Cellular neurochemical characterization and subcellular localization of phospholipase C β1 in rat brain

Montaña, Mario; Caño, Gontzal Garcı́a del; Jesús, Maider López de; González-Burguera, Imanol; Echeazarra, Leyre; Barrondo, Sergio; Sallés, Joan

doi:10.1016/j.neuroscience.2012.06.039

Cited by 34 publications

(54 citation statements)

References 102 publications

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“…The intensity of immunolabeling varied in the Purkinje cell stripes; for simplicity three categories of stripes were distinguished; intense, moderate, and faint/negative stripes. PLCβ1 + stripes had not been recognized previously with a proprietary antibody (Fukaya et al 2008), but recently they were shown with commercial PLCβ1 antibodies (Montaña et al 2012). Stripes of PLCβ3 + and PLCβ4 + Purkinje cells had been described in detail in the mouse cerebellum.…”

Section: Resultsmentioning

confidence: 99%

Differential distribution of phospholipase C beta isoforms and diaglycerol kinase-beta in rodents cerebella corroborates the division of unipolar brush cells into two major subtypes

et al. 2013

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Sublineage diversification of specific neural cell classes occurs in complex as well as simply organized regions of the central and peripheral nervous systems; the significance of the phenomenon, however, remains insufficiently understood. The unipolar brush cells (UBCs) are glutamatergic cerebellar interneurons that occur at high density in vestibulocerebellum. As they are classified into subsets that differ in chemical phenotypes, intrinsic properties, and lobular distribution, they represent a valuable neuronal model to study subclass diversification. In this study we show that cerebellar UBCs of adult rats and mice form two subclasses – type I and type II UBCs - defined by somatodendritic expression of calretinin (CR), mGluR1α, phospholipases PLCβ1 and PLCβ4, and diacylglycerol kinase-beta (DGKβ). We demonstrate that PLCβ1 is associated only with the CR+ type I UBCs while PLCβ4 and DGKβ are exclusively present in mGluR1α+ type II UBCs. Notably, all PLCβ4+ UBCs, representing about 2/3 of entire UBC population, also express mGluR1α. Furthermore, our data show that the sum of CR+ type I UBCs and mGluR1α+ type II UBCs accounts for the entire UBC class identified with Tbr2 immunolabeling. The two UBC subtypes also show a very different albeit somehow overlapping topographical distribution as illustrated by detailed cerebellar maps in this study. Our data not only complement and extend the previous knowledge on the diversity and subclass specificity of the chemical phenotypes within the UBC population but provide a new angle to the understanding of the signaling networks in type I and type II UBCs.

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Section: Resultsmentioning

confidence: 99%

Differential distribution of phospholipase C beta isoforms and diaglycerol kinase-beta in rodents cerebella corroborates the division of unipolar brush cells into two major subtypes

et al. 2013

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“…Since PtdIns(4,5) P 2 is the source of Ins(1,4,5) P 3 and PLC is also available in the nucleus, 9 , 11 , 18 , 30 it would be a natural course of event for Ins(1,4,5) P 3 to be produced from the PtdIns(4,5) P 2 of the vesicle membranes and open the nucleoplasmic Ca 2+ store vesicle Ins(1,4,5) P 3 R/Ca 2+ channels to induce Ca 2+ release. Underscoring this possibility and confirming the past results, 24 , 25 PtdIns(4,5) P 2 was shown to exist in the nucleoplasm (Fig.…”

Section: Resultsmentioning

confidence: 99%

Localization and projected role of phosphatidylinositol 4-kinases IIα and IIβ in inositol 1,4,5-trisphosphate-sensitive nucleoplasmic Ca²⁺store vesicles

Yoo¹,

Huh

et al. 2014

Nucleus

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Phosphatidylinositol (PI) kinases are key molecules that participate in the phosphoinositide signaling in the cytoplasm. Despite the accumulating evidence that supports the existence and operation of independent PI signaling system in the nucleus, the exact location of the PI kinases inside the nucleus is not well defined. Here we show that PI4-kinases IIα and IIβ, which play central roles in PI(4,5)P2 synthesis and PI signaling, are localized in numerous small nucleoplasmic vesicles that function as inositol 1,4,5-trisphosphate (Ins(1,4,5)P3)-sensitive Ca2+ stores. This is in accord with the past results that showed the localization of PI4(P)5-kinases that are essential in PI(4,5)P2 production and PI(4,5)P2 in nuclear matrix. Along with PI(4,5)P2 that also exists on the nucleoplasmic vesicle membranes, the localization of PI4-kinases IIα and IIβ in the nucleoplasmic vesicles strongly implicates the vesicles to the PI signaling as well as the Ins(1,4,5)P3-depenent Ca2+ signaling in the nucleus. Accordingly, the nucleoplasmic vesicles indeed release Ca2+ rapidly in response to Ins(1,4,5)P3. Further, the Ins(1,4,5)P3-induced Ca2+ release studies suggest that PI4KIIα and IIβ are localized near the Ins(1,4,5)P3 receptor (Ins(1,4,5)P3R)/Ca2+ channels on the Ca2+ store vesicle membranes. In view of the widespread presence of the Ins(1,4,5)P3-dependent Ca2+ store vesicles and the need to fine-control the nuclear Ca2+ concentrations at multiple sites along the chromatin fibers in the nucleus, the existence of the key PI enzymes in the Ins(1,4,5)P3-dependent nucleoplasmic Ca2+ store vesicles appears to be in perfect harmony with the physiological roles of the PI kinases in the nucleus.

