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Article ; Online: Urinary lumirubin excretion in jaundiced preterm neonates during phototherapy with blue light-emitting diode vs. green fluorescent lamp.

Uchida, Yumiko / Takahashi, Yukihiro / Kurata, Chikara / Morimoto, Yukihiro / Ohtani, Eishin / Tosaki, Asako / Kumagai, Akiko / Greimel, Peter / Nishikubo, Toshiya / Miyawaki, Atsushi

Scientific reports

2023 Volume 13, Issue 1, Page(s) 18359

Abstract: Phototherapy converts lipophilic unconjugated bilirubin to hydrophilic bilirubin photoisomers, such as lumirubin. We comparatively used a blue light-emitting diode (LED) and a green fluorescent lamp (FL) as light sources for phototherapy of ... ...

Abstract	Phototherapy converts lipophilic unconjugated bilirubin to hydrophilic bilirubin photoisomers, such as lumirubin. We comparatively used a blue light-emitting diode (LED) and a green fluorescent lamp (FL) as light sources for phototherapy of hyperbilirubinemic preterm neonates with the aim of examining potential differences in urinary lumirubin excretion between these two wavelengths. Urinary lumirubin levels were measured using a fluorescence assay with blue light exposure in the presence of the unconjugated bilirubin-inducible fluorescent protein UnaG, and denoted as urinary UnaG-bound bilirubin (UUB)/creatinine (Cr) (μg/mg Cr). Preterm neonates born at ≤ 33 weeks gestational age and treated with phototherapy were subjected to this study. The maximum UUB/Cr level during phototherapy per device intensity was compared between neonates treated with the blue LED and the green FL. A total of 61 neonates were examined to determine the maximum UUB/Cr levels. The median of maximum UUB/Cr excretion per light intensity of each device (μg/mg Cr/μW/cm
MeSH term(s)	Infant, Newborn ; Humans ; Phototherapy/methods ; Jaundice ; Jaundice, Neonatal/therapy ; Bilirubin/metabolism
Chemical Substances	lumirubin (83664-21-5) ; Bilirubin (RFM9X3LJ49)
Language	English
Publishing date	2023-10-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-023-45147-7
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Noninvasive monitoring of bilirubin photoisomer excretion during phototherapy.

Uchida, Yumiko / Takahashi, Yukihiro / Morimoto, Yukihiro / Greimel, Peter / Tosaki, Asako / Kumagai, Akiko / Nishikubo, Toshiya / Miyawaki, Atsushi

Scientific reports

2022 Volume 12, Issue 1, Page(s) 11798

Abstract: Lumirubin is the most prevalently excreted hydrophilic bilirubin photoisomer in phototherapy for neonatal jaundice caused by excess hydrophobic unconjugated bilirubin (ZZ-bilirubin). We developed a simple method to estimate the amount of lumirubin by ... ...

Abstract	Lumirubin is the most prevalently excreted hydrophilic bilirubin photoisomer in phototherapy for neonatal jaundice caused by excess hydrophobic unconjugated bilirubin (ZZ-bilirubin). We developed a simple method to estimate the amount of lumirubin by monitoring the reverse photoisomerization of lumirubin to ZZ-bilirubin. Although lumirubin formation was long considered irreversible, exposure to blue light in the presence of the fluorescent protein UnaG, which binds specifically and tightly to ZZ-bilirubin, enables the reverse photoisomerization of lumirubin. This reaction was first detected using a fluorescence assay of neonatal urine sampled during phototherapy and purified lumirubin. The phenomenon of reverse photoisomerization of lumirubin was validated using liquid chromatography-mass spectrometry, which confirmed that lumirubin is reconverted to ZZ-bilirubin in the presence of UnaG. Analyses of 20 urine samples from 17 neonates revealed a significant correlation (correlation coefficient [r] = 0.978; 95% confidence interval 0.867-0.979; P < .001) between lumirubin and ZZ-bilirubin concentration before and after reverse photoisomerization. In general, the rate of photo-reconversion of lumirubin to ZZ-bilirubin is approximately 40%. In conclusion, we demonstrate here that lumirubin can be photo-reconverted to ZZ-bilirubin via exposure to blue light in the presence of UnaG. Utilizing this approach, urinary lumirubin levels can be estimated using an easy-to-perform fluorescence assay.
MeSH term(s)	Bilirubin/metabolism ; Humans ; Infant, Newborn ; Jaundice, Neonatal/therapy ; Light ; Mass Spectrometry ; Phototherapy/methods
Chemical Substances	Bilirubin (RFM9X3LJ49)
Language	English
Publishing date	2022-07-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-16180-9
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Article ; Online: Gene expression profiling in neuronal cells identifies a different type of transcriptome modulated by NF-Y.

