Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.3.5.1 (succinate dehydrogenase)
 8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The depletion of proteoglycans (PGs), induced by a single intravenous injection of papain, is a useful model for studying the response of chondrocytes in vivo to injury. The present study concentrated on the activity of enzymes related to the synthesis of PGs, either directly, with uridine diphosphoglucose dehydrogenase (UDPGD), or indirectly, through the general oxidative metabolism of the chondrocytes. Most of the enzymes showed diminished activity on day 2; in some, there was little change in activity, whereas in others there was marked increase in activity over the following days. Thus, on day 9 the activities of glucose-6-phosphate dehydrogenase and of glyceraldehyde-3-phosphate dehydrogenase were twice the original (day 0) values, and those of succinate dehydrogenase and of UDPGD were one and a half times greater than the original activities. Such increased enzymatic activity preceded the increase in PG content, which by day 14 reached up to 80% of the initial value. Both the increased activity and the replenishment of the PG content were inhibited when hydrocortisone (10 mg/kg) was injected.
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PMID:Altered chondrocytic oxidative metabolism during the restoration of depleted intercellular matrix. 237 15

We have previously found that the restoration of cartilage matrical proteoglycans is preceded by markedly increased activity of uridine diphosphoglucose dehydrogenase (UDPGD), an enzyme directly associated with glycosaminoglycan (GAG) synthesis, and by increased activity of enzymes of the major energy yielding pathways (glucose-6-phosphate dehydrogenase (G6PD), glyceraldehyde-3-phosphate dehydrogenase (GAPD) and succinate dehydrogenase (SDH)). We did not find an increase in lactate dehydrogenase (LDH). In the present longitudinal study of rabbits (from 5 weeks to 42 months of age), we looked for age related changes in the activity of these enzymes in auricular chondrocytes, as well as for collagen and GAG content. Collagen content (micrograms/wet weight) increased up to 12 months and remained stable; total GAG content (micrograms/wet weight) reached its maximal value at growth and then declined gradually, reducing the GAG/collagen ratio dramatically from 36 to 8. At any age LDH was two to three times more active than either G6PD, aldolase, or GAPD. SDH and UDPGD activities were even lower. The age related changes varied: (1) LDH and GAPD were stable and did not change with either growing or aging; (2) G6PD and aldolase reached their maximal activity at 3-9 months, followed by a sharp drop at 12 months. G6PD remained stable, while aldolase continued to decline, although more slowly; (3) Maximal activity of SDH and UDPGD was measured at 5 weeks. Thus, the changes in enzyme activity in chondrocytes with age were specific for each enzyme. The significant decline in G6PD, aldolase, the rate-limiting enzymes of the pentose shunt and classic glycolysis, and SDH markedly reduced the ability of chondrocytes to generate energy.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Differential decline of rabbit chondrocytic dehydrogenases with age. 778 68