Skeletal muscle glycogenosis: an investigation of two dissimilar cases

Thomson, W. H.; Maclaurin, J. C.; Prineas, John W.

doi:10.1136/jnnp.26.1.60

Cited by 76 publications

(26 citation statements)

References 24 publications

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“…This may suggest the glycogen accumulation in skeletal muscle of uremic patients. Glycogen accumulation accompanied by a diminished lactate response to ischemic exercise, as indicated in this study on uremic patients, closely resembles the feature of McArdle's disease [11] or other glycogen storage diseases which have been shown to have the defect of glycolysis [16][17][18]. However, normal glycogen content of skeletal muscle in patients with chronic renal failure was reported on the basis of biochemical analysis [19], and variation of muscle glycogen content according to exercise and diet was also reported [9].…”

Section: Discussionmentioning

confidence: 75%

Impaired Lactate Production by Skeletal Muscle with Anaerobic Exercise in Patients with Chronic Renal Failure

Nakao

Fujiwara

Isoda

et al. 1982

Nephron

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The lactate concentration in antecubital venous blood was determined in 33 patients before and after ischemic forearm exercise. Before exercise, there was no significant difference in serum lactate level between uremic patients and controls. However, after ischemic exercise the mean serum lactate level in uremic patients was significantly lower than that of controls. The results may lead to the conclusion that uremic patients have a markedly reduced ability to form lactate with anaerobic exercise probably due to inhibition of glycolytic enzymes of skeletal muscle.

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Section: Discussionmentioning

confidence: 75%

Impaired Lactate Production by Skeletal Muscle with Anaerobic Exercise in Patients with Chronic Renal Failure

Nakao

Fujiwara

Isoda

et al. 1982

Nephron

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“…Even if considerable heterogeneities are seen clinically, only a few PGMdeficiency cases have been reported (Thomson et al 1963;Brown and Brown 1968;Sugie et al 1988), in which severe reduction of PGM activity is not lethal but causes muscle-glycogen-storage disease leading to decreased muscle mass. This finding seems reasonable because PGM1 plays an important role in the anaerobic glycolysis pathway; thus, PGM1 isozyme deficiency appears to be disadvantageous for survival.…”

Section: Discussionmentioning

confidence: 96%

Identification of Base Substitutions in Ten Types of Rare Variants of Phosphoglucomutase-1 (PGM1) Encountered in Japanese

Takahashi¹,

Omine²,

Kaneko³

et al. 2001

Human Biology

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In a previous starch-gel electrophoresis study of erythrocyte phosphoglucomutase-1 (PGM1) in 23,095 Japanese from Hiroshima and Nagasaki, we detected 14 types of rare variant alleles. To determine sequence differences in these rare alleles, cell lines were established from peripheral Blymphocytes from 24 unrelated individuals in whom nine types of rare variants are presumed to exist on the basis of earlier electrophoresis studies. cDNAs reverse transcribed from mRNAs extracted from these cell lines were amplified by polymerase chain reaction and sequences determined. Amino acid substitution types were deduced from each cDNA sequence. Although two individuals were reported to have an identical electromorph (PGM1 4HR3), sequence analysis revealed that alleles encoding these electromorphs possessed different base substitutions, and one was renamed PGM1 4HR4. As the amino acid substitution of ten different variants could be deduced by cDNA sequence in this study, the effect of each amino acid substitution on enzyme activity could be precisely simulated. The secondary structure of each variant predicted by computer simulations revealed that very decreased activity observed on PGM1 4HR2 protein was caused by significant secondary structure change introduced by the amino acid substitution. On the basis of the crystal structure, the amino acid substitutions of the ten types of rare variants seem to be outside the active center of this enzyme.

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“…McA rdle [10], who was the first to make this observation inferred that the symptoms of the disease are due to a defect in glycogen break down, which results in a much increased glycogen concentration in the muscle. Other authors, such as Schmidt and Mahler [17], Pearson et al [14], T homson et al [24], Rowland et al [16], H ockaday et al [6] de scribed similar cases. In patients with this kind of disease the specific sign is the induction of contracture by exercise of the forearm muscle while ar terial circulation is occluded (by a pressure cuff above the elbow).…”

Section: Discussionmentioning

confidence: 96%

Biochemical Determinations in a Recently Investigated Case of McArdle’s Disease

Luca¹,

Bănileanu²

1974

Eur Neurol

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Our study includes assays of the serum activities of ALD, CPK and GOT and GPT transaminase in a patient with McArdle’s disease. Muscle glycolysis has been investigated and the glycogen concentration and phosphorylase activity determined biochemically in the muscle biopsy. Our results point to three major biochemical features which are indicative of McArdle’s disease: in the blood, the failure of venous lactic acid to rise after ischaemic exercise, and in the muscle the increase of glycogen concentration and the lack of phosphorylase activity.

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Skeletal muscle glycogenosis: an investigation of two dissimilar cases

Cited by 76 publications

References 24 publications

Impaired Lactate Production by Skeletal Muscle with Anaerobic Exercise in Patients with Chronic Renal Failure

Impaired Lactate Production by Skeletal Muscle with Anaerobic Exercise in Patients with Chronic Renal Failure

Identification of Base Substitutions in Ten Types of Rare Variants of Phosphoglucomutase-1 (PGM1) Encountered in Japanese

Biochemical Determinations in a Recently Investigated Case of McArdle’s Disease

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