Differential RIP antigen (CNPase) expression in peripheral ensheathing glia

Toma, Jeremy S.; McPhail, Lowell T.; Ramer, Matt S.

doi:10.1016/j.brainres.2006.12.053

Cited by 26 publications

(31 citation statements)

References 43 publications

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“…However, there have been controversial reports regarding the expression in OECs and Schwann cells (Toma et al 2007;Santos-Silva and Cavalcante 2001;Ramón-Cueto and Nieto-Sampedro 1992). In the present study, we found CNPase in canine but not in rat OECs using the same antibody.…”

Section: Species-specific Expression Of Cnpase In Adult Canine Olfactcontrasting

confidence: 59%

“…Since it was reported recently that CNPase in situ is expressed by rat Schwann cells but not by OECs (Toma et al 2007), we used the same antibodies and the immunocytochemical protocols for immunstaining of adult rat tissue. In confirmation of previous results, it was found that adult rat OECs did not express detectable amounts of CNPase.…”

Section: Adult Canine But Not Rat Olfactory Ensheathing Cells Displaymentioning

confidence: 99%

“…In myelinating Schwann cells, CNPase is confined to non-compact myelin of the SchmidtLantermann incisures. While expression of CNPase has also been demonstrated in non-myelinating glia, such as Remak Schwann cells, terminal Schwann cells, and satellite cells, there have been controversial results regarding the expression of CNPase in OECs (Toma et al 2007;SantosSilva and Cavalcante 2001;Ramón-Cueto and NietoSampedro 1992). Since analysis of CNPase expression in many studies was restricted to the protein level, the conflicting results might have also arisen from distinct antibody specificities or protocols.…”

Section: Introductionmentioning

confidence: 96%

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Defining the morphological phenotype: 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) is a novel marker for in situ detection of canine but not rat olfactory ensheathing cells

Omar

Bock²,

Kreutzer³

et al. 2011

Cell Tissue Res

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Olfactory ensheathing cells (OECs) are the non-myelinating glial cells of the olfactory nerves and bulb. The fragmentary characterization of OECs in situ during normal development may be due to their small size requiring intricate ultrastructural analysis and to the fact that available markers for in situ detection are either expressed only by OEC subpopulations or lost during development. In the present study, we searched for markers with stable expression in OECs and investigated the spatiotemporal distribution of CNPase, an early oligodendrocyte/Schwann cell marker, in comparison with the prototype marker p75(NTR). Anti-CNPase antibodies labeled canine but not rat OECs in situ, while Schwann cells and oligodendrocytes were positive in both species. CNPase immunoreactivity in the dog was confined to all OECs throughout the postnatal development and associated with the entire cell body, including its finest processes, while p75(NTR) was mainly detected in perineural cells and only in some neonatal OECs. Adult olfactory bulb slices displayed CNPase expression after 4 and 10 days, while p75(NTR) was detectable only after 10 days in vitro. Finally, treatment of purified adult canine OECs with fibroblast growth factor-2 significantly reduced CNPase expression at the protein and mRNA level. Taken together, we conclude that CNPase but not p75(NTR) is a stable marker suitable for in situ visualization of OECs that will facilitate their light-microscopic characterization and challenge our general view of OEC marker expression in situ. The fact that canine but not rat OECs expressed CNPase supports the idea that glia from large animals differs substantially from rodents.

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Section: Species-specific Expression Of Cnpase In Adult Canine Olfactcontrasting

confidence: 59%

Section: Adult Canine But Not Rat Olfactory Ensheathing Cells Displaymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

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Defining the morphological phenotype: 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) is a novel marker for in situ detection of canine but not rat olfactory ensheathing cells

Omar

Bock²,

Kreutzer³

et al. 2011

Cell Tissue Res

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“…Open bar indicates peptide sequences for anti-Atrn antibody. associated protein 2 (MAP-2, a marker for dendrites and cell bodies; dilution 1:1,000), synaptophysin (a marker for presynaptic terminals; dilution 1:1,000), glutamic acid decarboxylase 65/67 (GAD65/67, a marker for GABAnergic neurons; dilution 1:1,000), glial fibrillary acidic protein (GFAP, a marker for mature astrocytes; dilution 1:2,000), RIP [recently identified as 2Ј,3Ј-cyclic nucleotide 3Ј-phosphodiesterase, CNPase (Toma et al, 2007), a marker for oligodendrocytes; dilution 1:1,000] OX42 [identified as type 3 complement receptor (Perry and Gordon, 1987), a marker for microglia; dilution 1:200], or tyrosine hydroxylase [TH, a marker for dopaminergic (DA) neurons; dilution 1:2,000] antibodies. Primary antibodies used in the present study are summarized in Table 1.…”

