The Regional and Subcellular Distribution of 2′,3′‐cyclic Nucleotide 3′‐phosphohydrolase in the Central Nervous System

Kurihara, Tadashi; Tsukada, Yasuzo

doi:10.1111/j.1471-4159.1967.tb06164.x

Cited by 456 publications

(137 citation statements)

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“…This protein, comprising 4-5% of the total protein of isolated CNS myelin, is the first of the major myelin-related proteins to appear in developing brain (Sprinkle et al, 1978). Although the physio-logical function of CNP remains unknown, the deposition of this protein in brain parallels the developmental accumulation of myelin and thus has served as a useful biochemical marker for myelin membrane in vitro (Kurihara and Tsukada, 1967;Olafson et al, 1969;Braun and Barchi, 1972). Despite the fact that 60% or more of the enzyme activity is present in subcellular fractions of brain that contain myelin, there has been considerable doubt about its actual presence in compact lamellae of the sheath (Shapira et al, 1978;Danks and Matthieu, 1979).…”

Section: Oligodendrocytesmentioning

confidence: 99%

Immunocytochemical localization by electron microscopy of 2'3'-cyclic nucleotide 3'-phosphodiesterase in developing oligodendrocytes of normal and mutant brain

et al. 1988

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Oligodendrocytes or their putative progenitors were the only cells found to be immunoreactive to polyclonal antisera against the enzyme 2′3′-cyclic nucleotide 3′-phosphodiesterase (CNP) in developing and mature brains of rats and mice, as visualized by light and electron microscopy. Prior to myelination (day 6), oligodendrocytes of the corpus callosum have reticular networks of CNP-containing filopodia, in addition to abundant CNP throughout the cytoplasm. Some glioblast-like cells of the subventricular zone are also immunoreactive to anti-CNP, suggesting that, as progenitors of oligodendroglia, they express this myelination-related protein as one of the earliest events in myelinogenesis. Following the commencement of myelination (day 15), many oligodendrocytes lose much of their lacelike network of fine projections, possessing, instead, larger CNP-filled processes that extend to myelin-bearing fibers. CNP was always found only in the cytoplasm-containing compartments of the cells and myelin sheaths; neither lamellae nor cellular membranes were immunostained. These data support our contention that CNP is not an intrinsic membrane protein, despite its strong interaction with membrane components when cells are disrupted. In mutant (mld) mice (day 25), the many distended and uncompacted oligodendroglial processes that invest axons with only a few turns of membrane contained cytoplasmic CNP, accounting for the elevated levels of CNP activity previously noted in tissue fractions.

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Section: Oligodendrocytesmentioning

confidence: 99%

Immunocytochemical localization by electron microscopy of 2'3'-cyclic nucleotide 3'-phosphodiesterase in developing oligodendrocytes of normal and mutant brain

et al. 1988

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“…In vitro, CNPase hydrolyzes 2',3'-cyclic nucleotides to form 2'-nucleotides [32,33], however, 2',3'-cyclic nucleotides are not known to have physiological relevance in mammals. In the CNS, CNPase is highly localized to the myelin sheath and oligodendroglia [34][35][36][37]. It is reasonable to assume that CNPase function may be related to differentiation of oligodendroglial cells.…”

Section: Resultsmentioning

confidence: 99%

Differential display PCR reveals increased expression of 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase by lithium

Wang¹,

Young²

1996

FEBS Letters

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Differential display PCR was used to study the effects of lithium on gene expression. Four candidate genes were isolated and verified by Northern hybridization after 1 week treatment of C6 glioma cells with therapeutically relevant concentrations of LiCI (1 mM). Sequencing analysis revealed three previously unidentified cDNA fragments in addition to a sequence with 99% homology with the cDNA for 2',3'-cyclic nucleotide 3'-phosphodiesterase type II (CNPasell). Since CNPaselI is important in myelinogenesis and possibly neuronal growth and repair, the present findings suggest that lithium treatment may regulate these processes.

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“…This enzyme activity has also been found in bacteria [7]. However, CNPase activity is most prominent in membranes of the central nervous system (CNS) [2] and shows a remarkably high activity in myelin [8], a tissue fraction in which only a few enzymes are present in readily measurable quantities. Developmental changes in CNPase activity have been shown to correlate well with myelination patterns in chick brain and spinal cord [9] and parts of rat brain [10].…”

Section: Introductionmentioning

confidence: 99%

Two molecular forms of the isolated brain enzyme 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase

1981

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The Regional and Subcellular Distribution of 2′,3′‐cyclic Nucleotide 3′‐phosphohydrolase in the Central Nervous System

Cited by 456 publications

References 1 publication

Immunocytochemical localization by electron microscopy of 2'3'-cyclic nucleotide 3'-phosphodiesterase in developing oligodendrocytes of normal and mutant brain

Immunocytochemical localization by electron microscopy of 2'3'-cyclic nucleotide 3'-phosphodiesterase in developing oligodendrocytes of normal and mutant brain

Differential display PCR reveals increased expression of 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase by lithium

Two molecular forms of the isolated brain enzyme 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase

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