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Leukocyte Trafficking Mediated by Selectin-Carbohydrate Interactions

McEver, Rodger P., Moore, Kevin L., Cummings, Richard D.·1995·Journal of Biological Chemistry
DOI 10.1074/jbc.270.19.11025
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FIG. 1 Selectins and their glycoprotein ligands. The domain organizations of the three human selectins are shown. Their estimated lengths are based on hydrodynamic data and electron microscopy (8-10). The lengths of GlyCAM-1, CD34, MAdCAM-1, and PSGL-1 are modeled from the dimensions of another mucin-like protein, CD43 (87). The length of ESL-1 is unknown. The membrane-proximal domain of CD34 has been tentatively assigned to the Ig superfamily. GlyCAM-1 is secreted rather than attached to the membrane. PSGL-1 has been studied in humans; the other glycoprotein ligands have been studied in mice. References are as follows: P-selectin (88), E-selectin (89), L-selectin (90), GlyCAM-1 (39, 45), CD34 (39, 46), MAdCAM-1 (69, 70), and PSGL-1 (9, 36, 40, 48). Not illustrated are three less well characterized glycoproteins: a 260-kDa ligand for E-selectin (38), a 160-kDa ligand for P-selectin (52), and a 200-kDa ligand for L-selectin (91).
FIG. 1 Selectins and their glycoprotein ligands. The domain organizations of the three human selectins are shown. Their estimated lengths are based on hydrodynamic data and electron microscopy (8-10). The lengths of GlyCAM-1, CD34, MAdCAM-1, and PSGL-1 are modeled from the dimensions of another mucin-like protein, CD43 (87). The length of ESL-1 is unknown. The membrane-proximal domain of CD34 has been tentatively assigned to the Ig superfamily. GlyCAM-1 is secreted rather than attached to the membrane. PSGL-1 has been studied in humans; the other glycoprotein ligands have been studied in mice. References are as follows: P-selectin (88), E-selectin (89), L-selectin (90), GlyCAM-1 (39, 45), CD34 (39, 46), MAdCAM-1 (69, 70), and PSGL-1 (9, 36, 40, 48). Not illustrated are three less well characterized glycoproteins: a 260-kDa ligand for E-selectin (38), a 160-kDa ligand for P-selectin (52), and a 200-kDa ligand for L-selectin (91).CC-BY · From the PDF
FIG. 2 sLe* tetrasaccharide containing a sulfate moiety at the C-6 position of the galactosyl residue. The conformation of the oligosaccharide is derived from Refs. 44, 92, and 93.
FIG. 2 sLe* tetrasaccharide containing a sulfate moiety at the C-6 position of the galactosyl residue. The conformation of the oligosaccharide is derived from Refs. 44, 92, and 93.CC-BY · From the PDF
FIG. 3 Interactions of PSGL-1 with P-selectin mediate attachment and rolling of neutrophils under flow. Rapid contacts between the two molecules should be favored by the projection of their binding domains above the glycocalyx and by the clustering of PSGL-1 on the tips of microvilli. It has not been determined whether other identified glycoprotein ligands participate in selectin-mediated attachment and rolling of leukocytes under shear stress.
FIG. 3 Interactions of PSGL-1 with P-selectin mediate attachment and rolling of neutrophils under flow. Rapid contacts between the two molecules should be favored by the projection of their binding domains above the glycocalyx and by the clustering of PSGL-1 on the tips of microvilli. It has not been determined whether other identified glycoprotein ligands participate in selectin-mediated attachment and rolling of leukocytes under shear stress.CC-BY · From the PDF

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Metadata

Authors
McEver, R. P., Moore, K. L., & Cummings, R. D.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1995-05
Volume
270
Issue
19
Pages
11025-11028
ISSN
0021-9258
DOI
10.1074/jbc.270.19.11025
Cited by
512
References
1
Language
en
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