Abstract:
:Previously, we showed that NO induces thymocyte apoptosis via a caspase-1-dependent mechanism [(1) ]. In the present study, we investigated the role of heme oxygenase, catalase, bax, and p53 in this process. The NO donor, S-nitroso-N-acetyl penicillamine (SNAP), induced DNA fragmentation in thymocytes in a time- and concentration-dependent way. SNAP (100 microM) induced 50--60% apoptosis; higher doses did not increase the rate of apoptosis significantly. SNAP decreased catalase and heme iron (Fe) levels without affecting superoxide dismutase, glutathione, or total Fe stores in thymocytes. SNAP significantly increased the expression of heme oxygenase 1 (HSP-32), p53, and bax but not bcl-2. Treatment with the heme oxygenase inhibitor, tin protoporphyrin IX inhibited SNAP-induced thymocyte apoptosis. Furthermore, thymocytes from p53 null mice were resistant to NO-induced apoptosis. Our data suggest that NO may induce its cytotoxic effects on thymocytes by modulating heme oxygenase and catalase activity as well as up-regulating pro-apoptotic proteins p53 and bax.
journal_name
J Leukoc Bioljournal_title
Journal of leukocyte biologyauthors
Gordon SA,Abou-Jaoude W,Hoffman RA,McCarthy SA,Kim YM,Zhou X,Zhang XR,Simmons RL,Chen Y,Schall L,Ford HRsubject
Has Abstractpub_date
2001-07-01 00:00:00pages
87-95issue
1eissn
0741-5400issn
1938-3673journal_volume
70pub_type
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