Yamanaka, Tomoyuki / Miyazaki, Haruko / Tosaki, Asako / Maity, Sankar N / Shimogori, Tomomi / Hattori, Nobutaka / Nukina, Nobuyuki

Scientific reports

2020 Volume 10, Issue 1, Page(s) 21714

Abstract: A heterotrimeric transcription factor NF-Y is crucial for cell-cycle progression in various types of cells. In contrast, studies using NF-YA knockout mice have unveiled its essential role in endoplasmic reticulum (ER) homeostasis in neuronal cells. ... ...

Abstract	A heterotrimeric transcription factor NF-Y is crucial for cell-cycle progression in various types of cells. In contrast, studies using NF-YA knockout mice have unveiled its essential role in endoplasmic reticulum (ER) homeostasis in neuronal cells. However, whether NF-Y modulates a different transcriptome to mediate distinct cellular functions remains obscure. Here, we knocked down NF-Y in two types of neuronal cells, neuro2a neuroblastoma cells and mouse brain striatal cells, and performed gene expression profiling. We found that down-regulated genes preferentially contained NF-Y-binding motifs in their proximal promoters, and notably enriched genes related to ER functions rather than those for cell cycle. This contrasts with the profiling data of HeLa and embryonic stem cells in which distinct down-regulation of cell cycle-related genes was observed. Clustering analysis further identified several functional clusters where populations of the down-regulated genes were highly distinct. Further analyses using chromatin immunoprecipitation and RNA-seq data revealed that the transcriptomic difference was not correlated with DNA binding of NF-Y but with splicing of NF-YA. These data suggest that neuronal cells have a different type of transcriptome in which ER-related genes are dominantly modulated by NF-Y, and imply that NF-YA splicing alteration could be involved in this cell type-specific gene modulation.
MeSH term(s)	Alternative Splicing ; Animals ; CCAAT-Binding Factor/genetics ; CCAAT-Binding Factor/physiology ; Cell Cycle/genetics ; Endoplasmic Reticulum/genetics ; Gene Expression Profiling ; HeLa Cells ; Homeostasis/genetics ; Humans ; Mice ; Neurons/metabolism ; Neurons/physiology ; RNA Splicing ; Transcriptome/genetics
Chemical Substances	CCAAT-Binding Factor
Language	English
Publishing date	2020-12-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-78682-8
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Article: Genome‐wide analyses in neuronal cells reveal that upstream transcription factors regulate lysosomal gene expression

Yamanaka, Tomoyuki / Tosaki, Asako / Kurosawa, Masaru / Shimogori, Tomomi / Hattori, Nobutaka / Nukina, Nobuyuki

FEBS journal. 2016 Mar., v. 283, no. 6

2016

Abstract: The upstream transcription factors (USFs) USF1 and USF2 are ubiquitously expressed transcription factors that are characterized by a conserved basic helix‐loop‐helix/leucine zipper DNA‐binding domain. They form homo‐ or heterodimers, and recognize E‐box ... ...

