Selectins: A family of adhesion receptors

Bevilacqua, Michael P.; Butcher, Eugene C.; Furie, Barbara C.; Furie, Bruce; Gallatin, Michael; Gimbrone, Michael A.; Harlan, John M.; Kishimoto, Karen M.; Lasky, Laurence A.; McEver, Rodger P.; Paulson, James C.; Rosen, Steven D.; Seed, Brian; Siegelman, Mark H.; Springer, T.; Stoolman, Lloyd M.; Tedder, Thomas F.; Varki, Ajit; Wagner, Denisa D.; Weissman, Irving L.; Zimmerman, Guy A.

doi:10.1016/0092-8674(91)90174-w

Cited by 341 publications

(136 citation statements)

References 2 publications

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“…Therefore, although the requirement for hydroxyl-groups of the mannose-or galactose-type within the binding-site on the carbohydrate molecules is determined by the E-N/Q-D pair of residues, other differences seen in the sequences of the lectin domains, and of the extensive loop carrying the binding sites in particular, seem to be also involved in ligand selection in the in vivo interaction of C-type lectins with complex carbohydrate structures. Domains identified by sequence comparison and predicted to have an overall folding similar to that seen in the crystal structure of the C-type lectin domain of MBP (Weis et al, 1991b), but lacking some of the characteristic residues involved in calcium/carbohydrate binding, are seen in a number of type I1 membrane proteins ( QPD-E-WND gal Tanaka et al, 1988 QPD-E-WND gal Zimmerman & Ruoslahti, 1989 QPD-E-WND gal Drickamer, 1981Spiess & Lodish, 1985Drickamer et al, 1984Ii et al, 1990Hoyle & Hill, 1991Sat0 et al, 1992Curtis et al, 1992Suter et al, 1987Yokoyama et al, 1989Chan & Takei, 1989Giorda et al, 1990Van Hoegen et al, 1990Houchins et al, 1991Wong et al, 1991Yoshimatsu et al, 1992Lee et al, 1991Taylor et al, 1989Drickamer et al, 1986White et al, 1985Benson et al, 1985Rust et al, 1991Holmskov et al, 1993bHolmskov et al, 1993aLasky et al, 1989Bevilacqua et al, 1991Johnson et al, 1989Christa et al, 1994Ng & Hew, 1992Ewart et al, 1992Rouquier et al, 1991Taylor et al, 1990 EPN-E-WND man (Drickamer, 1992). Not all of the carbohydrate specificities have been determined (*), and certain proteins, although a Proteins containing C-type lectin domains or regions w...…”

Section: The Iectin Domainmentioning

confidence: 99%

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

1994

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The collectins are a group of mammalian lectins containing collagen-like regions. They include mannan binding protein, bovine conglutinin, lung surfactant protein A, lung surfactant protein D, and a newly discovered bovine protein named collectin-43. These proteins share a very similar modular domain composition and overall 3-dimensional structure. They also appear to play similar biological roles in the preimmune defense against microorganisms in both serum and lung surfactant. The close evolutionary relationship between the collectins is further emphasized by a common pattern of exons in their genomic structures and the presence of a gene cluster on chromosome 10 in humans that contains the genes known for the human collectins. Studies on the structure/function relationships within the collectins could provide insight into the properties of a growing number of proteins also containing collagenous regions such as Clq, the hibernation protein, the a-and 0-ficolins, as well as the membrane acetylcholinesterase and the macrophage scavenger receptor.

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Section: The Iectin Domainmentioning

confidence: 99%

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

1994

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“…Selectins are involved in extravasation of leukocytes in that they bind leukocytes to endothelial cells [8]. CD34 is expressed on endothelial cells and may therefore play a role as ligand for L-selectin (CD62L) in stem cell adhesion to BM stroma [2].…”

Section: Selectinsmentioning

confidence: 99%

Difference between Expression of Adhesion Molecules on CD34 ⁺ Cells from Bone Marrow and G‐CSF‐Stimulated Peripheral Blood

Kröger¹,

Zeller²,

Hassan³

et al. 1998

STEM CELLS

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c-kit, CD58, CD62L and CD49d were less expressed on CD34 + cells of PBSC than of BM, the difference being statistically significant for CD49d (p < 0.05). CD49e and CD37 were expressed more in PBSC than BM without being statistically significant. The mean fluorescence intensity for all adhesion molecules on CD34 + cells did not differ significantly between PBSC and BM. The significantly lower expression of CD49d on G-CSF-mobilized PBSCs might suggest that downregulation of this molecule may be involved in the process of peripheral stem cell mobilization.

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“…For example, experimental autoimmune animal models are suppressed by treatment with anti-intercellular adhesion molecule (ICAM) antibody (2-A). Recently, adhesion molecules with lectin domain have been shownto be localized in the vascular system and termed the selectin family (5). The family comprises three selectins: E-, L-, and P-selectin.…”

Section: Introductionmentioning

confidence: 99%

Expression of Selectin Families and Their Ligand Sialyl Lewis X in the Muscles of Inflammatory Myopathies. An Immunohistochemical Study.

et al. 1999

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Object Adhesion molecules are suggested to play important roles in the pathogenesis of inflammatory diseases. Weexamined the expression of adhesion molecules in the muscles of human inflammatory myopathies. Methods Weimmunohistochemically studied the expression and distribution of two molecules in the selectin family (E-and P-selectin) and their commonligand sialyl Lewis X in 18 inflammatory myopathies, 13 disease controls, and 16 normal controls. Results In inflammatory myopathies, E-and P-selectin were upregulated on the surface of blood vessels, especially on the endothelial cells of the venules. Sialyl Lewis X was upregulated in the blood vessels, infiltrating leukocytes, and the surface of some atrophic myofibers. Somecontrol muscles also showed weakly positive staining with these molecules, however, expression of these molecules was most striking in the muscles of inflammatory myopathies. Conclusion The results suggested that these molecules are upregulated in inflammatory myopathies and might play a role in the pathogenesis of inflammatory myopathies. (Internal Medicine 38: 632-635, 1999)

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Selectins: A family of adhesion receptors

Cited by 341 publications

References 2 publications

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

Difference between Expression of Adhesion Molecules on CD34 ⁺ Cells from Bone Marrow and G‐CSF‐Stimulated Peripheral Blood

Expression of Selectin Families and Their Ligand Sialyl Lewis X in the Muscles of Inflammatory Myopathies. An Immunohistochemical Study.

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Selectins: A family of adhesion receptors

Cited by 341 publications

References 2 publications

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

Difference between Expression of Adhesion Molecules on CD34 + Cells from Bone Marrow and G‐CSF‐Stimulated Peripheral Blood

Expression of Selectin Families and Their Ligand Sialyl Lewis X in the Muscles of Inflammatory Myopathies. An Immunohistochemical Study.

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Difference between Expression of Adhesion Molecules on CD34 ⁺ Cells from Bone Marrow and G‐CSF‐Stimulated Peripheral Blood