Phosphofructokinase deficiency in skeletal muscle. A new type of glycogenosis

Tarui, Seiichiro; Okuno, Giichi; Ikura, Yuji; Tanaka, Takehiko; Suda, Masami; Nishikawa, Mitsuo

doi:10.1016/0006-291x(65)90156-7

Cited by 338 publications

(87 citation statements)

References 9 publications

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“…Interestingly, a genetic defect in human muscle phosphofructokinase also results in overaccumulation of glycogen (type VII glycogen storage disease; Ref. 30). The most important outcome of the present study is to refocus attention on the role of metabolites, specifically glucose-6-P, in regulating glycogen synthase.…”

Section: Discussionmentioning

confidence: 89%

Glucose-6-P Control of Glycogen Synthase Phosphorylation in Yeast

Huang

Wilson

Roach

1997

Journal of Biological Chemistry

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The SNF1 gene encodes a protein kinase necessary for expression of glucose-repressible genes and for the synthesis of the storage polysaccharide glycogen. From a genetic screen, we have found that mutation of the PFK2 gene, which encodes the ␤-subunit of 6-phosphofructo-1-kinase, restores glycogen accumulation in snf1 cells. Loss of PFK2 causes elevated levels of metabolites such as glucose-6-P, hyperaccumulation of glycogen, and activation of glycogen synthase, whereas glucose-6-P is reduced in snf1 cells. Other mutations that increase glucose-6-P, deletion of PFK1, which codes for the ␣-subunit of 6-phosphofructo-1-kinase, or of PGI1, the phosphoglucoisomerase gene, had similar effects on glycogen metabolism as did pfk2 mutants. We propose that elevated glucose-6-P mediates the effects of these mutations on glycogen storage. Glycogen synthase kinase activity was reduced in extracts from pfk2 cells but was restored to that of wild type if the extract was gel-filtered to remove small molecules. Also, added glucose-6-P inhibited the glycogen synthase kinase activity in extracts from wild-type cells, half-maximally at ϳ2 mM. We suggest that glucose-6-P controls glycogen synthase activity by two separate mechanisms. First, glucose-6-P is a direct activator of glycogen synthase, and second, it controls the phosphorylation state of glycogen synthase by inhibiting a glycogen synthase kinase.

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Section: Discussionmentioning

confidence: 89%

Glucose-6-P Control of Glycogen Synthase Phosphorylation in Yeast

Huang

Wilson

Roach

1997

Journal of Biological Chemistry

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“…The generator may lie within the CNS or in peripheral neuromuscular membranes. Whatever the location of the generator, it appears to be facilitated by a variety of factors that include strong voluntary contraction, exercise (Layzer et al 1986;Miles et al 1994;Schwellnus et al 1997), sleep (Gootnick 1943;Nicholson et al 1945), pregnancy (Oba 1967;Page et al 1953), and several pathologies such as myopathy, neuropathy, motoneuron disease (Brown 1951;McGee 1990), metabolic disorders (Layzer et al 1967;McArdle 1951;Tarui et al 1965), electrolyte imbalance (Edsall 1908;Oswald 1925;Talbott 1935), and endocrine pathology (Satoh et al 1983). However, the link between these factors and the involuntary muscle electrical activity that accompanies cramp remains unclear.…”

Section: Introductionmentioning

confidence: 99%

Reflex Inhibition of Normal Cramp Following Electrical Stimulation of the Muscle Tendon

Khan¹,

Burne²

2007

Journal of Neurophysiology

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“…Three different isoenzymes have been described: the liver, muscle, and platelet subtypes (2). The inherited deficiency of muscle PFK1 (PFK1-M) is associated with a heterogeneous group of clinical syndromes, including hemolysis, excess glycogen storage, and exercise-induced myopathy (3,4). The most common syndrome, known as glycogenosis type VII or Tarui's disease (4), appears to be prevalent among people of Ashkenazi Jewish, Italian, or Japanese ancestry with an autosomal recessive transmission (5)(6)(7).…”

Section: Introductionmentioning

confidence: 99%

Deficiency of phosphofructo-1-kinase/muscle subtype in humans impairs insulin secretion and causes insulin resistance.

Ristow¹,

Vorgerd²,

Möhlig³

et al. 1997

J. Clin. Invest.

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Non-insulin-dependent diabetes mellitus (NIDDM) is caused by peripheral insulin resistance and impaired ␤ cell function. Phosphofructo-1-kinase (PFK1) is a rate-limiting enzyme in glycolysis, and its muscle subtype (PFK1-M) deficiency leads to the autosomal recessively inherited glycogenosis type VII Tarui's disease. It was evaluated whether PFK1-M deficiency leads to alterations in insulin action or secretion in humans.A core family of four members was evaluated for PFK1-M deficiency by DNA and enzyme-activity analyses. All members underwent oral and intravenous glucose tolerance tests (oGTT and ivGTT) and an insulin-sensitivity test (IST) using octreotide.Enzyme PFK1-M deficiency causes impaired insulin secretion in response to glucose, demonstrating its participation in islet glucose metabolism, and peripheral insulin resistance. These combined metabolic sequelae of PFK-1 deficiency identify it as a candidate gene predisposing to NIDDM. ( J.

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Phosphofructokinase deficiency in skeletal muscle. A new type of glycogenosis

Cited by 338 publications

References 9 publications

Glucose-6-P Control of Glycogen Synthase Phosphorylation in Yeast

Glucose-6-P Control of Glycogen Synthase Phosphorylation in Yeast

Reflex Inhibition of Normal Cramp Following Electrical Stimulation of the Muscle Tendon

Deficiency of phosphofructo-1-kinase/muscle subtype in humans impairs insulin secretion and causes insulin resistance.

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