Abstract	The upstream transcription factors (USFs) USF1 and USF2 are ubiquitously expressed transcription factors that are characterized by a conserved basic helix‐loop‐helix/leucine zipper DNA‐binding domain. They form homo‐ or heterodimers, and recognize E‐box motifs to modulate gene expression. They are known to regulate diverse cellular functions, including the cell cycle, immune responses and glucose/lipid metabolism, but their roles in neuronal cells remain to be clarified. Here, we performed chromatin immunoprecipitation of USF1 from mouse brain cortex. Subsequent promoter array analysis (ChIP‐chip) indicated that USF1 exclusively bound to the CACGTG E‐box motifs in the proximal promoter regions. Importantly, functional annotation of the USF1‐binding targets revealed an enrichment of genes related to lysosomal functions. Gene expression array analysis using a neuronal cell line subsequently revealed that knockdown of USFs de‐regulated lysosomal gene expression. Altered expression was validated by quantitative RT‐PCR, supporting the conclusion that USFs regulate lysosomal gene expression. Furthermore, USF knockdown slightly increased LysoTracker Red staining, implying a role for USFs in modulating lysosomal homeostasis. Together, our comprehensive genome‐scale analyses identified lysosomal genes as targets of USFs in neuronal cells, suggesting a potential additional pathway of lysosomal regulation. DATABASE: The data for the gene expression array and ChIP‐chip have been submitted to the Gene Expression Omnibus (GEO) under accession numbers GSE76615 and GSE76616, respectively.
Keywords	DNA-binding domains ; brain ; cell cycle ; chromatin ; cortex ; gene expression ; genes ; glucose ; homeostasis ; immune response ; lipid metabolism ; mice ; neurons ; precipitin tests ; promoter regions ; reverse transcriptase polymerase chain reaction ; staining ; transcription factors
Language	English
Dates of publication	2016-03
Size	p. 1077-1087.
Publishing place	Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
Document type	Article
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13650
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Genome-wide analyses in neuronal cells reveal that upstream transcription factors regulate lysosomal gene expression.

Yamanaka, Tomoyuki / Tosaki, Asako / Kurosawa, Masaru / Shimogori, Tomomi / Hattori, Nobutaka / Nukina, Nobuyuki

The FEBS journal

2016 Volume 283, Issue 6, Page(s) 1077–1087

Abstract: Unlabelled: The upstream transcription factors (USFs) USF1 and USF2 are ubiquitously expressed transcription factors that are characterized by a conserved basic helix-loop-helix/leucine zipper DNA-binding domain. They form homo- or heterodimers, and ... ...

Abstract	Unlabelled: The upstream transcription factors (USFs) USF1 and USF2 are ubiquitously expressed transcription factors that are characterized by a conserved basic helix-loop-helix/leucine zipper DNA-binding domain. They form homo- or heterodimers, and recognize E-box motifs to modulate gene expression. They are known to regulate diverse cellular functions, including the cell cycle, immune responses and glucose/lipid metabolism, but their roles in neuronal cells remain to be clarified. Here, we performed chromatin immunoprecipitation of USF1 from mouse brain cortex. Subsequent promoter array analysis (ChIP-chip) indicated that USF1 exclusively bound to the CACGTG E-box motifs in the proximal promoter regions. Importantly, functional annotation of the USF1-binding targets revealed an enrichment of genes related to lysosomal functions. Gene expression array analysis using a neuronal cell line subsequently revealed that knockdown of USFs de-regulated lysosomal gene expression. Altered expression was validated by quantitative RT-PCR, supporting the conclusion that USFs regulate lysosomal gene expression. Furthermore, USF knockdown slightly increased LysoTracker Red staining, implying a role for USFs in modulating lysosomal homeostasis. Together, our comprehensive genome-scale analyses identified lysosomal genes as targets of USFs in neuronal cells, suggesting a potential additional pathway of lysosomal regulation. Database: The data for the gene expression array and ChIP-chip have been submitted to the Gene Expression Omnibus (GEO) under accession numbers GSE76615 and GSE76616, respectively.
MeSH term(s)	Animals ; Binding Sites/genetics ; Cell Line ; Cerebral Cortex/metabolism ; Chromatin Immunoprecipitation ; E-Box Elements ; Gene Expression Regulation ; Gene Knockdown Techniques ; Genome-Wide Association Study ; Lysosomes/genetics ; Lysosomes/metabolism ; Male ; Mice ; Mice, Inbred CBA ; Neurons/metabolism ; Oligonucleotide Array Sequence Analysis ; Promoter Regions, Genetic ; Upstream Stimulatory Factors/antagonists & inhibitors ; Upstream Stimulatory Factors/genetics ; Upstream Stimulatory Factors/metabolism
Chemical Substances	Upstream Stimulatory Factors ; Usf1 protein, mouse ; Usf2 protein, mouse
Language	English
Publishing date	2016-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13650
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Antigen testing for COVID-19 using image-based assessment of oral specimens

medRxiv

Abstract: While numerous diagnostic tests for COVID-19 have been developed for clinical and public health use, most of them provide binary or one-dimensional information on SARS-CoV-2 infection in pursuit of speed and ease of use. As their readouts are largely ... ...

