High Density Distribution of Endoplasmic Reticulum Proteins and Mitochondria at Specialized Ca2+ Release Sites in Oligodendrocyte Processes

Simpson, Peter B.; Mehotra, Surabhi; Lange, G. David; Russell, James T.

doi:10.1074/jbc.272.36.22654

Cited by 163 publications

(123 citation statements)

References 37 publications

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“…At the subcellular level, it is found in the cell body as well as in processes but is excluded from the nuclear region (Sheppard et al, 1997;Simpson et al, 1997). Type 3 IP 3 R is found in the kidney, gastrointestinal tract, pancreatic islets (Nathanson et al, 1994;Taylor et al, 1999;Patel et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

Knockdown of the type 2 and 3 inositol 1,4,5-trisphosphate receptors suppresses muscarinic antinociception in mice

et al. 2007

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Several literature reports indicate that supraspinal cholinergic antinociception induced both directly, through muscarinic agonists, and indirectly, by enhancing ACh extracellular levels through cholinesterase inhibitors, is mediated by M 1 receptor stimulation, indicating that M 1 muscarinic receptor subtype plays an essential role in the modulation of pain perception (Bartolini et al., 1992;Iwamoto and Marion, 1993;Ghelardini et al., 1996;Naguib and Yaksh, 1997;Ghelardini et al., 2000). More recently, intracellular mechanisms involved in supraspinal muscarinic antinociception in a condition of acute thermal nociception in normal animals have been investigated. M 1 muscarinic receptors typically couple via the ␣ subunits of the G q/11 family to activate phospholipase C (PLC) (Caulfield and Birdsall, 1998), and the activation of PLC results in hydrolysis of phosphatidyl 4,5-bisphosphate and production of inositol-1,4,5 trisphosphate (IP 3 ) and diacylglycerol (DAG). The main effect of DAG is to activate protein kinase C; IP 3 mediates the release of calcium from intracellular stores by binding to its receptors (Berridge, 1993). The involvement of receptor-mediated activation of the PLC-IP 3 pathway in the increase in pain threshold produced by administration of cholinomimetics was directly demonstrated. The inhibition of the IP 3 synthesis by pretreatment with LiCl, and the blockade of IP 3 receptors (IP 3 R) by administration of the IP 3 R antagonist heparin, dose dependently prevented physostigmine and oxotremorine antinociception (Galeotti et al., 2003).The receptor that recognizes IP 3 was first characterized as a protein called P400 that was enriched in normal cerebella (Mikoshiba et al., 1997); two other types of IP 3 receptors were then cloned. The original IP 3 receptor was named type 1 IP 3 receptor (IP 3 R1), whereas the others were named type 2 IP 3 receptor (IP 3 R2) and type 3 IP 3 receptor (IP 3 R3) (Patel et al., 1999). IP 3 Rs are recognized as a protein family of tetrameric ligand-gated Ca 2ϩ channels that allow mobilization of intracellular Ca 2ϩ stores in response to activation of cell surface receptors linked to IP 3 generation (Berridge, 1993). IP 3 R monomers are large proteins with a calculated molecular mass of about 300 kDa and all three isoforms of IP 3 R share 60 -70% amino acid similarity (Taylor et al., 1999).The aim of the present study was to investigate the role of type 1, 2 and 3 IP 3 Rs in the intracellular mechanism of muscarinic antinociception at a supraspinal level. To this purpose, we inhibited the expression of each IP 3 receptor subtype by using antisense oligonucleotides targeting IP 3 R mRNA sequences that are unique in the mouse genome and therefore assured stringent target selectivity.

