The results demonstrate that treatment with NiCl2 or acetazolamide prevents HAPE in rats and are consistent with a role for elevated pulmonary artery pressure in the pathogenesis of HAPE.
In addition to Diels-Alder and hetero-Diels-Alder reactions, tetrafluoro-o-benzoquinone (o-fluoranil) undergoes nucleophilic additions, addition-eliminations, dioxole formation, and charge-transfer complexation, reacting at every site on the molecular skeleton. It also effects dehydrogenations and other oxidations. The quinone can function as a (CF)(4) synthon.
The title quinone undergoes [4 + 2] cycloadditions in two ways, Diels-Alder on the ring and hetero-Diels-Alder by attack at the oxygens. The latter mode of reaction is strongly favored thermodynamically, but there is a kinetic bias favoring the normal Diels-Alder addition that often prevails, especially with cycloaddends that are not electron-rich.
S U M M A R Y Carbonic anhydrase (CA) is ubiquitously expressed and plays a pivotal role in acid-base balance, ion transport, and gas exchange. Limited observations by others, derived from functional, pharmacological, and histochemical studies, suggest that CA is present in vascular smooth muscle and is involved in vasoregulation. The present study, using measurements of bioactivity, inhibition characteristics, and immunohistochemical analysis, was undertaken to more fully evaluate CA in vascular smooth muscle. In isolated bovine aortic smooth muscle, which is devoid of erythrocytes, CA is present in low concentrations with a CO 2 hydration activity (at 0C) of 3.5 Ϯ 2.7 U/g. The I 50 for acetazolamide inhibition is 0.07 Ϯ 0.01 M. Results with dorzolamide and bromopyruvate, selective inhibitors of the CA II and I isozymes, respectively, show that roughly 75% of the CA activity is accounted for by CA I, with 20% due to CA II. These results accord qualitatively with immunocytochemical staining with specific CA I and II antibodies, showing that both isozymes are present and that their staining co-localizes with cells positive for smooth muscle ␣ -actin. These data establish the activity, inhibition, and isozyme pattern of carbonic anhydrase expression in mammalian vascular smooth muscle.
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