Abstract	While numerous diagnostic tests for COVID-19 have been developed for clinical and public health use, most of them provide binary or one-dimensional information on SARS-CoV-2 infection in pursuit of speed and ease of use. As their readouts are largely dependent on the specimen collection procedure, reliable diagnosis is still difficult. Here we report the development of a prototypical method for the immunocytochemical diagnosis of SARS-CoV-2 infection using oral specimens and fluorescent nanobodies against the viral spike and nucleocapsid proteins. Our cytological approach for the detection of SARS-CoV-2 infection was validated by our finding that at least half of SARS-CoV-2 RNAs in oral specimens were localized in the cellular fraction. Mapping antigens on sampled cells provided qualitative image data to which appropriate statistical texture analysis could be applied for the quantitative assessment of SARS-CoV-2 infectious status. A comprehensive comparative analysis revealed that oral cavity swabbing by medical workers provides specimens for COVID-19 diagnosis that yield comparable diagnostic accuracy as self-collected saliva specimens. Our diagnostic strategy may enable medical workers to acquire a wealth of information on virus-human cell interactions for multifaceted insight into COVID-19.
Keywords	covid19
Language	English
Publishing date	2022-05-27
Publisher	Cold Spring Harbor Laboratory Press
Document type	Article ; Online
DOI	10.1101/2022.05.27.22274752
Database	COVID19

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Article ; Online: Large-scale RNA interference screening in mammalian cells identifies novel regulators of mutant huntingtin aggregation.

Yamanaka, Tomoyuki / Wong, Hon Kit / Tosaki, Asako / Bauer, Peter O / Wada, Koji / Kurosawa, Masaru / Shimogori, Tomomi / Hattori, Nobutaka / Nukina, Nobuyuki

PloS one

2014 Volume 9, Issue 4, Page(s) e93891

Abstract: In polyglutamine (polyQ) diseases including Huntington's disease (HD), mutant proteins containing expanded polyQ stretch form aggregates in neurons. Genetic or RNAi screenings in yeast, C. elegans or Drosophila have identified multiple genes modifying ... ...

Abstract	In polyglutamine (polyQ) diseases including Huntington's disease (HD), mutant proteins containing expanded polyQ stretch form aggregates in neurons. Genetic or RNAi screenings in yeast, C. elegans or Drosophila have identified multiple genes modifying polyQ aggregation, a few of which are confirmed effective in mammals. However, the overall molecular mechanism underlying polyQ protein aggregation in mammalian cells still remains obscure. We here perform RNAi screening in mouse neuro2a cells to identify mammalian modifiers for aggregation of mutant huntingtin, a causative protein of HD. By systematic cell transfection and automated cell image analysis, we screen ∼ 12000 shRNA clones and identify 111 shRNAs that either suppress or enhance mutant huntingtin aggregation, without altering its gene expression. Classification of the shRNA-targets suggests that genes with various cellular functions such as gene transcription and protein phosphorylation are involved in modifying the aggregation. Subsequent analysis suggests that, in addition to the aggregation-modifiers sensitive to proteasome inhibition, some of them, such as a transcription factor Tcf20, and kinases Csnk1d and Pik3c2a, are insensitive to it. As for Tcf20, which contains polyQ stretches at N-terminus, its binding to mutant huntingtin aggregates is observed in neuro2a cells and in HD model mouse neurons. Notably, except Pik3c2a, the rest of the modifiers identified here are novel. Thus, our first large-scale RNAi screening in mammalian system identifies previously undescribed genetic players that regulate mutant huntingtin aggregation by several, possibly mammalian-specific mechanisms.
MeSH term(s)	Animals ; High-Throughput Screening Assays ; Huntingtin Protein ; Mice ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/metabolism ; RNA Interference ; RNA, Small Interfering/genetics ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Htt protein, mouse ; Huntingtin Protein ; Nerve Tissue Proteins ; Nuclear Proteins ; RNA, Small Interfering ; Tcf20 protein, mouse ; Transcription Factors ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Pik3c2a protein, mouse (EC 2.7.1.137)
Language	English
Publishing date	2014-04-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0093891
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Article ; Online: Parallel homodimer structures of the extracellular domains of the voltage-gated sodium channel β4 subunit explain its role in cell-cell adhesion.

