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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/06/29 02:56:59」(JST)

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Crystallographic structure P selectin lectin bound to sugar, shown in sticks.^[1]

The selectins (cluster of differentiation 62 or CD62) are a family of cell adhesion molecules (or CAMs). All selectins are single-chain transmembrane glycoproteins that share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding.^[2] Selectins bind to sugar moieties and so are considered to be a type of lectin, cell adhesion proteins that bind sugar polymers.^[3]

Structure

All three known members of the selectin family (L-, E-, and P-selectin) share a similar cassette structure: an N-terminal, calcium-dependent lectin domain, an epidermal growth factor (EGF)-like domain, a variable number of consensus repeat units (2, 6, and 9 for L-, E-, and P-selectin, respectively), a transmembrane domain (TM) and an intracellular cytoplasmic tail (cyto). The transmembrane and cytoplasmic parts are not conserved across the selectins being responsible for their targeting to different compartments.^[4] Though they share common elements, their tissue distribution and binding kinetics are quite different, reflecting their divergent roles in various pathophysiological processes.^[5]

Types

There are three subsets of selectins:

E-selectin (in endothelial cells)
L-selectin (in lymphocytes)
P-selectin (in platelets and endothelial cells)

L-selectin is the smallest of the vascular selectins, expressed on all granulocytes and monocytes and on most lymphocytes, can be found in most leukocytes. P-selectin, the largest selectin, is stored in α-granules of platelets and in Weibel–Palade bodies of endothelial cells, and is translocated to the cell surface of activated endothelial cells and platelets. E-selectin is not expressed under baseline conditions, except in skin microvessels, but is rapidly induced by inflammatory cytokines.

These three types share a significant degree of sequence homology among themselves (except in the transmembrane and cytoplasmic domains) and between species. Analysis of this homology has revealed that the lectin domain, which binds sugars, is most conserved, suggesting that the three selectins bind similar sugar structures. Interestingly, the cytoplasmic and transmembrane domains are highly conserved between species, but not conserved across the selectins. These parts of the selectin molecules are responsible for their targeting to different compartments: P-selectin to secretory granules, E-selectin to the plasma membrane, and L-selectin to the tips of microfolds on leukocytes.^[4]

Etymology

The name selectin comes from the words "selected" and "lectins," which are a type of carbohydrate-recognizing protein.^{[citation needed]}

Function

Selectins are involved in constitutive lymphocyte homing, and in chronic and acute inflammation processes, including post-ischemic inflammation in muscle, kidney and heart, skin inflammation, atherosclerosis, glomerulonephritis and lupus erythematosus^[4] and cancer metastasis.

During an inflammatory response, stimuli such as histamine and thrombin cause endothelial cells to mobilize P-selectin from stores inside the cell to the cell surface. In addition, cytokines such as TNF-alpha stimulate the expression of E-selectin and additional P-selectin a few hours later.

As the leukocyte rolls along the blood vessel wall, the distal lectin-like domain of the selectin binds to certain carbohydrate groups presented on proteins (such as PSGL-1) on the leukocyte, which slows the cell and allows it to leave the blood vessel and enter the site of infection. The low-affinity nature of selectins is what allows the characteristic "rolling" action attributed to leukocytes during the leukocyte adhesion cascade.^[2]

Each selectin has a carbohydrate recognition domain that mediates binding to specific glycans on apposing cells. They have remarkably similar protein folds and carbohydrate binding residues,^[1] leading to overlap in the glycans to which they bind.

Selectins bind to the sialyl Lewis X (SLe^x) determinant “NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc.” However, SLe^x, per se, does not constitute an effective selectin receptor. Instead, SLe^x and related sialylated, fucosylated glycans are components of more extensive binding determinants.^[6]

The best-characterized ligand for the three selectins is P-selectin glycoprotein ligand-1 (PSGL-1), which is a mucin-type glycoprotein expressed on all white blood cells.

