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Mac-1 (CD11b/CD18) as accessory molecule for Fc alpha R (CD89) binding of IgA.
- Source :
-
Journal of immunology (Baltimore, Md. : 1950) [J Immunol] 2002 Oct 01; Vol. 169 (7), pp. 3831-6. - Publication Year :
- 2002
-
Abstract
- 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.
- Subjects :
- Animals
Humans
Lectins metabolism
Macrophage-1 Antigen genetics
Macrophage-1 Antigen physiology
Mice
Mice, Inbred C57BL
Mice, Knockout
Mice, Transgenic
Neutrophils immunology
Neutrophils metabolism
Protein Structure, Tertiary
Respiratory Burst immunology
Secretory Component metabolism
Antigens, CD metabolism
Binding Sites, Antibody genetics
CD11b Antigen metabolism
CD18 Antigens metabolism
Immunoglobulin A metabolism
Macrophage-1 Antigen metabolism
Receptors, Fc metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0022-1767
- Volume :
- 169
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Journal of immunology (Baltimore, Md. : 1950)
- Publication Type :
- Academic Journal
- Accession number :
- 12244179
- Full Text :
- https://doi.org/10.4049/jimmunol.169.7.3831