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)

The frequent association of myotonia with dystrophy and the knowledge that calcium is increased in injured skeletal muscle cells suggest a possible relationship between cell calcium and myotonic alterations. This investigation has been performed to study the role of calcium in experimental myotonia induced by anthracene-9-carboxylic acid (9-AC) in rats treated with several regimens of food and exercise. Thirty-two rats were divided into 4 groups of 8 rats each, one control and 3 experimental groups. The treatments included caffeine plus exercise (group 2), and a calcium-rich diet (group 3); these procedures were designed to increase intracellular calcium; another group was treated with 9-AC as a myotonia-inducer (group 4). The treatment for all groups lasted 60 days. No significant differences in plasma sodium, potassium, chloride and calcium between control and experimental groups were observed. Whole muscle calcium in wet tissue samples did no change with any treatment. On the contrary, mitochondrial calcium showed a significantly higher concentration in group 3 and 4. CPK and aldolase activities in groups 1, 2 and 3 were similar; but in group 4 these enzyme activities were significantly higher (p less than 0.05). The electrical and mechanical responses were not altered in any rat with any experimental treatment. Our data suggest that myotonia is a predisposing factor for an altered mitochondrial calcium homeostasis in this model; in addition, the enzyme activities of CPK and aldolase were increased in the rats of group 4 implicating that myotonia is a crucial factor in the development of enzymatic abnormalities.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of myotonia induced by anthracene-9-carboxylic acid on mitochondrial calcium, plasma creatinine-phosphokinase and aldolase activity in the rat. 139 15

DIDS (4,4'-di-isothiocyanostilbene-2,2'-disulfonate), an anion channel blocker, triggers Ca2+ release from skeletal muscle SR (sarcoplasmic reticulum). The present study characterized the effects of DIDS on rabbit skeletal single Ca2+-release channel/RyR1 (ryanodine receptor type 1) incorporated into a planar lipid bilayer. When junctional SR vesicles were used for channel incorporation (native RyR1), DIDS increased the mean P(o) (open probability) of RyR1 without affecting unitary conductance when Cs+ was used as the charge carrier. Lifetime analysis of single RyR1 activities showed that 10 microM DIDS induced reversible long-lived open events (P(o)=0.451+/-0.038) in the presence of 10 microM Ca2+, due mainly to a new third component for both open and closed time constants. However, when purified RyR1 was examined in the same condition, 10 microM DIDS became considerably less potent (P(o)=0.206+/-0.025), although the caffeine response was similar between native and purified RyR1. Hence we postulated that a DIDS-binding protein, essential for the DIDS sensitivity of RyR1, was lost during RyR1 purification. DIDS-affinity column chromatography of solubilized junctional SR, and MALDI-TOF (matrix-assisted laser-desorption ionization-time-of-flight) MS analysis of the affinity-column-associated proteins, identified four major DIDS-binding proteins in the SR fraction. Among them, aldolase was the only protein that greatly potentiated DIDS sensitivity. The association between RyR1 and aldolase was further confirmed by co-immunoprecipitation and aldolase-affinity batch-column chromatography. Taken together, we conclude that aldolase is physically associated with RyR1 and could confer a considerable potentiation of the DIDS effect on RyR1.
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PMID:Aldolase potentiates DIDS activation of the ryanodine receptor in rabbit skeletal sarcoplasmic reticulum. 1681 80