Biochem Biophys Res Commun 1996,
PMID: 8912630
Sekine, C; Yagita, H; Kobata, T; Hasunuma, T; Nishioka, K; Okumura, K
In this study, we investigated the IL-1 beta converting enzyme (ICE) family cysteine proteases responsible for the Fas-mediated apoptosis of rheumatoid arthritis (RA) synoviocytes and their involvement in proinflammatory cytokine production. CPP32 inhibitor, but not ICE inhibitor, was capable of inhibiting the Fas-mediated apoptosis of RA synovial cells. CPP32, but not ICE, was activated in response to anti-Fas stimulation. IL-8, but not IL-1 beta, was secreted from the anti-Fas-stimulated RA synoviocytes even in the presence of CPP32 inhibitor. These results demonstrated that CPP32, but not ICE, is the predominant cysteine protease that mediates the Fas-mediated apoptosis of RA synovial cells. We also demonstrated that anti-Fas stimulation of RA synoviocytes leads to IL-8 secretion independently of the CPP32-mediated apoptosis, which would accelerate inflammation.
Diseases/Pathways annotated by Medline MESH: Arthritis, Rheumatoid
Document information provided by NCBI PubMed
Text Mining Data
IL-8 → Fas: "
Fas mediated stimulation
induces IL-8 secretion by rheumatoid arthritis synoviocytes independently of CPP32 mediated apoptosis
"
ICE → anti-Fas: "
CPP32, but not ICE , was activated in response to anti-Fas stimulation
"
CPP32 → anti-Fas: "
CPP32 , but not ICE, was activated in response to anti-Fas stimulation
"
IL-1 beta ⊣ CPP32: "
IL-8, but not IL-1 beta , was secreted from the anti-Fas stimulated RA synoviocytes even in the presence of CPP32 inhibitor
"
IL-8 ⊣ CPP32: "
IL-8 , but not IL-1 beta, was secreted from the anti-Fas stimulated RA synoviocytes even in the presence of CPP32 inhibitor
"
Manually curated Databases
No curated data.