Shimizu, Hideaki / Tosaki, Asako / Ohsawa, Noboru / Ishizuka-Katsura, Yoshiko / Shoji, Shisako / Miyazaki, Haruko / Oyama, Fumitaka / Terada, Takaho / Shirouzu, Mikako / Sekine, Shun-Ichi / Nukina, Nobuyuki / Yokoyama, Shigeyuki

The Journal of biological chemistry

2017 Volume 292, Issue 32, Page(s) 13428–13440

Abstract: Voltage-gated sodium channels (VGSCs) are transmembrane proteins required for the generation of action potentials in excitable cells and essential for propagating electrical impulses along nerve cells. VGSCs are complexes of a pore-forming α subunit and ... ...

Abstract	Voltage-gated sodium channels (VGSCs) are transmembrane proteins required for the generation of action potentials in excitable cells and essential for propagating electrical impulses along nerve cells. VGSCs are complexes of a pore-forming α subunit and auxiliary β subunits, designated as β1/β1B-β4 (encoded by
MeSH term(s)	Animals ; CHO Cells ; Cell Adhesion ; Cricetulus ; Crystallography, X-Ray ; Cysteine/chemistry ; Cystine/chemistry ; Dimerization ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Mice ; Models, Molecular ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Protein Conformation ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Voltage-Gated Sodium Channel beta-4 Subunit/chemistry ; Voltage-Gated Sodium Channel beta-4 Subunit/genetics ; Voltage-Gated Sodium Channel beta-4 Subunit/metabolism
Chemical Substances	Peptide Fragments ; Recombinant Fusion Proteins ; Recombinant Proteins ; SCN4B protein, human ; Scn4b protein, mouse ; Voltage-Gated Sodium Channel beta-4 Subunit ; Cystine (48TCX9A1VT) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2017-06-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M117.786509
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Mutant huntingtin fragment selectively suppresses Brn-2 POU domain transcription factor to mediate hypothalamic cell dysfunction.

Yamanaka, Tomoyuki / Tosaki, Asako / Miyazaki, Haruko / Kurosawa, Masaru / Furukawa, Yoshiaki / Yamada, Mizuki / Nukina, Nobuyuki

Human molecular genetics

2010 Volume 19, Issue 11, Page(s) 2099–2112

Abstract: In polyglutamine diseases including Huntington's disease (HD), mutant proteins containing expanded polyglutamine stretches form nuclear aggregates in neurons. Although analysis of their disease models suggested a significance of transcriptional ... ...

