WordNet
- the mathematical process of obtaining the derivative of a function
- a discrimination between things as different and distinct; "it is necessary to make a distinction between love and infatuation" (同)distinction
PrepTutorEJDIC
- 神経単位,神経細胞,ニューロン,ノイロン
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- 1. 分化（レチノイン酸）症候群 differentiation retinoic acid syndrome
- 2. 幹細胞の概要 overview of stem cells
- 3. 分化型甲状腺癌：マネージメントの概要 differentiated thyroid cancer overview of management
- 4. 松果体部腫瘍 pineal gland masses
- 5. 原発不明の低分化癌 poorly differentiated cancer from an unknown primary site
English Journal
- Hsp90 activity is necessary to acquire a proper neuronal polarization.
- Benitez MJ1, Sanchez-Ponce D2, Garrido JJ3, Wandosell F4.Author information 1Centro de Biología Molecular "Severo Ochoa", CSIC-UAM, Univ. Autonoma de Madrid, 28049 Madrid, Spain; Dpto Química Física Aplicada, Univ. Autónoma de Madrid, 28049 Madrid, Spain.2Instituto Cajal, CSIC, Department of Molecular, Cellular and Developmental Neurobiology, Madrid 28002, Spain.3Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Madrid, Spain; Instituto Cajal, CSIC, Department of Molecular, Cellular and Developmental Neurobiology, Madrid 28002, Spain. Electronic address: jjgarrido@cajal.csic.es.4Centro de Biología Molecular "Severo Ochoa", CSIC-UAM, Univ. Autonoma de Madrid, 28049 Madrid, Spain; Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Madrid, Spain. Electronic address: fwandosell@cbm.uam.es.AbstractChaperones are critical for the folding and regulation of a wide array of cellular proteins. Heat Shock Proteins (Hsps) are the most representative group of chaperones. Hsp90 represents up to 1-2% of soluble protein. Although the Hsp90 role is being studied in neurodegenerative diseases, its role in neuronal differentiation remains mostly unknown. Since neuronal polarity mechanisms depend on local stability and degradation, we asked whether Hsp90 could be a regulator of axonal polarity and growth. Thus, we studied the role of Hsp90 activity in a well established model of cultured hippocampal neurons using an Hsp90 specific inhibitor, 17-AAG. Our present data shows that Hsp90 inhibition at different developmental stages disturbs neuronal polarity formation or axonal elongation. Hsp90 inhibition during the first 3h in culture promotes multiple axon morphology, while this inhibition after 3h slows down axonal elongation. Hsp90 inhibition was accompanied by decreased Akt and GSK3 expression, as well as, a reduced Akt activity. In parallel, we detected an alteration of kinesin-1 subcellular distribution. Moreover, these effects were seconded by changes in Hsp70/Hsc70 subcellular localization that seem to compensate the lack of Hsp90 activity. In conclusion, our data strongly suggests that Hsp90 activity is necessary to control the expression, activity or location of specific kinases and motor proteins during the axon specification and axon elongation processes. Even more, our data demonstrate the existence of a "time-window" for axon specification in this model of cultured neurons after which the inhibition of Hsp90 only affects axonal elongation mechanisms.
- Biochimica et biophysica acta.Biochim Biophys Acta.2014 Feb;1843(2):245-52. doi: 10.1016/j.bbamcr.2013.11.013. Epub 2013 Nov 25.
- Chaperones are critical for the folding and regulation of a wide array of cellular proteins. Heat Shock Proteins (Hsps) are the most representative group of chaperones. Hsp90 represents up to 1-2% of soluble protein. Although the Hsp90 role is being studied in neurodegenerative diseases, its role in
- PMID 24286867
- Neo-innervation of a bioengineered intestinal smooth muscle construct around chitosan scaffold.
- Zakhem E1, Raghavan S1, Bitar KN2.Author information 1Wake Forest Institute for Regenerative Medicine, Wake Forest School of Medicine, Winston-Salem, NC, United States; Virginia Tech-Wake Forest School of Biomedical Engineering and Sciences, Winston-Salem, United States.2Wake Forest Institute for Regenerative Medicine, Wake Forest School of Medicine, Winston-Salem, NC, United States; Virginia Tech-Wake Forest School of Biomedical Engineering and Sciences, Winston-Salem, United States. Electronic address: kbitar@wakehealth.edu.AbstractNeuromuscular disorders of the gut result in disturbances in gastrointestinal transit. The objective of this study was to evaluate the neo-innervation of smooth muscle in an attempt to restore lost innervation. We have previously shown the potential use of composite chitosan scaffolds as support for intestinal smooth muscle constructs. However, the constructs lacked neuronal component. Here, we bioengineered innervated colonic smooth muscle constructs using rabbit colon smooth muscle and enteric neural progenitor cells. We also bioengineered smooth muscle only tissue constructs using colonic smooth muscle cells. The constructs were placed next to each other around tubular chitosan scaffolds and left in culture. Real time force generation conducted on the intrinsically innervated smooth muscle constructs showed differentiated functional neurons. The bioengineered smooth muscle only constructs became neo-innervated. The neo-innervation results were confirmed by immunostaining assays. Chitosan supported (1) the differentiation of neural progenitor cells in the constructs and (2) the neo-innervation of non-innervated smooth muscle around the same scaffold.
