LFA-1-mediated leukocyte adhesion regulated by interaction of CD43 with LFA-1 and CD147

Khunkaewla, Panida; Schiller, Herbert B.; Paster, Wolfgang; Leksa, Vladimı́r; Cermak, Laird S.; Anděra, Ladislav; Hořejšı́, Václav; Stockinger, Hannes

doi:10.1016/j.molimm.2007.09.032

Cited by 31 publications

(25 citation statements)

References 41 publications

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“…Previous studies have defined a number of cell surface molecules that are associated with cell aggregation. The antigens LFA-1, CD43 and CD98 appear to participate in cell aggregation in different cell lines, and interestingly, further studies have shown that these molecules may also interact with CD147 (Cho et al, 2001;Khunkaewla et al, 2008). Based on these findings, we further tested the surface expression of these three molecules using flow cytometric analysis after knocking down of CD147 in Jurkat T cells.…”

Section: Discussionmentioning

confidence: 94%

CD147 and CD98 complex-mediated homotypic aggregation attenuates the CypA-induced chemotactic effect on Jurkat T cells

Guo

Zhang

et al. 2015

Molecular Immunology

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Section: Discussionmentioning

confidence: 94%

CD147 and CD98 complex-mediated homotypic aggregation attenuates the CypA-induced chemotactic effect on Jurkat T cells

Guo

Zhang

et al. 2015

Molecular Immunology

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“…This technique is very robust and avoids some of the run variation and derivitization artifacts seen in other proteomic techniques. Phosphopeptides whose ratios varied in a CR3-dependent and s␤glu-mediated way include previously reported integrin-associated proteins, such as Vimentin, phosphatidylinositol 3-dependent protein kinase-1, STAT5B, Rho GTPase-activating protein 12, keritins 8 and 18, N-myc downstream regulated gene family member 3, scaffold attachment factor B-like transcription modulator, myosin heavy chain 10, sialophorin, and components of EGF signaling (42)(43)(44)(45)(46)(47)(48). Also represented were peptides known to be involved in the cellular response to other PAMPs, including ERK2 and TRAF (TNF receptor-associated factor)-type zinc finger domain-containing protein 1, the former of which was confirmed by Western blot analysis (26, 30) (supplemental Fig.…”

Section: Discussionmentioning

confidence: 96%

Lectin Site Ligation of CR3 Induces Conformational Changes and Signaling

O’Brien

Heflin

Lavigne

et al. 2012

Journal of Biological Chemistry

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Background: CR3 is a ␤ 2 integrin that contains a lectin-like domain that binds the fungal pathogen-associated molecular pattern ␤-glucan. Results: Soluble ␤-glucan stabilizes an intermediate CR3 conformation that induces differential intracellular phosphorylation. Conclusion: CR3 is a signaling pattern recognition receptor for ␤-glucan. Significance: The CR3 receptor is a target for the design of novel immune modulators.

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“…In addition to PSGL-1 and CD44, CD43 is known to function as an E-selectin ligand. 32 However, there was no difference of CD43 expression between Bsg ϩ/ϩ and Bsg Ϫ/Ϫ neutrophils (Supplementary Figure S2A). Furthermore, the beads used for Figure 4C did not contain PSGL-1, CD44, or CD43 (Supple- BASIC RESEARCH www.jasn.org mentary Figure S2B).…”

Section: Expression Of Other Adhesion-related Molecules In Bsg-deficimentioning

confidence: 92%

The E-Selectin Ligand Basigin/CD147 Is Responsible for Neutrophil Recruitment in Renal Ischemia/Reperfusion

Kato¹,

Yuzawa²,

Kosugi³

et al. 2009

Journal of the American Society of Nephrology

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E-selectin and its ligands are essential for extravasation of leukocytes in inflammation. Here, we report that basigin (Bsg)/CD147 is a ligand for E-selectin that promotes renal inflammation in ischemia/ reperfusion. The selectins and their ligands are essential for leukocyte tethering/rolling on endothelial cells and the initiation of inflammatory response. The selectins are C-type lectins and consist of three members, i.e., P-, L-, and E-selectin. 1,2 P-selectin is expressed upon inflammatory stimulation in platelets and endothelial cells. L-selectin is constitutively expressed on the tip of leukocyte microvilli and implicated in lymphocyte homing to lymph nodes. 3 E-selectin is specifically induced in the endothelium upon inflammatory stimulation. Thus, E-and P-selectin closely collaborate with one another and play a major role in leukocyte recruitment to inflammatory sites. 4 -6 Among the several glycoproteins reported to bind to E-selectin, three have been identified as representative physiologic E-selectin ligands on neutrophils. There are P-selectin glycoprotein ligand-1 (PSGL-1), E-selectin ligand-1, and CD44, and all three play distinct roles during tethering and slow rolling of neutrophils on the endothelium. 7 A minimal recognition motif for all selectins is sialylated and fucosylated glycan determinants, such as sialyl Lewis X, that decorate the terminal extensions of carbohydrates of these molecules. 8,9 However, because of the poor immunogenicity of highly gly-

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LFA-1-mediated leukocyte adhesion regulated by interaction of CD43 with LFA-1 and CD147

Cited by 31 publications

References 41 publications

CD147 and CD98 complex-mediated homotypic aggregation attenuates the CypA-induced chemotactic effect on Jurkat T cells

CD147 and CD98 complex-mediated homotypic aggregation attenuates the CypA-induced chemotactic effect on Jurkat T cells

Lectin Site Ligation of CR3 Induces Conformational Changes and Signaling

The E-Selectin Ligand Basigin/CD147 Is Responsible for Neutrophil Recruitment in Renal Ischemia/Reperfusion

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