PMID: 7538822Jun 1, 1995Paper

Regulation of cell adhesion molecule expression and function associated with neutrophil apoptosis.

Blood
Ian DransfieldC Haslett

Abstract

We have investigated the adhesive capacity of neutrophils after spontaneous apoptosis, which occurs during in vitro culture. Apoptotic neutrophils show reduced adhesion to E selectin and the CD18 integrin ligand fibrinogen. Neutrophil apoptosis is associated with changes in the levels of surface expression of key receptors that mediate neutrophil adhesion events. Notably, apoptotic neutrophils show reduced expression of L-selectin/selectin ligand. In contrast, CD11b/CD18 and CD11c/CD18 integrins are expressed at increased levels. The reduced capacity for adhesion of apoptotic neutrophils may be achieved by very different mechanisms. Regulation of the levels of surface expression of receptors/ligand may control selectin-mediated adhesion, possibly as a result of protease/sialidase activity. In contrast, modulation of integrin-mediated adhesion may involve functional uncoupling of receptors present on the surface of the apoptotic cell without alteration in levels of surface expression. The altered adhesive potential of the apoptotic neutrophil may serve to limit release of its histotoxic contents and reduce inappropriate tissue injury.

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Apoptosis

Apoptosis is a specific process that leads to programmed cell death through the activation of an evolutionary conserved intracellular pathway leading to pathognomic cellular changes distinct from cellular necrosis

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Cell adhesion molecules are a subset of cell adhesion proteins located on the cell surface involved in binding with other cells or with the extracellular matrix in the process called cell adhesion. In essence, cell adhesion molecules help cells stick to each other and to their surroundings. Cell adhesion is a crucial component in maintaining tissue structure and function. Discover the latest research on adhesion molecule and their role in health and disease here.

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