- Biomaterials.Biomaterials.2014 Feb;35(6):1882-9. doi: 10.1016/j.biomaterials.2013.11.049. Epub 2013 Dec 7.
- Neuromuscular disorders of the gut result in disturbances in gastrointestinal transit. The objective of this study was to evaluate the neo-innervation of smooth muscle in an attempt to restore lost innervation. We have previously shown the potential use of composite chitosan scaffolds as support for
- PMID 24315576
- Expression analysis of ATAD3 isoforms in rodent and human cell lines and tissues.
- Li S1, Lamarche F2, Charton R3, Delphin C4, Gires O5, Hubstenberger A6, Schlattner U1, Rousseau D7.Author information 1INSERM U1055, Laboratoire de Bioénergétique Fondamentale et Appliquée (LBFA) et SFR Biologie Environnementale et Systémique (BEeSy), Joseph Fourier University, Grenoble F-38041, France.2INSERM U1055, Laboratoire de Bioénergétique Fondamentale et Appliquée (LBFA) et SFR Biologie Environnementale et Systémique (BEeSy), Joseph Fourier University, Grenoble F-38041, France; Grenoble University Hospital, Grenoble F-38043, France.3Département de Microbiologie et Infectiologie, Faculté de Médecine, Université de Sherbrooke, Sherbrooke, QC J1J3P9, Canada.4Grenoble Institut des Neurosciences (GIN), INSERM U836-UJF-CEA-CHU, Université Joseph Fourier, 38706 La Tronche Cedex, France.5Ludwig-Maximilians-Universität München, ENT Research, ENT Clinics, Marchioninistr. 15, D-81377 München, Germany.6Department of Cell and Developmental Biology, University of Wisconsin, Aurora, CO 80045, USA.7INSERM U1055, Laboratoire de Bioénergétique Fondamentale et Appliquée (LBFA) et SFR Biologie Environnementale et Systémique (BEeSy), Joseph Fourier University, Grenoble F-38041, France. Electronic address: Denis.Rousseau@ujf-grenoble.fr.AbstractATAD3 (ATPase family AAA-Domain containing protein 3) is a mitochondrial inner membrane ATPase with unknown but vital functions. Initial researches have focused essentially on the major p66-ATAD3 isoform, but other proteins and mRNAs are described in the data banks. Using a set of anti-peptide antibodies and by the use of rodent and human cell lines and organs, we tried to detail ATAD3 gene expression profiles and to verify the existence of the various ATAD3 isoforms. In rodent, the single ATAD3 gene is expressed as a major isoform of 67kDa, (ATAD3l; long), in all cells and organs studied. A second isoform, p57-ATAD3s (small), is expressed specifically throughout brain development and in adult, and overexpressed around the peri-natal period. p57-ATAD3s is also expressed in neuronal and glial rodent cell lines, and during in vitro differentiation of primary cultured rat oligodendrocytes. Other smaller isoforms were also detected in a tissue-specific manner. In human and primates, ATAD3 paralogues are encoded by three genes (ATAD3A, 3B and 3C), each of them presenting several putative variants. Analyzing the expression of ATAD3A and ATAD3B with four specific anti-peptide antibodies, and comparing their expressions with in vitro expressed ATAD3 cDNAs, we were able to observe and define five isoforms. In particular, the previously described p72-ATAD3B is confirmed to be in certain cases a phosphorylated form of ATAD3As. Moreover, we observed that the ATAD3As phosphorylation level is regulated by insulin and serum. Finally, exploring ATAD3 mRNA expression, we confirmed the existence of an alternative splicing in rodent and of several mRNA isoforms in human. Considering these observations, we propose the development of a uniform denomination for ATAD3 isoforms in rodent and human.
- Gene.Gene.2014 Feb 1;535(1):60-9. doi: 10.1016/j.gene.2013.10.062. Epub 2013 Nov 14.
- ATAD3 (ATPase family AAA-Domain containing protein 3) is a mitochondrial inner membrane ATPase with unknown but vital functions. Initial researches have focused essentially on the major p66-ATAD3 isoform, but other proteins and mRNAs are described in the data banks. Using a set of anti-peptide antib
- PMID 24239551
Japanese Journal
- Calcium dysregulation contributes to neurodegeneration in FTLD patient iPSC-derived neurons.
- Scientific Reports 6, 2016-10-10
- NAID 120005850272
- Effective Cellular Morphology Analysis for Differentiation Processes by a Fluorescent 1,3a,6a-Triazapentalene Derivative Probe in Live Cells
- PLOS ONE 11(8), e0160625, 2016-08-04
- NAID 120005851071
- P2Y4 Nucleotide Receptor in Neuronal Precursors Induces Glutamatergic Subtype Markers in Their Descendant Neurons
- Stem Cell Reports 6, 474-482, 2016-04-12
- NAID 120005767003
Related Links
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★リンクテーブル★
| リンク元 | 「神経細胞分化」「ニューロン分化」 |
| 関連記事 | 「neuronal」「differentiation」 |
「神経細胞分化」
「ニューロン分化」
「neuronal」
- 神経細胞の、ニューロンの、神経型の
「differentiation」
- n.