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Neutrophil Adhesion to Periostin is Mediated by Integrins
Author(s) -
Reaves Titus A.,
Liu Yuan,
Norris Russell,
Borg Thomas,
Lebel David P.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.570.10
Subject(s) - periostin , cell adhesion molecule , integrin , chemistry , microbiology and biotechnology , extracellular matrix , integrin alpha m , matricellular protein , adhesion , cell adhesion , biology , receptor , biochemistry , organic chemistry
Neutrophil (PMN) localization at the lumenal epithelium surface is a key histological feature of the large intestine of inflammatory bowel disease ((IBD), Crohn's Disease and Ulcerative Colitis) patients. Extracellular matrix proteins (ECM) can affect PMN recruitment and other functions. Periostin, an ECM protein secreted by fibroblasts during cellular injury and tissue repair, was investigated as an adhesive molecule for PMN. Immunofluorescence reveals that periostin similarly to the subepithelial fibroblasts is confined to the base of the crypt epithelium. Flow Cytometry and adhesion results show that intestinal fibroblasts and T84 epithelial cells adhere to periostin and express periostin on the cell surface. Anti‐αvβ3 and anti‐αvβ5 (known integrin receptors for periostin) antibodies inhibit periostin adhesion to fibroblasts and T84 cells. In particular, anti‐αvβ3 and anti‐αvβ5 antibodies inhibit 50% of adhesion. However, anti‐CD11b antibodies inhibit 95% of this adhesion. PMN surface expression of periostin is reduced when PMN are exposed to microbial products and anti‐periostin antibodies inhibit PMN adhesion to fibrinogen (a known ligand for CD11b, a precursor to fibrin, and important in the inflammatory response) by 85%. Thus, PMN adhesion to periostin can be modulated by αvβ3, αvβ5 and CD11b integrins and may play a role in PMN‐epithelial interactions in IBD.