Neutrophils and eosinophils bind to E-selectin. One of the reported ligands for E-selectin is the sialylated Lewis X antigen (SLe^x). Eosinophils, like neutrophils, use sialylated, protease-resistant structures to bind to E-selectin, although the eosinophil expresses much lower levels of these structures on its surface.^[7]

Ligands for P-selectin on eosinophils and neutrophils are similar sialylated, protease-sensitive, endo-beta-galactosidase-resistant structures, clearly different than those reported for E-selectin, and suggest disparate roles for P-selectin and E-selectin during recruitment during inflammatory responses.^[8]

Bonding mechanisms

Selectins have hinge domains, allowing them to undergo rapid conformational changes in the nanosecond range between ‘open’ and ‘closed’ conformations. Shear stress on the selectin molecule causes it to favor the ‘open’ conformation.^[9]

In leukocyte rolling, the ‘open’ conformation of the selectin allows it to bind to inward sialyl Lewis molecules farther up along the PSGL-1 chain, increasing overall binding affinity—if the selectin-sialyl Lewis bond breaks, it can slide and form new bonds with the other sialyl Lewis molecules down the chain. In the ‘closed’ conformation, however, the selectin is only able to bind to one sialyl Lewis molecule, and thus has greatly reduced binding affinity.

The result of such is that selectins exhibit catch and slip bond behavior—under low shear stresses, their bonding affinities are actually increased by an increase in tensile force applied to the bond because of more selectins preferring the ‘open’ conformation. At high stresses, the binding affinities are still reduced because the selectin-ligand bond is still a normal slip bond. It is thought that this shear stress threshold helps select for the right diameter of blood vessels to initiate leukocyte extravasation, and may also help prevent inappropriate leukocyte aggregation during vascular stasis.^[10]

Role in cancer

It is becoming evident that selectin may play a role in inflammation and progression of cancer.^[4] Tumor cells exploit the selectin-dependent mechanisms mediating cell tethering and rolling interactions through recognition of carbohydrate ligands on tumor cell to enhance distant organ metastasis,^[11]^[12] showing ‘leukocyte mimicry’.^[13]

A number of studies have shown increased expression of carbohydrate ligands on metastatic tumor,^[14] enhanced E-selectin expression on the surface of endothelial vessels at the site at tumor metastasis,^[15] and the capacity of metastatic tumor cells to roll and adhere to endothelial cells, indicating the role of selectins in metastasis.^[16] In addition to E-selectin, the role of P-selectin (expressed on platelets) and L-selectin (on leukocytes) in cancer dissemination has been suggested in the way that they interact with circulating cancer cells at an early stage of metastasis.^[17]^[18]

Organ selectivity

The selectins and selectin ligands determine the organ selectivity of metastasis. Several factors may explain the seed and soil theory or homing of metastasis. In particular, genetic regulation and activation of specific chemokines, cytokines and proteases may direct metastasis to a preferred organ. In fact, the extravasation of circulating tumor cells in the host organ requires successive adhesive interactions between endothelial cells and their ligands or counter-receptors present on the cancer cells. Metastatic cells that show a high propensity to metastasize to certain organs adhere at higher rates to venular endothelial cells isolated from these target sites. Moreover, they invade the target tissue at higher rates and respond better to paracrine growth factors released from the target site.

Typically, the cancer cell/endothelial cell interactions imply first a selectin-mediated initial attachment and rolling of the circulating cancer cells on the endothelium. The rolling cancer cells then become activated by locally released chemokines present at the surface of endothelial cells. This triggers the activation of integrins from the cancer cells allowing their firmer adhesion to members of the Ig-CAM family such as ICAM, initiating the transendothelial migration and extravasation processes.[72]

The appropriate set of endothelial receptors is sometimes not expressed constitutively and the cancer cells have to trigger their expression. In this context, the culture supernatants of cancer cells can trigger the expression of E- selectin by endothelial cells suggesting that cancer cells may release by themselves cytokines such as TNF-α, IL-β or INF-γ that will directly activate endothelial cells to express E-selectin, P-selectin, ICAM-2 or VCAM. On the other hand, several studies further show that cancer cells may initiate the expression of endothelial adhesion molecules in a more indirect ways.

