XXXX -like temperatures affect neutrophil @entity1991 signaling, apoptosis, and ANCA-antigen expression.

@entity2304 @entity558 @entity1991 @entity1333 @entity3806 @entity1995 @entity19 @entity1457 @entity619 @entity1994 @entity1993 @entity221 @entity4357
The neutrophil is pivotal to ANCA @entity1333 pathogenesis. @entity221 frequently complicates ANCA diseases. This study investigated the effects of short-term heat exposure on apoptosis in neutrophils that were treated with @entity558 , @entity2304 , @entity3806 , and @entity619 . All compounds delayed apoptosis. Heat abrogated the apoptosis-delaying effect of @entity558 without affecting constitutive apoptosis or delayed apoptosis by @entity2304 , @entity3806 , or @entity619 . The heat effect was dose dependent over the 39 to 42 degrees C range. @entity1991 but not extracellular signal-regulated kinase, @entity1995 mitogen-activated protein kinase (MAPK), or @entity4357 3-kinase/ @entity1994 controlled @entity558 -delayed apoptosis. Furthermore, @entity558 -induced @entity1993 degradation, DNA binding, and @entity1991 -dependent gene transcription activation were abrogated by short-term heat. When core temperatures were raised to 40.5 degrees C for 30 min in @entity19 , @entity558 -induced neutrophil @entity1991 activation also was prevented. Short-term heat removed @entity1457 protein 90 from the IkappaB kinase complex, resulting in failure of @entity558 -induced IkappaB kinase activation. Despite delayed apoptosis, ANCA antigen expression was increased in @entity558 -treated neutrophils. ANCA antigen increase was prevented by @entity1995 inhibition and by heat exposure. Heat exposure did not inhibit @entity558 -induced @entity1995 MAPK phosphorylation. Instead, apoptosis-mediated @entity1995 degradation was accelerated, thereby decreasing the @entity1995 that was available for @entity558 -mediated ANCA antigen upregulation. These data suggest that @entity221 -like temperatures modulate neutrophil behavior in this disease.
