Engagement of the monocyte surface antigen CD14 induces lymphocyte function-associated antigen-1/intercellular adhesion molecule-1-dependent homotypic adhesion

Roger P. Lauener, Raif S. Geha, Donata Vercelli

Research output: Contribution to journalArticle

70 Citations (Scopus)

Abstract

Murine anti-CD14 mAb which recognize different CD14 epitopes induced marked homotypic adhesion of normal human monocytes. Induction of aggregation by anti-CD14 mAb required Mg2+, occurred at an optimal temperature of 37°C, but not at 4°C, and exhibited a kinetics which differed from adhesion triggered by IFN-γ and anti-CD43 mAb. Monocyte adhesion induced by anti-CD14 mAb required neither FcγR engagement nor cross-linking of CD14, because adhesion was induced by F(ab)′2 fragments, as well as by monovalent F(ab) fragments of anti-CD14 mAb. mAb to CD11a, CD18, and intercellular adhesion molecule-1 (ICAM-1), but not antibodies to CD11b and CD11c, inhibited monocyte adhesion induced by CD14 engagement. These results indicate that CD14-dependent adhesion is mediated by lymphocyte function-associated Ag-1/ICAM-1 interactions. This was confirmed by the absence of aggregation in anti-CD14-stimulated cells from a patient with leukocyte adhesion deficiency. Monocyte adhesion upon CD14 engagement was blocked by an inhibitor of protein kinases, sphingosine. This suggests that protein kinases play a role in the intracellular signaling pathway(s) which couple CD14 to lymphocyte function-associated Ag-1/ICAM-1.

Original languageEnglish (US)
Pages (from-to)1390-1394
Number of pages5
JournalJournal of Immunology
Volume145
Issue number5
StatePublished - Sep 1 1990
Externally publishedYes

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Lymphocyte Function-Associated Antigen-1
Intercellular Adhesion Molecule-1
Surface Antigens
Monocytes
Lymphocytes
Sphingosine
Protein Kinase Inhibitors
Protein Kinases
Epitopes
Leukocytes
Temperature
Antibodies

ASJC Scopus subject areas

  • Immunology

Cite this

Engagement of the monocyte surface antigen CD14 induces lymphocyte function-associated antigen-1/intercellular adhesion molecule-1-dependent homotypic adhesion. / Lauener, Roger P.; Geha, Raif S.; Vercelli, Donata.

In: Journal of Immunology, Vol. 145, No. 5, 01.09.1990, p. 1390-1394.

Research output: Contribution to journalArticle

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abstract = "Murine anti-CD14 mAb which recognize different CD14 epitopes induced marked homotypic adhesion of normal human monocytes. Induction of aggregation by anti-CD14 mAb required Mg2+, occurred at an optimal temperature of 37°C, but not at 4°C, and exhibited a kinetics which differed from adhesion triggered by IFN-γ and anti-CD43 mAb. Monocyte adhesion induced by anti-CD14 mAb required neither FcγR engagement nor cross-linking of CD14, because adhesion was induced by F(ab)′2 fragments, as well as by monovalent F(ab) fragments of anti-CD14 mAb. mAb to CD11a, CD18, and intercellular adhesion molecule-1 (ICAM-1), but not antibodies to CD11b and CD11c, inhibited monocyte adhesion induced by CD14 engagement. These results indicate that CD14-dependent adhesion is mediated by lymphocyte function-associated Ag-1/ICAM-1 interactions. This was confirmed by the absence of aggregation in anti-CD14-stimulated cells from a patient with leukocyte adhesion deficiency. Monocyte adhesion upon CD14 engagement was blocked by an inhibitor of protein kinases, sphingosine. This suggests that protein kinases play a role in the intracellular signaling pathway(s) which couple CD14 to lymphocyte function-associated Ag-1/ICAM-1.",
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AB - Murine anti-CD14 mAb which recognize different CD14 epitopes induced marked homotypic adhesion of normal human monocytes. Induction of aggregation by anti-CD14 mAb required Mg2+, occurred at an optimal temperature of 37°C, but not at 4°C, and exhibited a kinetics which differed from adhesion triggered by IFN-γ and anti-CD43 mAb. Monocyte adhesion induced by anti-CD14 mAb required neither FcγR engagement nor cross-linking of CD14, because adhesion was induced by F(ab)′2 fragments, as well as by monovalent F(ab) fragments of anti-CD14 mAb. mAb to CD11a, CD18, and intercellular adhesion molecule-1 (ICAM-1), but not antibodies to CD11b and CD11c, inhibited monocyte adhesion induced by CD14 engagement. These results indicate that CD14-dependent adhesion is mediated by lymphocyte function-associated Ag-1/ICAM-1 interactions. This was confirmed by the absence of aggregation in anti-CD14-stimulated cells from a patient with leukocyte adhesion deficiency. Monocyte adhesion upon CD14 engagement was blocked by an inhibitor of protein kinases, sphingosine. This suggests that protein kinases play a role in the intracellular signaling pathway(s) which couple CD14 to lymphocyte function-associated Ag-1/ICAM-1.

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