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“…Rodent studies showed that PLCβ1 expression is undetectable by PCR from freshly isolated astrocytes, but it can be detected in established astrocytoma cell lines and C6 rat glioma cell lines [15, 20–23]. Interestingly, PLCβ1 expression is inducible from primary cultured astrocytes when stimulated with lipopolysaccharide [22].…”

Section: Discussionmentioning

confidence: 99%

“…Nucleus presence of PLCβ1 was demonstrated in cortical neurons of rabbit brain [15, 47], and evidence demonstrated that two isoforms have their preference in the cytosol and nuclear of C6 glioma cells, respectively [23]; PLCβ1 was also shown to be transited into the nucleus among C6 glial cell and Neuro2A cell (mouse neuroblastoma cell line) under stimuli [48]. Inside the nuclear, PLCβ1 is one of the key molecules that regulate nuclear inositides, and latest research concludes that nuclear inositides are independently regulated and nuclear inositol lipids themselves can modulate nuclear processes, such as transcription and pre-mRNA splicing, growth, proliferation, cell cycle regulation, and differentiation [49].…”

Section: Discussionmentioning

confidence: 99%

“…The PLCβ1 protein catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate (PIP2), which plays an important role in the intracellular signal transduction of extracellular signals, such as metabotropic glutamate. In rodent brain tissue, PLCβ1 is present in pyramidal neurons and interneurons, but is absent in astrocytes by immunohistochemistry [15, 18, 19]. However, PLCβ1 expression is detectable in cultured oligodendrocytes and astrocytes [20, 21].…”

Section: Introductionmentioning

confidence: 99%

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Phospholipase C Beta 1: a Candidate Signature Gene for Proneural Subtype High-Grade Glioma

Chang

Liu

et al. 2015

Mol Neurobiol

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Phospholipase C beta 1 (PLCβ1) expresses in gliomas and cultured glial cells, but its expression is barely detectable in normal glial cells. We analyzed data from Gene Expression Omnibus (GEO-GDSxxx), The Cancer Genome Atlas (TCGA), and the Repository for Molecular Brain Neoplasia Data (REMBRANDT) to explore the potential role of PLCβ1 as a biomarker in high-grade glioma (HGG). PLCβ1 expression is significantly higher in grade III gliomas than that in grade IV gliomas from GDS1815 (n = 24 vs. 76), GDS1962 (n = 19 vs. 81), and GDS1975 (n = 26 vs. 59). In GDS1815, PLCβ1 expression correlates with several known proneural (PN) signature genes; its expression from PN subtype (n = 15) is significantly higher than that from mesenchymal (Mes) subtype (n = 33) HGG. In GDS1962, PLCβ1 expression is the highest in nontumor brain tissue (n = 23) and is significantly higher than its expression in grade II gliomas [astrocytomas (n = 7) and oligodendrogliomas (n = 37)]. A Kaplan-Meier survival curve from a REMBRANDT cohort demonstrates that glioma patients with intermediate PLCβ1 expression (n = 103) survived significantly longer than PLCβ1 downregulated (2X) groups (n = 226). From TCGA data, PLCβ1 RNA-Seq signal inversely correlates with the pathological grades, and PLCβ1 expression in PN (n = 8) is of significantly higher levels than that in Mes (n = 8) subtypes of glioblastoma. The top 50 % of PLCβ1 expression subgroup (n = 294) of gliomas (grades II to IV merged) survived significantly longer than the low 50 percentile of the PLCβ1 expression subgroup (n = 293). p values are less than 0.05 for all these analyses. We conclude that PLCβ1 is a candidate signature gene for PN subtype HGG, and its expression inversely correlates with glioma pathological grade and is a potential prognostic factor.Electronic supplementary materialThe online version of this article (doi:10.1007/s12035-015-9518-2) contains supplementary material, which is available to authorized users.

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Cellular neurochemical characterization and subcellular localization of phospholipase C β1 in rat brain

Cited by 34 publications

References 102 publications

Differential distribution of phospholipase C beta isoforms and diaglycerol kinase-beta in rodents cerebella corroborates the division of unipolar brush cells into two major subtypes

Differential distribution of phospholipase C beta isoforms and diaglycerol kinase-beta in rodents cerebella corroborates the division of unipolar brush cells into two major subtypes

Localization and projected role of phosphatidylinositol 4-kinases IIα and IIβ in inositol 1,4,5-trisphosphate-sensitive nucleoplasmic Ca²⁺store vesicles

Phospholipase C Beta 1: a Candidate Signature Gene for Proneural Subtype High-Grade Glioma

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Cellular neurochemical characterization and subcellular localization of phospholipase C β1 in rat brain

Cited by 34 publications

References 102 publications

Differential distribution of phospholipase C beta isoforms and diaglycerol kinase-beta in rodents cerebella corroborates the division of unipolar brush cells into two major subtypes

Differential distribution of phospholipase C beta isoforms and diaglycerol kinase-beta in rodents cerebella corroborates the division of unipolar brush cells into two major subtypes

Localization and projected role of phosphatidylinositol 4-kinases IIα and IIβ in inositol 1,4,5-trisphosphate-sensitive nucleoplasmic Ca2+store vesicles

Phospholipase C Beta 1: a Candidate Signature Gene for Proneural Subtype High-Grade Glioma

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Localization and projected role of phosphatidylinositol 4-kinases IIα and IIβ in inositol 1,4,5-trisphosphate-sensitive nucleoplasmic Ca²⁺store vesicles