewis X glycan modification of PSGL1 and PODXL2, and tyrosine sulfation modifications of PSGL1. Sulfation on 'Tyr-51' of PSGL1 is important for L-selectin binding.
Subcellular location
Membrane; Single-pass type I membrane protein.
Tissue specificity
Expressed in B-cell lines and T-lymphocytes. Ref.2
Sequence similarities
Belongs to the selectin/LECAM family.
Contains 1 C-type lectin domain.
Contains 1 EGF-like domain.
Contains 2 Sushi (CCP/SCR) domains.
P-selectin glycoprotein ligand 1
Short name=PSGL-1
Alternative name(s):
Selectin P ligand
CD_antigen=CD162
:Function
A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture. Ref.13 Ref.15
Subunit structure
Homodimer; disulfide-linked. Interaction with P-, E- and L-selectins, through their lectin/EGF domains, is required for promoting recruitment and rolling of leukocytes. These interactions require sialyl Lewis X glycan modification but there is a differing dependence for tyrosine sulfations. Sulfation on Tyr-51 of PSGL1 is most important for high affinity L-selectin/SELL binding while P-selectin/SELP requires sulfation on Tyr-48. E-selectin/SELE binds with much lower affinity and requires the sLe(x) epitope, but apparantly not tyrosine sulfation. Dimerization appears not to be required for P-selectin/SELP binding. Interacts with SNX20. Interacts with MSN and SYK; mediates the activation of SYK by SELPLG. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Subcellular location
Membrane; Single-pass type I membrane protein.
Tissue specificity
Expressed on neutrophils, monocytes and most lymphocytes.
Post-translational modification
Displays complex, core-2, sialylated and fucosylated O-linked oligosaccharides, at least some of which appear to contain poly-N-acetyllactosamine with varying degrees of substitution. Mainly disialylated or neutral forms of the core-2 tetrasaccharide, Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% fucose with alpha-1,3 linkage present in two forms: One species is a disialylated, monofucosylated glycan, and the other, a monosialylated, trifucosylated glycan with a polylactosamine backbone. The fucosylated forms carry the Lewis antigen and are important for interaction with selectins and for functioning in leukocyte rolling. The modification containing the sialyl Lewis X glycan is on Thr-57. No sulfated O-glycans. Some N-glycosylation.
Sulfation, in conjunction with the SLe(x)-containing glycan, is necessary for P- and L-selectin binding. High affinity P-selectin binding has a preferred requirement for the isomer sulfated on both Tyr-48 and Tyr-51, whereas L-selectin binding requires predominantly sulfation on Tyr-51 with sulfation on Tyr-48 playing only a minor role. These sulfations play an important role in L- and P-selectin-mediated neutrophil recruitment, and leukocyte rolling.