Abstract	In polyglutamine diseases including Huntington's disease (HD), mutant proteins containing expanded polyglutamine stretches form nuclear aggregates in neurons. Although analysis of their disease models suggested a significance of transcriptional dysregulation in these diseases, how it mediates the specific neuronal cell dysfunction remains obscure. Here we performed a comprehensive analysis of altered DNA binding of multiple transcription factors using R6/2 HD model mice brains that express an N-terminal fragment of mutant huntingtin (mutant Nhtt). We found a reduction of DNA binding of Brn-2, a POU domain transcription factor involved in differentiation and function of hypothalamic neurosecretory neurons. We provide evidence supporting that Brn-2 loses its function through two pathways, its sequestration by mutant Nhtt and its reduced transcription, leading to reduced expression of hypothalamic neuropeptides. In contrast to Brn-2, its functionally related protein, Brn-1, was not sequestered by mutant Nhtt but was upregulated in R6/2 brain, except in hypothalamus. Our data indicate that functional suppression of Brn-2 together with a region-specific lack of compensation by Brn-1 mediates hypothalamic cell dysfunction by mutant Nhtt.
MeSH term(s)	Animals ; DNA/metabolism ; Electrophoretic Mobility Shift Assay ; Homeodomain Proteins/genetics ; Homeodomain Proteins/metabolism ; Huntingtin Protein ; Huntington Disease/genetics ; Huntington Disease/metabolism ; Huntington Disease/pathology ; Hypothalamus/cytology ; Hypothalamus/metabolism ; Immunohistochemistry ; In Situ Hybridization ; Male ; Mice ; Microscopy, Fluorescence ; Mutation/genetics ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Neurons/pathology ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; POU Domain Factors/genetics ; POU Domain Factors/metabolism ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	Homeodomain Proteins ; Htt protein, mouse ; Huntingtin Protein ; Nerve Tissue Proteins ; Nuclear Proteins ; POU Domain Factors ; transcription factor Brn-2 ; DNA (9007-49-2)
Language	English
Publishing date	2010-02-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddq087
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Article ; Online: Loss of aPKCλ in differentiated neurons disrupts the polarity complex but does not induce obvious neuronal loss or disorientation in mouse brains.

Yamanaka, Tomoyuki / Tosaki, Asako / Kurosawa, Masaru / Akimoto, Kazunori / Hirose, Tomonori / Ohno, Shigeo / Hattori, Nobutaka / Nukina, Nobuyuki

PloS one

2013 Volume 8, Issue 12, Page(s) e84036

Abstract: Cell polarity plays a critical role in neuronal differentiation during development of the central nervous system (CNS). Recent studies have established the significance of atypical protein kinase C (aPKC) and its interacting partners, which include PAR-3, ...

Abstract	Cell polarity plays a critical role in neuronal differentiation during development of the central nervous system (CNS). Recent studies have established the significance of atypical protein kinase C (aPKC) and its interacting partners, which include PAR-3, PAR-6 and Lgl, in regulating cell polarization during neuronal differentiation. However, their roles in neuronal maintenance after CNS development remain unclear. Here we performed conditional deletion of aPKCλ, a major aPKC isoform in the brain, in differentiated neurons of mice by camk2a-cre or synapsinI-cre mediated gene targeting. We found significant reduction of aPKCλ and total aPKCs in the adult mouse brains. The aPKCλ deletion also reduced PAR-6β, possibly by its destabilization, whereas expression of other related proteins such as PAR-3 and Lgl-1 was unaffected. Biochemical analyses suggested that a significant fraction of aPKCλ formed a protein complex with PAR-6β and Lgl-1 in the brain lysates, which was disrupted by the aPKCλ deletion. Notably, the aPKCλ deletion mice did not show apparent cell loss/degeneration in the brain. In addition, neuronal orientation/distribution seemed to be unaffected. Thus, despite the polarity complex disruption, neuronal deletion of aPKCλ does not induce obvious cell loss or disorientation in mouse brains after cell differentiation.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Blotting, Western ; Brain/metabolism ; Brain/pathology ; Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules/metabolism ; Cell Cycle Proteins ; Cell Differentiation ; Cell Polarity ; Female ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Immunoenzyme Techniques ; Immunoprecipitation ; Integrases/metabolism ; Isoenzymes/physiology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurogenesis/physiology ; Neurons/metabolism ; Neurons/pathology ; Protein Kinase C/physiology ; RNA, Messenger/genetics ; Real-Time Polymerase Chain Reaction ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cell Adhesion Molecules ; Cell Cycle Proteins ; Glycoproteins ; Isoenzymes ; LGL1 protein, mouse ; Par6 protein, mouse ; Pard3 protein, mouse ; RNA, Messenger ; Protein Kinase C (EC 2.7.11.13) ; protein kinase C lambda (EC 2.7.11.13) ; Cre recombinase (EC 2.7.7.-) ; Integrases (EC 2.7.7.-)
Language	English
Publishing date	2013-12-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0084036
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