Mac-1 (CD11b/CD18) as Accessory Molecule for FcαR (CD89) Binding of IgA | Zendy

Annemiek B. van Spriel | Zendy; Jeanette H.W. Leusen | Zendy; Henriette A. Vilé | Zendy; Jan G. J. van de Winkel | Zendy

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Mac-1 (CD11b/CD18) as Accessory Molecule for FcαR (CD89) Binding of IgA

Author(s) -

Annemiek B. van Spriel,

Jeanette H.W. Leusen,

Henriette A. Vilé,

Jan G. J. van de Winkel

Publication year - 2002

Publication title -

the journal of immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.737

H-Index - 372

eISSN - 1550-6606

pISSN - 0022-1767

DOI - 10.4049/jimmunol.169.7.3831

Subject(s) - secretory component , j chain , integrin alpha m , chemistry , secretory iga , receptor , immunology , microbiology and biotechnology , antibody , biology , biochemistry

IgA, the principal ligand for FcalphaRI, exists in serum as monomeric IgA and at mucosal sites as secretory IgA (SIgA). SIgA consists of dimeric IgA linked by joining chain and secretory components. Human polymorphonuclear leukocytes (PMN) and mouse PMN transgenic for human FcalphaRI exhibited spreading and elicited respiratory burst activity upon interaction with either serum or SIgA. However, PMN devoid of the beta(2) integrin Mac-1 (Mac-1(-/-)) were unable to bind SIgA, despite expression of FcalphaRI. Consistent with this, serum IgA stimulated Mac-1(-/-) PMN oxygen radical production, in contrast to SIgA. Binding studies showed the secretory component, by itself, to interact with Mac-1-expressing PMN, but not with Mac-1(-/-) PMN. These data demonstrate an essential role for Mac-1 in establishing SIgA-FcalphaRI interactions.

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