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Vol. 300, Issue 2, 367-375, February 2002
10 Years Later
Department of Experimental and Clinical Pharmacology and
Toxicology, Friedrich Alexander University Erlangen-Nürnberg,
Erlangen, Germany
The enzyme cyclooxygenase (COX) catalyzes the first step of the
synthesis of prostanoids. In the early 1990s, COX was demonstrated to
exist as two distinct isoforms. COX-1 is constitutively expressed as a
"housekeeping" enzyme in most tissues. By contrast, COX-2 can be
up-regulated by various pro-inflammatory agents, including lipopolysaccharide, cytokines, and growth factors. Whereas many of the
side effects of nonsteroidal anti-inflammatory drugs (NSAIDs) (e.g.,
gastrointestinal ulceration and bleeding, platelet dysfunctions) are
caused by a suppression of COX-1 activity, inhibition of COX-2-derived prostanoids facilitates the anti-inflammatory, analgesic, and antipyretic effects of NSAIDs. During the past few years specific inhibitors of the COX-2 enzyme have emerged as important
pharmacological tools for treatment of pain and arthritis. However,
although COX-2 was initially regarded as a source of pathological
prostanoids only, recent studies have indicated that this isoenzyme
mediates a variety of physiological responses within the organism. The present review assesses recent advances in COX-2 research, with particular emphasis on new insights into pathophysiological and physiological functions of this isoenzyme.
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