Isozyme composition and phosphorylation of brain phosphofructokinase

Foe, Lawrence G.; Kemp, Robert G.

doi:10.1016/0003-9861(84)90016-x

Cited by 58 publications

(20 citation statements)

References 25 publications

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“…The A and B isozymes are present as homotetramers and have been isolated in essentially homogeneous form from skeletal muscle and liver, respectively [14][15]. The C isozyme has also been isolated from brain [16], but brain PFK is a heterotetramer, and consists of a hybrid mixture of the A, B and C types of subunit [17]. In general, subunit composition is responsible for the difference in the properties of these isozymes.…”

Section: Resultsmentioning

confidence: 99%

Phosphofructokinase in rabbit dental pulp is less sensitive to ATP inhibition.

Yamazaki

Hara

Kurihara

et al. 1989

The Journal of Nihon University School of Dentistry

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Section: Resultsmentioning

confidence: 99%

Phosphofructokinase in rabbit dental pulp is less sensitive to ATP inhibition.

Yamazaki

Hara

Kurihara

et al. 1989

The Journal of Nihon University School of Dentistry

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“…1991). Brain PFK‐1, maximally activated with 4–6 µ m Fru‐2,6‐P 2 , is saturated with Fru‐2,6‐P 2 under normal conditions (Foe and Kemp 1984; Yamamoto et al . 1990; Ambrosio et al .…”

Section: Discussionmentioning

confidence: 99%

Identification of a nerve ending‐enriched 29‐kDa protein, labeled with [3‐³²P]1,3‐bisphosphoglycerate, as monophosphoglycerate mutase: inhibition by fructose‐2,6‐bisphosphate via enhancement of dephosphorylation

Ikemoto

Ueda

2003

Journal of Neurochemistry

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Glucose metabolism is of vital importance in normal brain function. Evidence indicates that glycolysis, in addition to production of ATP, plays an important role in maintaining normal synaptic function. In an effort to understand the potential involvement of a glycolytic intermediate (s) Glucose metabolism is of paramount importance in brain function. Cerebral energy is derived from glucose under normal conditions (Siesjo 1978). Hence, the necessity for glucose in brain function had been considered solely due to ATP production. However, evidence has accumulated indicating that hypoglycemia leads to neuronal dysfunction, as judged by abnormal electroencephalogram and population spikes, as well as to abnormal behavior, long before cerebral ATP is depleted (Dirks et al. 1980;Cox and Bachelard 1982;Ghajar et al. 1982). This suggests that sustaining global cellular ATP at the normal level would not substitute for the glucose metabolism requirement. Morino et al. (1991)

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“…The apparent molecular weights of the L-type, M-type, and C-type subunits from normal dog were 78, 86, and 88 kD, respectively, and the relative PFK subunit proportions (L:M:C) were 27:49:24. The relative subunit amounts (L:M:C) in rat and rabbit brain PFK isozymes are 13:49:38 and 14:37:49, respectively [3,20]. In human cerebral cor tex, the percentages (L:M:C) are 15:55:30 [21].…”

Section: Introductionmentioning

confidence: 97%

Presence of a Truncated M-Type Subunit and Altered Kinetic Properties of 6-Phosphofructo-l-Kinase Isozymes in the Brain of a Dog Affected by Glycogen Storage Disease Type VII1

Mhaskar¹,

Giger²,

Dunaway³

1991

Enzyme

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6-Phosphofructo-1-kinase (PFK) activity in the brain of a dog affected by glycogen storage disease type VII was only 31 % of the PFK activity in the normal dog brain. PFK in the normal dog brain was composed of L-type, M-type and C-type subunits with apparent molecular weights of 78,000, 86,000, and 88,000, respectively, and subunit proportions (L:M:C) of 27:49:24. PFK in the affected dog brain was composed of nearly equal levels of the normal L-type and C-type subunits, but a normal M-type subunit was not detected. Using antidog muscle PFK IgG, immunoblots of gels containing partially purified PFK from the affected dog brain revealed a small amount of immunoreactive protein with an apparent molecular weight of 84,000, suggesting the presence of a truncated M-type subunit. Kinetic studies indicated that the PFK isozymes in the affected dog brain exhibited significantly different kinetic regulatory properties when compared to the PFK isozyme pool in the normal dog brain.

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Isozyme composition and phosphorylation of brain phosphofructokinase

Cited by 58 publications

References 25 publications

Phosphofructokinase in rabbit dental pulp is less sensitive to ATP inhibition.

Phosphofructokinase in rabbit dental pulp is less sensitive to ATP inhibition.

Identification of a nerve ending‐enriched 29‐kDa protein, labeled with [3‐³²P]1,3‐bisphosphoglycerate, as monophosphoglycerate mutase: inhibition by fructose‐2,6‐bisphosphate via enhancement of dephosphorylation

Presence of a Truncated M-Type Subunit and Altered Kinetic Properties of 6-Phosphofructo-l-Kinase Isozymes in the Brain of a Dog Affected by Glycogen Storage Disease Type VII1

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Isozyme composition and phosphorylation of brain phosphofructokinase

Cited by 58 publications

References 25 publications

Phosphofructokinase in rabbit dental pulp is less sensitive to ATP inhibition.

Phosphofructokinase in rabbit dental pulp is less sensitive to ATP inhibition.

Identification of a nerve ending‐enriched 29‐kDa protein, labeled with [3‐32P]1,3‐bisphosphoglycerate, as monophosphoglycerate mutase: inhibition by fructose‐2,6‐bisphosphate via enhancement of dephosphorylation

Presence of a Truncated M-Type Subunit and Altered Kinetic Properties of 6-Phosphofructo-l-Kinase Isozymes in the Brain of a Dog Affected by Glycogen Storage Disease Type VII1

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Identification of a nerve ending‐enriched 29‐kDa protein, labeled with [3‐³²P]1,3‐bisphosphoglycerate, as monophosphoglycerate mutase: inhibition by fructose‐2,6‐bisphosphate via enhancement of dephosphorylation