| First Author | Thom SR | Year | 2008 |
| Journal | J Biol Chem | Volume | 283 |
| Issue | 16 | Pages | 10822-34 |
| PubMed ID | 18283105 | Mgi Jnum | J:136546 |
| Mgi Id | MGI:3796471 | Doi | 10.1074/jbc.M709200200 |
| Citation | Thom SR, et al. (2008) Actin S-nitrosylation inhibits neutrophil beta2 integrin function. J Biol Chem 283(16):10822-34 |
| abstractText | The focus of this work was to elucidate the mechanism for inhibition of neutrophil beta(2) integrin adhesion molecules by hyperoxia. Results demonstrate that exposure to high oxygen partial pressures increases synthesis of reactive species derived from type 2 nitric-oxide synthase and myeloperoxidase, leading to excessive S-nitrosylation of beta-actin and possibly profilin. Hyperoxia causes S-nitrosylation of the four cysteine moieties closest to the carboxyl-terminal end of actin, which results in formation of short actin filaments. This alters actin polymerization, network formation, and intracellular distribution, as well as inhibits beta(2) integrin clustering. If neutrophils are exposed to ultraviolet light to reverse S-nitrosylation, or are incubated with N-formyl-methionyl-leucine-phenylalanine to trigger 'inside-out' activation, the effects of hyperoxia are reversed. We conclude that cytoskeletal changes triggered by hyperoxia inhibit beta(2) integrin-dependent neutrophil adhesion. |