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Section: Discussionmentioning

confidence: 99%

Knockdown of the type 2 and 3 inositol 1,4,5-trisphosphate receptors suppresses muscarinic antinociception in mice

et al. 2007

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“…For example, initiation of global Ca 2+ waves in myocytes preferentially occurs in mitochondrion-poor regions of the cell (Boitier et al, 1999). A positive feedback effect of mitochondria on Ins(1,4,5)P3-mediated signals has been reported only in oligodendrocytes, in which Ca 2+ wave initiation and amplification sites are found in mitochondrion-rich regions of the cell (Simpson et al, 1997).…”

Section: The Calcium Signalling Hardware In Eggsmentioning

confidence: 99%

Calcium wave pacemakers in eggs

Dumollard

Carroll

Dupont

et al. 2002

Journal of Cell Science

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During the past 25 years, the characterization of sperm-triggered calcium signals in eggs has progressed from the discovery of a single calcium increase at fertilization in the medaka fish to the observation of repetitive calcium waves initiated by multiple meiotic calcium wave pacemakers in the ascidian. In eggs of all animal species, sperm-triggered inositol (1,4,5)-trisphosphate[Ins(1,4,5)P3] production regulates the vast array of calcium wave patterns observed in the different species. The spatial organization of calcium waves is driven either by the intracellular distribution of the calcium release machinery or by the localized and dynamic production of calcium-releasing second messengers. In the highly polarized egg cell, cortical endoplasmic reticulum (ER)-rich clusters act as pacemaker sites dedicated to the initiation of global calcium waves. The extensive ER network made of interconnected ER-rich domains supports calcium wave propagation throughout the egg. Fertilization triggers two types of calcium wave pacemakers depending on the species: in mice, the pacemaker site in the vegetal cortex of the egg is probably a site that has enhanced sensitivity to Ins(1,4,5)P3; in ascidians, the calcium wave pacemaker may rely on a local source of Ins(1,4,5)P3 production apposed to a cluster of ER in the vegetal cortex.

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“…The present study also found a large number of mitochondrial proteins in myelin of both human and mouse, including TCA cycle enzymes (e.g., aconitate hydratase) and respiratory chain enzymes (e.g., cytochrome c). Although the possibility remains that they represent a contamination of myelin (5, 7), mitochondria are known to localize in OL processes (31) and are present in peripheral nervous system (32) and CNS myelin (33). It is likely that myelin internode mitochondria provide the ATP that is needed for the expansion of myelin membranes during myelination.…”

Section: Protein Identification By Sequential 1-dimensional Page and mentioning

confidence: 99%

Human myelin proteome and comparative analysis with mouse myelin

Ishii¹,

Dutta

Wark³

et al. 2009

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

106

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Myelin, formed by oligodendrocytes (OLs) in the CNS, is critical for axonal functions, and its damage leads to debilitating neurological disorders such as multiple sclerosis. Understanding the molecular mechanisms of myelination and the pathogenesis of human myelin disease has been limited partly by the relative lack of identification and functional characterization of the repertoire of human myelin proteins. Here, we present a large-scale analysis of the myelin proteome, using the shotgun approach of 1-dimensional PAGE and liquid chromatography/tandem MS. Three hundred eight proteins were commonly identified from human and mouse myelin fractions. Comparative microarray analysis of human white and gray matter showed that transcripts of several of these were elevated in OL-rich white matter compared with gray matter, providing confidence in their detection in myelin. Comparison with other databases showed that 111 of the identified proteins/transcripts also were expressed in OLs, rather than in astrocytes or neurons. Comparison with 4 previous myelin proteomes further confirmed more than 50% of the identified proteins and revealed the presence of 163 additional proteins. A select group of identified proteins also were verified by immunoblotting. We classified the identified proteins into biological subgroups and discussed their relevance in myelin biogenesis and maintenance. Taken together, the study provides insights into the complexity of this metabolically active membrane and creates a valuable resource for future in-depth study of specific proteins in myelin with relevance to human demyelinating diseases.microarray ͉ oligodendrocyte ͉ proteomics ͉ mass spectrometry

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High Density Distribution of Endoplasmic Reticulum Proteins and Mitochondria at Specialized Ca2+ Release Sites in Oligodendrocyte Processes

Cited by 163 publications

References 37 publications

Knockdown of the type 2 and 3 inositol 1,4,5-trisphosphate receptors suppresses muscarinic antinociception in mice

Knockdown of the type 2 and 3 inositol 1,4,5-trisphosphate receptors suppresses muscarinic antinociception in mice

Calcium wave pacemakers in eggs

Human myelin proteome and comparative analysis with mouse myelin

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