Possible formation of a nonuniform superconducting state in the heavy-fermion compound UPd2Al3.
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Biomedical subjects
Publications and source records attributed to T Komatsubara.
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The protein mass of group II phospholipase A2 (PLA2) levels were immunochemically measured in sera of 43 patients with Crohn's disease (CD), 43 patients with ulcerative colitis (UC), and 35 healthy volunteers, and compared with PLA2 enzymatic activity. Serum immunoreactive group II PLA2 (IR-PLA2 II) levels of active CD patients were significantly higher than those of the controls and inactive CD patients. Serum IR-PLA2 II levels were also significantly greater in patients with severe UC and moderate UC than in the controls and patients with mild UC. Serum IR-PLA2 II levels were found to be closely correlated with serum PLA2 activity in patients with CD and UC. Serum IR-PLA2 II levels and PLA2 activity decreased by antiinflammatory treatment in six patients with CD and two with UC. These results suggest that serum IR-PLA2 II levels can be a useful parameter in the evaluation of disease activity of CD and UC, and that elevated PLA2 enzymatic activity in sera of patients with CD and UC is attributable to increased protein concentration of group II PLA2, in agreement with our previous results.
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Previously, we reported the presence of group II-like phospholipase A2 activity in the soluble fraction of rat gingiva. In the present study, we found that treatment of rat gingival cells with human recombinant interleukin-1 beta resulted in dose-dependent stimulation of intracellular and extracellular phospholipase A2 activity. Antisera against group II phospholipase A2 totally blocked the interleukin-1 beta-induced phospholipase A2 activity, but antisera against group I phospholipase A2 did not. Moreover, immunoblot analysis showed that the induced phospholipase A2 was group II phospholipase A2. These findings suggest that the induced enzyme belongs to the group II phospholipase A2 family of proinflammatory enzymes.
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