Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Similarities in morphology between copper-deficient cartilage and abnormal cartilage associated with tibial dyschondroplasis (TD) led to studies dealing with copper metabolism and its possible relation to TD. Abnormal cartilage and copper deficient cartilage cells both oxidize significantly less glucose to CO2 and water when compared to normal epiphyseal and day-old hypertrophic cartilage cells. Plasma ceruloplasmin levels and cartilage copper content were not different between normal birds and those affected wth TD, which seemed to rule out a genetic defect in copper metabolism as being partly responsible for the abnormal cartilage occurrence. Mitochondrial marker enzyme activities were investigated, and abnormal cartilage showed a significant decrease in activity of both cytochrome oxidase and citrate synthase. The yield of mitochondria on a percent of total activity basis was quite low from both normal and abnormal cartilages, and, thus, an absolute conclusion with regard to mitochondrial impairment cannot be made at this time.
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PMID:Metabolism of abnormal cartilage cells associated with tibial dyschondroplasia. 741 92

Oviparously developing embryos of the crustacean Artemia franciscana encyst and enter diapause, exhibiting a level of stress tolerance seldom seen in metazoans. The extraordinary stress resistance of encysted Artemia embryos is thought to depend in part on the regulated synthesis of artemin, a ferritin superfamily member. The objective of this study was to better understand artemin function, and to this end the protein was synthesized in Escherichia coli and purified to apparent homogeneity. Purified artemin consisted of oligomers approximately 700 kDa in molecular mass that dissociated into monomers and a small number of dimers upon SDS/PAGE. Artemin inhibited heat-induced aggregation of citrate synthase in vitro, an activity characteristic of molecular chaperones and shown here to be shared by apoferritin and ferritin. This is the first report that apoferritin/ferritin may protect cells from stress other than by iron sequestration. Stably transfected mammalian cells synthesizing artemin were more resistant to heat and H(2)O(2) than were cells transfected with vector only, actions also shared by molecular chaperones such as the small heat shock proteins. The data indicate that artemin is a structurally modified ferritin arising either from a common ancestor gene or by duplication of the ferritin gene. Divergence, including acquisition of a C-terminal peptide extension and ferroxidase center modification, eliminated iron sequestration, but chaperone activity was retained. Therefore, because artemin accumulates abundantly during development, it has the potential to protect embryos from stress during encystment and diapause without adversely affecting iron metabolism.
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PMID:Functional characterization of artemin, a ferritin homolog synthesized in Artemia embryos during encystment and diapause. 1725 68