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pubmed-article:3014830pubmed:abstractTextArticular cartilage contains any ectoenzyme activity, NTP-PPH, which is capable of generating PPi from NTP substrates. The PPi generated is from the cleavage of the alpha-beta pyrophosphate bond of NTP and does not result from the effects of NTP catabolites. NTP-PPH activity is expressed on human skin fibroblasts in culture and is significantly increased in subjects with CPPD deposition. In addition, cultured fibroblasts from subjects with CPPD disease have higher intracellular PPi concentrations compared to cells from normals and patients with OA. These results support the hypothesis that alterations in PPi metabolism provide the metabolic basis for CPPD deposition.lld:pubmed
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pubmed-article:3014830pubmed:authorpubmed-author:RyanL MLMlld:pubmed
pubmed-article:3014830pubmed:authorpubmed-author:WortmannR LRLlld:pubmed
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pubmed-article:3014830pubmed:pagination153-6lld:pubmed
pubmed-article:3014830pubmed:dateRevised2004-11-17lld:pubmed
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pubmed-article:3014830pubmed:year1986lld:pubmed
pubmed-article:3014830pubmed:articleTitleEcto-nucleoside triphosphate pyrophosphohydrolase activity and calcium pyrophosphate dihydrate crystal deposition disease.lld:pubmed
pubmed-article:3014830pubmed:publicationTypeJournal Articlelld:pubmed