Section: Immunohistochemistrymentioning

confidence: 99%

Attractin/mahogany protein expression in the rodent central nervous system

Nakadate

Sakakibara

Ueda

2008

J of Comparative Neurology

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Attractin/Mahogany protein (Atrn) is known to be involved in a number of physiological and neuropathological events. Although the ubiquitous distribution of atrn mRNA has been described in neurons, lack of detailed information concerning the cellular and subcellular localization of protein product is impeding understanding of the role of Atrn. The present study immunohistochemically examined distributions of Atrn in rat and mouse central nervous systems (CNSs) by using a novel antibody for Atrn. Atrn was intensely expressed in most neurons and dendrites of large neurons, such as cortical pyramidal neurons and cerebellar Purkinje neurons. Intense Atrn expression was also observed in the neuropil of gray matter in many regions of the CNS, such as the main and accessory olfactory bulb, cerebral cortex, caudate putamen, dorsal lateral geniculate nucleus, medial eminence, superior colliculus, hippocampus, dentate gyrus, and layers 1 and 2 of the spinal cord. Furthermore, we found that astrocytes, microglia, and ependymal cells also express Atrn protein. Immunoelectron microscopy showed the subcellular distribution of Atrn in the plasma membrane of cell soma, dendrites, and spines in neurons and in the cytoplasmic membrane of Golgi apparatus, endoplasmic reticulum, and mitochondria in neurons and glial cells. These findings indicate that Atrn is more widely expressed throughout the CNS than previously reported, and expression of Atrn by various cell types suggests that Atrn may serve multiple functions in the CNS.

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“…The Cnp1 promoter is also active in nonmyelinating Schwann cells (Toma et al, 2007) that engulf multiple small C-fiber axons to form a Remak bundle. Here, Cre recombination was demonstrated indirectly by strong immunostaining of phosphorylated AKT kinase (Fig.…”

Section: "Remak Myelin"mentioning

confidence: 99%

Elevated Phosphatidylinositol 3,4,5-Trisphosphate in Glia Triggers Cell-Autonomous Membrane Wrapping and Myelination

Goebbels¹,

Oltrogge²,

Kemper³

et al. 2010

Journal of Neuroscience

302

292

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In the developing nervous system, constitutive activation of the AKT/mTOR (mammalian target of rapamycin) pathway in myelinating glial cells is associated with hypermyelination of the brain, but is reportedly insufficient to drive myelination by Schwann cells. We have hypothesized that it requires additional mechanisms downstream of NRG1/ErbB signaling to trigger myelination in the peripheral nervous system. Here, we demonstrate that elevated levels of phosphatidylinositol 3,4,5-trisphosphate (PIP3) have developmental effects on both oligodendrocytes and Schwann cells. By generating conditional mouse mutants, we found that Pten-deficient Schwann cells are enhanced in number and can sort and myelinate axons with calibers well below 1 m. Unexpectedly, mutant glial cells also spirally enwrap C-fiber axons within Remak bundles and even collagen fibrils, which lack any membrane surface. Importantly, PIP3-dependent hypermyelination of central axons, which is observed when targeting Pten in oligodendrocytes, can also be induced after tamoxifenmediated Cre recombination in adult mice. We conclude that it requires distinct PIP3 effector mechanisms to trigger axonal wrapping. That myelin synthesis is not restricted to early development but can occur later in life is relevant to developmental disorders and myelin disease.

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Differential RIP antigen (CNPase) expression in peripheral ensheathing glia

Cited by 26 publications

References 43 publications

Defining the morphological phenotype: 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) is a novel marker for in situ detection of canine but not rat olfactory ensheathing cells

Defining the morphological phenotype: 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) is a novel marker for in situ detection of canine but not rat olfactory ensheathing cells

Attractin/mahogany protein expression in the rodent central nervous system

Elevated Phosphatidylinositol 3,4,5-Trisphosphate in Glia Triggers Cell-Autonomous Membrane Wrapping and Myelination

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