Since the adhesion of several cancer cells to endothelium requires the presence of endothelial selectins as well as sialyl Lewis carbohydrates on cancer cells, the degree of expression of selectins on the vascular wall and the presence of the appropriate ligand on cancer cells are determinant for their adhesion and extravasation into a specific organ. The differential selectin expression profile on endothelium and the specific interactions of selectins expressed by endothelial cells of potential target organs and their ligands expressed on cancer cells are major determinants that underlie the organ-specific distribution of metastases.

Research

Selectins are involved in projects to treat osteoporosis, a disease that occurs when bone-creating cells called osteoblasts become too scarce. Osteoblasts develop from stem cells, and scientists hope to eventually be able to treat osteoporosis by adding stem cells to a patient’s bone marrow. Researchers have developed a way to use selectins to direct stem cells introduced into the vascular system to the bone marrow.^[19] E-selectins are constitutively expressed in the bone marrow, and researchers have shown that tagging stem cells with a certain glycoprotein causes these cells to migrate to the bone marrow. Thus, selectins may someday be essential to a regenerative therapy for osteoporosis.^[20]

References

^ ^a ^b PDB: 1G1R; Somers WS; Tang J; Shaw GD; Camphausen RT (October 2000). "Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1". Cell 103 (3): 467–79. doi:10.1016/S0092-8674(00)00138-0. PMID 11081633.
^ ^a ^b Cotran; Kumar, Collins (1998). Robbins Pathologic Basis of Disease. Philadelphia: W.B Saunders Company. ISBN 0-7216-7335-X.
^ Parham, Peter (2005). The immune system (2nd ed.). New York: Garland Science. pp. 244–245. ISBN 0-8153-4093-1.
^ ^a ^b ^c ^d Ley K (June 2003). "The role of selectins in inflammation and disease". Trends Mol Med 9 (6): 263–8. doi:10.1016/S1471-4914(03)00071-6. PMID 12829015.
^ Cheung LS; Raman PS; Balzer EM; Wirtz D; Konstantopoulos K (February 2011). "Biophysics of selectin-ligand interactions in inflammation and cancer". Phys Biol 8 (1): 015013. doi:10.1088/1478-3975/8/1/015013. PMID 21301059.
^ Nimrichter L; Burdick MM; Aoki K; Laroy W; Fierro MA; Hudson SA; Von Seggern CE; Cotter RJ; Bochner BS; Tiemeyer M; Konstantopoulos K; Schnaar RL (November 2008). "E-selectin receptors on human leukocytes". Blood 112 (9): 3744–52. doi:10.1182/blood-2008-04-149641. PMC 2572800. PMID 18579791.
^ Bochner BS; Sterbinsky SA; Bickel CA; Werfel S; Wein M; Newman W (January 1994). "Differences between human eosinophils and neutrophils in the function and expression of sialic acid-containing counterligands for E-selectin". J. Immunol. 152 (2): 774–82. PMID 7506734.
^ Wein M; Sterbinsky SA; Bickel CA; Schleimer RP; Bochner BS (March 1995). "Comparison of human eosinophil and neutrophil ligands for P-selectin: ligands for P-selectin differ from those for E-selectin". Am. J. Respir. Cell Mol. Biol. 12 (3): 315–9. doi:10.1165/ajrcmb.12.3.7532979. PMID 7532979.
^ Thomas, W. "For Catch Bonds, it all hinges on the interdomain region". The Journal of Cell Biology 174: 911–913 (2006). doi:10.1083/jcb.200609029.
^ Yago, Tadayuki. "Catch Bonds Govern Adhesion through L-selectin at Threshold Shear". The Journal of Cell Biology 166: 913–923 (2004). doi:10.1083/jcb.200403144. PMC 2172126. PMID 15364963.
^ Barthel SR; Gavino JD; Descheny L; Dimitroff CJ (November 2007). "Targeting selectins and selectin ligands in inflammation and cancer". Expert Opin. Ther. Targets 11 (11): 1473–91. doi:10.1517/14728222.11.11.1473. PMC 2559865. PMID 18028011.
^ St Hill CA (2012). "Interactions between endothelial selectins and cancer cells regulate metastasis". Front. Biosci. 16: 3233–51. doi:10.2741/3909. PMID 21622232.
^ Witz IP (2006). "Tumor-microenvironment interactions: the selectin-selectin ligand axis in tumor-endothelium cross talk". Cancer Treat. Res. Cancer Treatment and Research 130: 125–40. doi:10.1007/0-387-26283-0_6. ISBN 978-0-387-26282-6. PMID 16610706.
^ Nakamori S; Kameyama M; Imaoka S; Furukawa H; Ishikawa O; Sasaki Y; Izumi Y; Irimura T (April 1997). "Involvement of carbohydrate antigen sialyl Lewis(x) in colorectal cancer metastasis". Dis. Colon Rectum 40 (4): 420–31. doi:10.1007/BF02258386. PMID 9106690.
^ Matsuura N; Narita T; Mitsuoka C; Kimura N; Kannagi R; Imai T; Funahashi H; Takagi H (1997). "Increased concentration of soluble E-selectin in the sera of breast cancer patients". Anticancer Res. 17 (2B): 1367–72. PMID 9137500.
^ Gout S; Morin C; Houle F; Huot J (September 2006). "Death receptor-3, a new E-Selectin counter-receptor that confers migration and survival advantages to colon carcinoma cells by triggering p38 and ERK MAPK activation". Cancer Res. 66 (18): 9117–24. doi:10.1158/0008-5472.CAN-05-4605. PMID 16982754.
^ Borsig L; Wong R; Hynes RO; Varki NM; Varki A (February 2002). "Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis". Proc. Natl. Acad. Sci. U.S.A. 99 (4): 2193–8. doi:10.1073/pnas.261704098. PMC 122341. PMID 11854515.
^ Peeters CF; Ruers TJ; Westphal JR; de Waal RM (February 2005). "Progressive loss of endothelial P-selectin expression with increasing malignancy in colorectal cancer". Lab. Invest. 85 (2): 248–56. doi:10.1038/labinvest.3700217. PMID 15640834.
^ In the lab of Robert Sackstein Harvard University
^ Sackstein Lab

