Glycerol Phosphate Dehydrogenase: Reduced Activity in Multiple Sclerosis Plaques Confirms Localization in Oligodendrocytes

Hirsch, Hilde E.; Blanco, Cesar E.; Parks, Mary Ellen

doi:10.1111/j.1471-4159.1980.tb11212.x

Cited by 16 publications

(7 citation statements)

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“…(1970) but not by Kuhlman and Lowry ( 1956). Our value for GPDH in the adult rat brain falls within the range of 30-67 nmol/min/mg protein reported in the literature (Laatsch, 1962;deVellis et a]., 1967;McGinnis and deVellis, 1974;Hirsch et a]., 1980), and the developmental increase that we found between 20 and 60 days had been observed in other studies (Laatsch, 1962; deVellis e t a]., 1967). Differences in the animals' genetic backgrounds, the reaction temperatures, and the regions of the brain can probably account for the differences among these reports.…”

Section: Discussionsupporting

confidence: 90%

“…Because of the immunocytochemical localization of glycerol-3-phosphate dehydrogenase ( G P D H ) (i-a-g1ycerophosphate:NAD oxidoreductase, E C 1.1.1.8) in the oligodendrocytes of rat cerebellum (Leveille et al, 1980) as well as the early proposal of a role for this enzyme in lipid biosynthesis during myelination (Laatsch, 1962), it was anticipated that isolated oligodendrocytes might be enriched in GPDH. Furthermore, studies of G 6 glioma and primary oligodendrocyte cultures had suggested the oligodendrocytes t o be the target cells for glucocorticoid induction of this enzyme in the CNS McCarthy and devellis, 1980), a n 4 loss of GPDH in multiple sclerosis plaques had been cited a s evidence for the oligodendroglial localization of this enzyme (Hirsch et al, 1980). Therefore, the comparison of the G P D H activities in bulkisolated oligodendrocytes, neurons, and astrocytes was of particular interest.…”

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confidence: 99%

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Glycerol Phosphate Dehydrogenase, Glucose‐6‐Phosphate Dehydrogenase, and Lactate Dehydrogenase: Activities in Oligodendrocytes, Neurons, Astrocytes, and Myelin Isolated from Developing Rat Brains

Cammer

et al. 1982

Journal of Neurochemistry

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Glycerol phosphate dehydrogenase (GPDH), glucose-6-phosphate dehydrogenase (G6PDH), and lactate dehydrogenase (LDH) activities were determined in oligodendrocytes, neurons, and astrocytes isolated from the brains of developing rats. The activity of each enzyme was significantly lower in both neurons and astrocytes than in oligodendrocytes. The GPDH activity in oligodendrocytes increased more than 4-fold during development, and at 120 days cells of this type had 1.4-fold the specific activity of forebrain homogenates. The G6PDH activities in oligodendrocytes from 10-day-old rats were 1.4-fold the activities in the forebrain homogenates. The activities of this enzyme in oligodendrocytes were progressively lower at later ages, such that at 120 days the cells had 0.8 times the specific activities of homogenates. The oligodendrocytes had 0.6 times the homogenate activities of LDH at 10 days, and this ratio had decreased to 0.2 by 120 days. These enzymes were also measured in myelin isolated from 20-, 60-, and 120-day-old rats. By 120 days the specific activities of G6PDH and LDH in myelin were less than 8% of the respective activities in homogenates. The GPDH activity in myelin was, however, at least 20% the specific activity in the homogenates, even in the oldest animals. It is proposed that LDH could be used as a marker for oligodendroglial cytoplasm in subfractions of myelin and in myelin-related membrane vesicles.

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Section: Discussionsupporting

confidence: 90%

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confidence: 99%

Glycerol Phosphate Dehydrogenase, Glucose‐6‐Phosphate Dehydrogenase, and Lactate Dehydrogenase: Activities in Oligodendrocytes, Neurons, Astrocytes, and Myelin Isolated from Developing Rat Brains

Cammer

et al. 1982

Journal of Neurochemistry

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“…Histopathological evaluation of these slides was carried out by Pierre Duquette, MD, and Ivan Robitaille, MD, both of Montreal. Summaries of their analyses of most of the plaques studied and of the clinical histories of the patients were reported previously [5,6]. Plaques selected for the present study were those for which biochemical data relating to plaque activity were available from previous work Tissue sections were stored under vacuum at -2o"C, under which conditions most enzymes retain their activity for many years [8].…”

