Polarization and interaction of adhesion molecules P-selectin glycoprotein ligand 1 and intercellular adhesion molecule 3 with moesin and ezrin in myeloid cells

José L. Alonso-Lebrero, Juan M. Serrador, Carmen Dominguez-Jiménez, Olga Barreiro, Alfonso Luque, Miguel A. Del Pozo, Karen Snapp, Geoffrey Kansas, Reinhard Schwartz-Albiez, Heinz Furthmayr, Francisco Lozano, Francisco Sánchez-Madrid*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

91 Scopus citations

Abstract

In response to the chemoattractants interleukin 8, C5a, N-formyl- methionyl-leucylphenylalanine, and interleukin 15, adhesion molecules P- selectin glycoprotein ligand 1 (PSGL-1), intercellular adhesion molecule 3 (ICAM-3), CD43, and CD44 are redistributed to a newly formed uropod in human neutrophils. The adhesion molecules PSGL-1 and ICAM-3 were found to colocalize with the cytoskeletal protein moesin in the uropod of stimulated neutrophils. Interaction of PSGL-1 with moesin was shown in HL-60 cell lysates by isolating a complex with glutathione S-transferase fusions of the cytoplasmic domain of PSGL-1. Bands of 78- and 81-kd were identified as moesin and ezrin by Western blot analysis. ICAM-3 and moesin also coeluted from neutrophil lysates with an anti-ICAM-3 immunoaffinity assay. Direct interaction of the cytoplasmic domains of ICAM-3 and PSGL-1 with the amino- terminal domain of recombinant moesin was demonstrated by protein-protein binding assays. These results suggest that the redistribution of PSGL-1 and its association with intracellular molecules, including the ezrin-radixin- moesin actin-binding proteins, regulate functions mediated by PSGL-1 in leukocytes stimulated by chemoattractants. (C) 2000 by The American Society of Hematology.

Original languageEnglish (US)
Pages (from-to)2413-2419
Number of pages7
JournalBlood
Volume95
Issue number7
DOIs
StatePublished - Apr 1 2000

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

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