External links

Sackstein Lab of Research
Computer-generated movie of the mobilization of P-selectin inside a leukocyte at mcb.harvard.edu

UpToDate Contents

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English Journal

Chitosan oligosaccharides downregulate the expression of E-selectin and ICAM-1 induced by LPS in endothelial cells by inhibiting MAP kinase signaling.

Li Y, Xu Q, Wei P, Cheng L, Peng Q, Li S, Yin H, Du Y.Author information Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, Liaoning, P.R. China.AbstractThe expression of adhesion molecules in endothelial cells elicited by lipopolysaccharide (LPS) is involved in the adhesive interaction between endothelial cells and monocytes in inflammation. In this study, in order to characterize the anti-inflammatory effects of chitosan oligosaccharides (COS) on LPS‑induced inflammation and to elucidate the underlying mechanisms, the mRNA levels of E-selectin and intercellular adhesion molecule-1 (ICAM-1) were measured in porcine iliac artery endothelial cells (PIECs). When these cells were treated with COS, the LPS-induced mRNA expression of E-selectin and ICAM-1 was reduced through the inhibition of the signal transduction cascade, p38 mitogen‑activated protein kinase (MAPK)/extracellular regulated protein kinase 1/2 (ERK1/2) and nuclear factor-κB (NF-κB). Moreover, through the inhibition of p38 MAPK and ERK1/2, COS suppressed the LPS-induced NF-κB p65 translocation. We found that COS suppressed the phosphorylation of p38 MAPK and the translocation of NF-κB p65 into the nucleus in a dose-dependent manner, and inhibited the adhesion of U973 cells to PIECs. Based on these results, it can be concluded that COS downregulate the expression of E-selectin and ICAM-1 by inhibiting the phosphorylation of MAPKs and the activation of NF-κB in LPS-treated PIECs. Our study demonstrates the valuable anti-inflammatory properties of COS.
International journal of molecular medicine.Int J Mol Med.2014 Feb;33(2):392-400. doi: 10.3892/ijmm.2013.1589. Epub 2013 Dec 13.
The expression of adhesion molecules in endothelial cells elicited by lipopolysaccharide (LPS) is involved in the adhesive interaction between endothelial cells and monocytes in inflammation. In this study, in order to characterize the anti-inflammatory effects of chitosan oligosaccharides (COS) on
PMID 24336934

Carnosol inhibits cell adhesion molecules and chemokine expression by tumor necrosis factor-α in human umbilical vein endothelial cells through the nuclear factor-κB and mitogen-activated protein kinase pathways.

