alphadbeta2 integrin is expressed on human eosinophils and functions as an alternative ligand for vascular cell adhesion molecule 1 (VCAM-1). J Exp Med 1998 Dec 07;188(11):2187-91
Date
12/08/1998Pubmed ID
9841932Pubmed Central ID
PMC2212388DOI
10.1084/jem.188.11.2187Scopus ID
2-s2.0-0032494851 (requires institutional sign-in at Scopus site) 117 CitationsAbstract
The beta2 family of integrins, CD11a, CD11b, CD11c, and alphad, are expressed on most leukocytes. We show that the newest member of this family, alphad, is expressed on human eosinophils in peripheral blood, and surface expression can be upregulated within minutes by phorbol ester or calcium ionophore A23187. Culture of eosinophils with interleukin 5 (IL-5) leads to a two- to fourfold increase in alphad levels by 3-7 d without a change in alpha4 integrin expression. Eosinophils isolated from late phase bronchoalveolar lavage fluids express alphad at levels similar to that seen after 3 d of IL-5 culture. Regarding alphadbeta2 ligands, in both freshly isolated and IL-5-cultured eosinophils, as well as alphadbeta2-transfected Chinese hamster ovary cells, alphadbeta2 can function as a ligand for vascular cell adhesion molecule 1 (VCAM-1). This conclusion is based on the ability of monoclonal antibodies to alphad, beta2, or VCAM-1 to block cell attachment in static adhesion assays. In experiments with eosinophils, the relative contribution of alphadbeta2 integrin- mediated adhesion is enhanced after IL-5 culture. These experiments demonstrate that alphadbeta2 is an alternative ligand for VCAM-1, and this integrin may play a role in eosinophil adhesion to VCAM-1 in states of chronic inflammation.
Author List
Grayson MH, Van der Vieren M, Sterbinsky SA, Michael Gallatin W, Hoffman PA, Staunton DE, Bochner BSMESH terms used to index this publication - Major topics in bold
AnimalsCD11 Antigens
Cell Adhesion
Cricetinae
Eosinophils
Humans
Integrin alpha Chains
Integrins
Ligands
Receptors, Cytoadhesin
Vascular Cell Adhesion Molecule-1
