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

Braun, P.E.; Sandillon, F.; Edwards, A.M.; Matthieu, J.-M.; Privat, Alain

doi:10.1523/jneurosci.08-08-03057.1988

Cited by 141 publications

(98 citation statements)

References 29 publications

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“…On the other hand, Olig3 and Nkx2.2 (but not Olig1 or Olig2) co-stained with ␤III-tubulin in SVZa (Fig. 7G, 7J), while Nkx2.2 and Olig2 co-labeled with the oligodendrocyte marker CNP (Braun et al, 1988) in the adjacent striatal parenchyma (Fig. 7H).…”

Section: Expression Of Olig Proteins By Svza Progenitorsmentioning

confidence: 99%

Transcription factor protein expression patterns by neural or neuronal progenitor cells of adult monkey subventricular zone

Tonchev¹,

Yamashima²,

Sawamoto³

2006

Neuroscience

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Abstract-The anterior subventricular zone of the adult mammalian brain contains progenitor cells which are upregulated after cerebral ischemia. We have previously reported that while a part of the progenitors residing in adult monkey anterior subventricular zone travels to the olfactory bulb, many of these cells sustain location in the anterior subventricular zone for months after injury, exhibiting a phenotype of either neural or neuronal precursors. Here we show that ischemia increased the numbers of anterior subventricular zone progenitor cells expressing developmentally regulated transcription factors including Pax6 (paired-box 6), Emx2 (empty spiracles-homeobox 2), Sox 1-3 (sex determining region Y-box 1-3), Ngn1 (neurogenin 1), Dlx1,5 (distalless-homeobox 1,5), Olig1,3 (oligodendrocyte lineage gene 1,3) and Nkx2.2 (Nk-box 2.2), as compared with control brains. Analysis of transcription factor protein expression by sustained neural or neuronal precursors in anterior subventricular zone revealed that these two cell types were positive for characteristic sets of transcription factors. The proteins Pax6, Emx2, Sox2,3 and Olig1 were predominantly localized to dividing neural precursors while the factors Sox1, Ngn1, Dlx1,5, Olig2 and Nkx2.2 were mainly expressed by neuronal precursors. Further, differences between monkeys and non-primate mammals emerged, related to expression patterns of Pax6, Olig2 and Dlx2. Our results suggest that a complex network of developmental signals might be involved in the specification of primate progenitor cells.

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Section: Expression Of Olig Proteins By Svza Progenitorsmentioning

confidence: 99%

Transcription factor protein expression patterns by neural or neuronal progenitor cells of adult monkey subventricular zone

Tonchev¹,

Yamashima²,

Sawamoto³

2006

Neuroscience

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“…CNPase also cross-links with actin (18,19). Like JN, CNPase is found mainly in the cytoplasmcontaining noncompact regions of the myelin sheath (20,21). In CNPase1-knockout mice, axons undergo swelling and degeneration without significant abnormality of the myelin sheath (22).…”

Section: Jn: An Oligodendroglia Marker Of a Previously Unidentified Pmentioning

confidence: 99%

Juxtanodin: An oligodendroglial protein that promotes cellular arborization and 2′,3′-cyclic nucleotide-3′-phosphodiesterase trafficking