Yao H1, Chen Y1, Zhang L2, He X1, He X1, Lian L1, Wu X1, Lan P1.Author information 1Department of Colorectal Surgery, The Sixth Affiliated Hospital of Sun Yat-Sen University, Guangdong Gastrointestinal Hospital, Guangzhou, Guangdong 510655, P.R. China.2Laboratory of Surgery, The First Affiliated Hospital of Sun Yat-sen University, Guangzhou, Guangdong 510080, P.R. China.AbstractInflammatory bowel diseases (IBD) are gastrointestinal disorders associated with chronic inflammatory processes. Carnosol has been demonstrated to possess anti-inflammatory properties. This study examined the suppressive effect of carnosol on the expression of cell adhesion molecules (CAMs) and chemokines in human umbilical vein endothelial cells (HUVECs) and the possible underlying mechanism. The effect of carnosol on CAM and chemokine expression in HUVECs was identified by western blotting and ELISA, respectively. nuclear factor (NF)-κB activation of HUVECs was analyzed using the TransAM NF-κB Family kit. The effect of carnosol on the tumor necrosis factor (TNF)-α-induced activation of the NF-κB and mitogen-activated protein kinase (MAPK) pathways, and was subsequently analyzed using western blotting. Carnosol not only inhibited TNF-α-induced protein expression of intercellular adhesion molecule (ICAM)-1, vascular cell adhesion molecule (VCAM)-1 and E-selectin in HUVECs, but also suppressed interleukin (IL)-8 and monocyte chemoattractant protein (MCP)-1 expression. In addition, carnosol inhibited the TNF-α-induced phosphorylation of p-65 and IκB-α, as well as the activation of NF-κB. The same result was observed in TNF-α-stimulated phosphorylation of ERK1/2 and p-38. It was demonstrated that carnosol inhibited TNF-α-induced CAM and chemokine expression in HUVECs. The underlying mechanism may be associated with the blocking of the NF-κB and MAPK pathways. These results indicate that carnosol may be a novel therapeutic agent for targeting endothelial cells in IBDs.
Molecular medicine reports.Mol Med Rep.2014 Feb;9(2):476-80. doi: 10.3892/mmr.2013.1839. Epub 2013 Dec 3.
Inflammatory bowel diseases (IBD) are gastrointestinal disorders associated with chronic inflammatory processes. Carnosol has been demonstrated to possess anti-inflammatory properties. This study examined the suppressive effect of carnosol on the expression of cell adhesion molecules (CAMs) and chem
PMID 24316968

Isoflurane on brain inflammation.

