Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Percutaneous needle biopsies were obtained from six limb muscles in six horses before and during a training programme of 10 or 15 weeks designed to involve both aerobic and anaerobic work. In a subsequent detraining period, biopsies were also taken after 5 and 10 weeks. 2. Samples were analysed biochemically for enzyme activity of lactic dehydrogenase (LDH), creatine phosphokinase (CPK), aldolase (ALD), citrate synthase (CS), aspartate aminotransferase (AST), and alanine aminotransferase (ALT) and for glycogen content. Fibre typing was carried out histochemically before and 10 weeks after commencement of training. 3. There was a significant increase in the percentage of high myosin ATPase activity pH 9-4/high oxidative (FTH) fibres with a corresponding decrease in high myosin ATPase activity pH 9-4/low oxidative (FT) fibres and low myosin ATPase activity pH 9-4/high oxidative (ST) fibres after 10 weeks training. 4. During training, enzyme activities increased progressively but at different rates with an approximate twofold increase in all of the enzymes except CPK by the end of the training period. Changes in all the muscles studied were similar. Glycogen content increased by approximately 33% which was significant when all the muscles were considered together. 5. A decrease in enzyme activity occurred after 5 weeks detraining. However at 10 weeks a consistent but inexplicable increase in all enzyme levels, except CS again occurred. 6. It is concluded that training increased greatly the activity of enzymes involved in both aerobic and anaerobic metabolism.
 ...
PMID:The effect of training and detraining on muscle composition in the horse. 14 28

Skeletal limb muscles of the dog could generally be differentiated into three fibre types according to myosin adenosine triphosphatase (ATPase) (pH 9.4) and succinic dehydrogenase activities. However, because this was not always possible, for comparative purposes only, division into low myosin ATPase (slow twitch) type I and high myosin ATPase (fast twitch) type II fibres was used. The percentage of these fibre types in m deltoideus, m triceps brachii caput longum, m vastus lateralis, m gluteus medius, m biceps femoris and m semitendinosus was examined in the greyhound, crossbred and foxhound. In all muscles the greyhound had a significantly higher percentage of fibres with high myosin ATPase activity at pH 9.4 than the other breeds, with almost 100 per cent in most muscles examined. The activities of nine enzymes and glycogen concentration were determined in m gluteus medius and m semitendinosus of the greyhound and crossbred. Significantly higher levels of creatine kinase, aldolase, alanine aminotransferase and citrate synthase and significantly lower activities of 3-hydroxyacyl coenzyme A dehydrogenase and hexokinase were found in both muscles of the greyhound. The implications of these findings are discussed.
 ...
PMID:Skeletal muscle fibre composition in the dog and its relationship to athletic ability. 645 29

Structural relationships between the myofibrillar contractile apparatus and the enzymes that generate ATP for muscle contraction are not well understood. We explored whether glycolytic enzymes are localized in Drosophila flight muscle and whether localization is required for function. We find that glycerol-3-phosphate dehydrogenase (GPDH) is localized at Z-discs and M-lines. The glycolytic enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are also localized along the sarcomere with a periodic pattern that is indistinguishable from that of GPDH localization. Furthermore, localization of aldolase and GAPDH requires simultaneous localization of GPDH, because aldolase and GAPDH are not localized along the sarcomere in muscles of strains that carry Gpdh null alleles. In an attempt to understand the process of glycolytic enzyme colocalization, we have explored in more detail the mechanism of GPDH localization. In flight muscle, there is only one GPDH isoform, GPDH-1, which is distinguished from isoforms found in other tissues by having three C-terminal amino acids: glutamine, asparagine, and leucine. Transgenic flies that can produce only GPDH-1 display enzyme colocalization similar to wild-type flies. However, transgenic flies that synthesize only GPDH-3, lacking the C-terminal tripeptide, do not show the periodic banding pattern of localization at Z-discs and M-lines for GPDH. In addition, neither GAPDH nor aldolase colocalize at Z-discs and M-lines in the sarcomeres of muscles from GPDH-3 transgenic flies. Failure of the glycolytic enzymes to colocalize in the sarcomere results in the inability to fly, even though the full complement of active glycolytic enzymes is present in flight muscles. Therefore, the presence of active enzymes in the cell is not sufficient for muscle function; colocalization of the enzymes is required. These results indicate that the mechanisms by which ATP is supplied to the myosin ATPase, for muscle contraction, requires a highly organized cellular system.
 ...
PMID:Flight muscle function in Drosophila requires colocalization of glycolytic enzymes. 930 64