| First Author | Raptis SZ | Year | 2005 |
| Journal | Immunity | Volume | 22 |
| Issue | 6 | Pages | 679-91 |
| PubMed ID | 15963783 | Mgi Jnum | J:99112 |
| Mgi Id | MGI:3581120 | Doi | 10.1016/j.immuni.2005.03.015 |
| Citation | Raptis SZ, et al. (2005) Serine protease cathepsin g regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering. Immunity 22(6):679-91 |
| abstractText | The polymorphonuclear leukocyte (PMN)-derived serine proteases play a key role in immune complex (IC)-mediated inflammation. However, the mechanisms by which these proteases regulate inflammatory response remain largely undefined. Here, we show that IC-activated cathepsin G- and neutrophil elastase-deficient (CG/NE) PMNs adhered normally to IC-coated surfaces but did not undergo CD11b clustering and failed to initiate cytoskeletal reorganization and cell spreading. As a result, CG/NE-deficient PMNs exhibited severe defects in MIP-2 secretion and reactive oxygen intermediates production. Exogenously added CG, but not proteolytically inactive CG, was sufficient to restore these defects. These findings identify an important role for CG in integrin-dependent PMN effector functions that are separate from and downstream of integrin-dependent adhesion. |