Zhang

Cao²,

Guo³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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In the process of screening cell-type-specific genes, we identified juxtanodin (JN), an oligodendroglial protein featuring a putative C-terminal actin-binding domain. At the cellular level, JN in the rat CNS colocalized with 2 ,3 -cyclic nucleotide-3 -phosphodiesterase (CNPase), a cytoskeleton-related oligodendroglial protein. In the myelin sheath, JN was found mainly in the abaxon and the lateral few terminal loops. Its apposition to the myelinated axon, through the latter, defined an axonal subregion, herewith termed juxtanode, at the Ranvier node-paranode junction. During forebrain ontogenesis, JN expression paralleled that of MBPs but lagged behind CNPase. Juxtanodin transfection promoted arborization of cultured OLN-93 cells and augmented endogenous CNPase expression and transport to the process arbors of cultured primary oligodendrocyte precursors. These results reveal JN as a cytoskeleton-related oligodendroglial protein that delineates the juxtanode and might serve oligodendrocyte motility, differentiation, or myelin-axon signaling. Functionally, JN may be involved in CNS myelination and͞or specialization of the node of Ranvier.myelin-axon interaction ͉ oligodendrocyte ͉ node of Ranvier ͉ cytoskeleton O ligodendroglia are highly specialized myelin-forming cells of the CNS. Adequate myelination serves to insulate and accelerate the propagation of action potentials. Abnormalities in myelin formation͞maintenance may underlie diverse neurological disorders, ranging from multiple sclerosis to schizophrenia (1, 2). Matched with highly specialized functions and unique architecture, various oligodendrocyte͞myelin-selective molecules, such as myelin basic protein (MBP), myelin-associated glycoprotein, and 2Ј,3Ј-cyclic nucleotide-3Ј-phosphodiesterase (CNPase), have been isolated and characterized (1, 3). It is likely that many more are yet to be revealed. The identification and characterization of such molecules will probably help elucidate molecular mechanisms of myelination and dys-or demyelinating diseases.The unique architecture of the myelin sheath entails specialized, yet elusive, cytoskeletal mechanisms of myelin-forming cells. Here, we report the molecular features, cellular expression, and functional roles of juxtanodin (JN), a previously unidentified cytoskeleton-related oligodendrocyte-specific protein. Materials and MethodsIdentification and Characterization of the mRNA. Cell-type-specific CNS genes were sought out by in situ hybridization histochemistry (ISH). Briefly, cDNA clones (n ϭ 1,500) from a rat brain cDNA library (Invitrogen) were sequenced and compared by BLAST searches against National Center for Biotechnology Information nucleotide and protein nonredundant databases (4). For the unannotated cDNA sequences (n ϭ 274), expression of the mRNAs in the CNS was mapped by ISH using digoxigeninlabeled riboprobes. A 3.6-kb cDNA clone with a predicted ORF encoding 282 amino acid residues was thereby identified, and the gene was subsequently named juxtanodin (JN). A search of EST databases revealed an...

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“…CNP is associated exclusively with these glial cells in the nervous system, and constitutes 4% of the total myelin proteins in the central nervous system; it is also present at lower levels in photoreceptor cells and several nonneural cells, notably lymphocytes (3,4). In oligodendrocytes, this enzyme is found throughout the cell body but is much more abundant within the process extensions, as well as in the outer cell periphery, in close apposition to the plasma membrane (5,6). Although its biological function is unknown, numerous independent studies suggest a role for this protein in migration and/or expansion of membranes during myelination (7)(8)(9)(10)(11)(12).…”

mentioning

confidence: 99%

Identification of Essential Residues in 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase

Lee¹,

Gravel²,

Gao

et al. 2001

Journal of Biological Chemistry

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2,3-Cyclic nucleotide 3-phosphodiesterase (CNP; EC 3.1.4.37) catalyzes in vitro hydrolysis of 3-phosphodiester bonds in 2,3-cyclic nucleotides to produce 2-nucleotides exclusively. N-terminal deletion mapping of the C-terminal two-thirds of recombinant rat CNP1 identified a region that possesses the catalytic domain, with further truncations abolishing activity. Proteolysis and kinetic analysis indicated that this domain forms a compact globular structure and contains all of the catalytically essential features. Subsequently, this catalytic fragment of CNP1 (CNP-CF) was used for chemical modification studies to identify amino acid residues essential for activity. 5,5-Dithiobis-(2-nitrobenzoic acid) modification studies and kinetic analysis of cysteine CNP-CF mutants revealed the nonessential role of cysteines for enzymatic activity. On the other hand, modification studies with diethyl pyrocarbonate indicated that two histidines are essential for CNPase activity. Consequently, the only two conserved histidines, His-230 and His-309, were mutated to phenylalanine and leucine. All four histidine mutants had k cat values 1000-fold lower than wild-type CNP-CF, but K m values were similar. Circular dichroism studies demonstrated that the low catalytic activities of the histidine mutants were not due to gross changes in secondary structure. Taken together, these results demonstrate that both histidines assume critical roles for catalysis.

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

Cited by 141 publications

References 29 publications

Transcription factor protein expression patterns by neural or neuronal progenitor cells of adult monkey subventricular zone

Transcription factor protein expression patterns by neural or neuronal progenitor cells of adult monkey subventricular zone

Juxtanodin: An oligodendroglial protein that promotes cellular arborization and 2′,3′-cyclic nucleotide-3′-phosphodiesterase trafficking

Identification of Essential Residues in 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase

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