Section: Tissue Samplesmentioning

confidence: 99%

Na⁺ ‐ and K⁺‐dependent adenosine triphosphatase changes in multiple sclerosis plaques

Hirsch

Parks

1983

Annals of Neurology

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Na+- and K+-dependent adenosine triphosphatase [(Na+ + K+)-ATPase] was studied in microdissected samples from sections of histologically active and inactive plaques of multiple sclerosis. In active plaques the enzyme was found to be markedly reduced in activity, whereas in old, chronic plaques ATPase activities were higher than those of unaffected white matter. White matter from control patients and normal-appearing white matter from MS patients did not differ with regard to ATPase activities. The results suggest that reversible changes in the sodium pump mechanism may be involved in the pathophysiology of multiple sclerosis.

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“…The results of our experiment thus confirm theirs. Hirano et al (1985) reported that the CNP activities in rats which had been exposed to hyperphenylalaninemia in their fetal lives were significantly lower than those in controls at 15 days of age, while there was no difference in the activity of glycerol-3-phosphate dehydrogenase (GPDH), a marker enzyme for oligodendroglia (Hirsh et al, 1980;Leveille et al, 1980) at that time. This normal activity of GPDH suggests there is some exclusive damage to the mechanism of myelination.…”

Section: Discussionmentioning

confidence: 99%

Effects of Maternal Hyperphenylalaninemia on Postnatal Myelination in Mice

Sasahara

Ohya

Shimada

1987

Congenital Anomalies

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The effects of maternal hyperphenylalaninemia induced by phenylalanine and p-chlorophenylalanine loading diets on brain growth and myelination were studied in mice. The wet weights, protein contents and activities of 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNP) of the cerebrum, brain stem and cerebellum were estimated on 7, 14, 21, 28 and 56 days after the birth. Protein and lipid contents in the myelin fraction of the whole brain were also examined on days 28 and 56. In the experimental groups, the activities of CNP, a marker enzyme of myelin, were lower than those in the control in each part of the brain. The protein contents in the light myelin subfraction, which is regarded as a mature type of myelin, were also decreased in the experimental group after 28 days of age, while those in the heavy myelin subfraction, which is regarded as an immature type of myelin, showed no significant reduction even after 28 days of age. These results suggest that maternal hyperphenylalaninemia has a potential effect on postnatal myelination of the brain, and also that impaired myelination may play some role in the pathogenesis of mental retardation of maternal phenylketonuria. The proportions of unsaturated to saturated fatty acids in phosphatidylethanolamine and sphingomyelin were decreased significantly on day 56 in the heavy myelin subfraction in compariscin to the controls. These changes may have some correlation with interference in the formation of matured myelin.

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Glycerol Phosphate Dehydrogenase: Reduced Activity in Multiple Sclerosis Plaques Confirms Localization in Oligodendrocytes

Cited by 16 publications

References 12 publications

Glycerol Phosphate Dehydrogenase, Glucose‐6‐Phosphate Dehydrogenase, and Lactate Dehydrogenase: Activities in Oligodendrocytes, Neurons, Astrocytes, and Myelin Isolated from Developing Rat Brains

Glycerol Phosphate Dehydrogenase, Glucose‐6‐Phosphate Dehydrogenase, and Lactate Dehydrogenase: Activities in Oligodendrocytes, Neurons, Astrocytes, and Myelin Isolated from Developing Rat Brains

Na⁺ ‐ and K⁺‐dependent adenosine triphosphatase changes in multiple sclerosis plaques

Effects of Maternal Hyperphenylalaninemia on Postnatal Myelination in Mice

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Glycerol Phosphate Dehydrogenase: Reduced Activity in Multiple Sclerosis Plaques Confirms Localization in Oligodendrocytes

Cited by 16 publications

References 12 publications

Glycerol Phosphate Dehydrogenase, Glucose‐6‐Phosphate Dehydrogenase, and Lactate Dehydrogenase: Activities in Oligodendrocytes, Neurons, Astrocytes, and Myelin Isolated from Developing Rat Brains

Glycerol Phosphate Dehydrogenase, Glucose‐6‐Phosphate Dehydrogenase, and Lactate Dehydrogenase: Activities in Oligodendrocytes, Neurons, Astrocytes, and Myelin Isolated from Developing Rat Brains

Na+ ‐ and K+‐dependent adenosine triphosphatase changes in multiple sclerosis plaques

Effects of Maternal Hyperphenylalaninemia on Postnatal Myelination in Mice

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Na⁺ ‐ and K⁺‐dependent adenosine triphosphatase changes in multiple sclerosis plaques