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Blood, Vol. 95 No. 7 (April 1), 2000:
pp. 2413-2419
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 Domínguez-Jiménez,
Olga Barreiro,
Alfonso Luque,
Miguel A. del Pozo,
Karen Snapp,
Geoffrey Kansas,
Reinhard Schwartz-Albiez,
Heinz Furthmayr,
Francisco Lozano, and
Francisco Sánchez-Madrid
From the Servicio de Inmunología, Hospital de la Princesa,
Madrid, Spain; Northwestern University Medical School, Chicago, IL;
Molecular Mechanisms of Disease Laboratories, Department of Pathology,
Stanford University Medical Center, Stanford, CA; Tumor Immunology
Program, German Cancer Research Center, Heidelberg, Germany; and Servei
d'Immunologia, Hospital Clinic, Barcelona, Spain.
In response to the chemoattractants interleukin 8, C5a,
N-formyl-methionyl-leucyl-phenylalanine, 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.
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