Altay O1, Suzuki H1, Hasegawa Y1, Ostrowski RP1, Tang J1, Zhang JH2.Author information 1Department of Physiology, Loma Linda University School of Medicine, Loma Linda, USA.2Department of Physiology, Loma Linda University School of Medicine, Loma Linda, USA; Department of Neurosurgery, Loma Linda University School of Medicine, Loma Linda, USA. Electronic address: johnzhang3910@yahoo.com.AbstractBrain inflammation may play an important role in the pathophysiology of early brain injury after subarachnoid hemorrhage (SAH). Our aim was to demonstrate brain inflammation development and to determine whether isoflurane, a clinically available volatile anesthetic agent, prevents brain inflammation after SAH. This study used 162 8-week-old male CD-1 mice. We induced SAH with endovascular perforation in mice and randomly assigned animals to sham-operated (n=21), SAH+vehicle-air (n=35) and SAH+2% isoflurane (n=31). In addition to the evaluation of brain injury (neurological scores, brain edema and Evans blue dye extravasation), brain inflammation was evaluated by means of expression changes in markers of inflammatory cells (ionized calcium binding adaptor molecule-1, myeloperoxidase), cytokines (tumor necrosis factor [TNF]-α, interleukin-1β), adhesion molecules (intercellular adhesion molecule [ICAM]-1, P-selectin), inducers of inflammation (cyclooxygenase-2, phosphorylated c-Jun N-terminal kinase [p-JNK]) and endothelial cell activation (von Willebrand factor) at 24h post-SAH. Sphingosine kinase inhibitor (N, N-dimethylsphingosine [DMS]) and sphingosine-1-phosphate receptor-1/3 antagonist (VPC23019) were used to block isoflurane's effects (n=22, each). SAH caused early brain injury, which was associated with inflammation so that all evaluated markers of inflammation were increased. Isoflurane significantly inhibited both brain injury (P<0.001, respectively) and inflammation (myeloperoxidase, P=0.022; interleukin-1β, P=0.002; TNF-α, P=0.015; P-selectin, P=0.010; ICAM-1, P=0.016; p-JNK, P<0.001; cyclooxygenase-2, P=0.003, respectively). This beneficial effect of isoflurane was abolished with DMS and VPC23019. Isoflurane may suppress post-SAH brain inflammation possibly via the sphingosine-related pathway.
Neurobiology of disease.Neurobiol Dis.2014 Feb;62:365-71. doi: 10.1016/j.nbd.2013.09.016. Epub 2013 Sep 29.
Brain inflammation may play an important role in the pathophysiology of early brain injury after subarachnoid hemorrhage (SAH). Our aim was to demonstrate brain inflammation development and to determine whether isoflurane, a clinically available volatile anesthetic agent, prevents brain inflammation
PMID 24084689

Japanese Journal

Serum Adhesion Molecule Levels as Prognostic Markers in Patients with Early Systemic Sclerosis: A Multicentre, Prospective, Observational Study

Hasegawa Minoru,Asano Yoshihide,Endo Hirahito,Fujimoto Manabu,Goto Daisuke,Ihn Hironobu,Inoue Katsumi,Ishikawa Osamu,Kawaguchi Yasushi,Kuwana Masataka,Ogawa Fumihide,Takahashi Hiroki,Tanaka Sumiaki,Sato Shinichi,Takehara Kazuhiko
PLoS ONE 9(2), e88150, 2014-02-06
… Concentrations of intercellular adhesion molecule (ICAM) -1, E-selectin, L-selectin, and P-selectin in serum samples from all patients were measured by enzyme-linked immunosorbent asssay (ELISA). … Results: At their first visit, serum levels of ICAM-1, E-selection, P-selectin were significantly elevated and serum L-selectin levels were significantly reduced in patients with SSc compared with healthy controls. …
NAID 120005457100

Exacerbation of Intracranial Aneurysm and Aortic Dissection in Hypertensive Rat Treated With the Prostaglandin F–Receptor Antagonist AS604872

Fukuda Miyuki,Aoki Tomohiro,Manabe Toshiaki,Maekawa Akiko,Shirakawa Takayuki,Kataoka Hiroharu,Takagi Yasushi,Miyamoto Susumu,Narumiya Shuh
Journal of Pharmacological Sciences, 2014
… Notably, AS604872 induced expression of pro-inflammatory genes such as E-selectin in lesions and significantly enhanced macrophage infiltration. … Suppression of surface expression of E-selectin with cimetidine prevented macrophage infiltration and aortic dissection. …
NAID 130004700281

Effects of Eicosapentaenoic Acid on Platelet Function in Patients Taking Long-Term Aspirin Following Coronary Stent Implantation

Takada Kaoru,Ishikawa Shuichi,Yokoyama Naoyuki,Hosogoe Naoyoshi,Isshiki Takaaki
International Heart Journal 55(3), 228-233, 2014
… Furthermore, no significant differences were observed in the expression of PAC-1 and CD62P on the platelet surface membranes or in the soluble P-selectin concentration. …
NAID 130004449394

Related Pictures

E-selectin; Antigens, CD62E; CD62E Antigens; E Selectin; Endothelial Leukocyte Selectins and chemokines use shared and distinct signals to activate β2 integrins in The telling tail of L-selectin | Biochemical Society Transactions Sandbox Reserved 716 - Proteopedia, life in 3D Distinct kinetic and mechanical properties govern selectin-leukocyte interactions FIGURES Frontiers | E-Selectin Ligands in the Human Mononuclear Phagocyte System: Implications