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  1. Article ; Online: Lipids and lysosomes.

    Hamer, Isabelle / Van Beersel, Guillaume / Arnould, Thierry / Jadot, Michel

    Current drug metabolism

    2012  Volume 13, Issue 10, Page(s) 1371–1387

    Abstract: Lysosomes are cytoplasmic organelles delimited by a single membrane and filled with a variety of hydrolytic enzymes active at acidic pH and collectively capable to degrade the vast majority of macromolecules entering lysosomes via endocytosis, ... ...

    Abstract Lysosomes are cytoplasmic organelles delimited by a single membrane and filled with a variety of hydrolytic enzymes active at acidic pH and collectively capable to degrade the vast majority of macromolecules entering lysosomes via endocytosis, phagocytosis or autophagy. In this review, we describe the lipid composition and the dynamic properties of lysosomal membrane, the main delivery pathways of lipids to lysosomes and their catabolism inside lysosomes. Then, we present the consequences of a lipid accumulation as seen in various lysosomal storage diseases on lysosomal functions. Finally, we discuss about the possible involvement of lysosomes in lipotoxicity.
    MeSH term(s) Animals ; Cell Membrane/metabolism ; Humans ; Lipid Metabolism ; Lysosomes/metabolism ; Mitochondria/metabolism
    Language English
    Publishing date 2012-09-12
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 2064815-7
    ISSN 1875-5453 ; 1389-2002
    ISSN (online) 1875-5453
    ISSN 1389-2002
    DOI 10.2174/138920012803762684
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5584: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
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  2. Article ; Online: Different molecular mechanisms involved in spontaneous and oxidative stress-induced mitochondrial fragmentation in tripeptidyl peptidase-1 (TPP-1)-deficient fibroblasts.

    Van Beersel, Guillaume / Tihon, Eliane / Demine, Stéphane / Hamer, Isabelle / Jadot, Michel / Arnould, Thierry

    Bioscience reports

    2013  Volume 33, Issue 2, Page(s) e00023

    Abstract: NCLs (neuronal ceroid lipofuscinoses) form a group of eight inherited autosomal recessive diseases characterized by the intralysosomal accumulation of autofluorescent pigments, called ceroids. Recent data suggest that the pathogenesis of NCL is ... ...

    Abstract NCLs (neuronal ceroid lipofuscinoses) form a group of eight inherited autosomal recessive diseases characterized by the intralysosomal accumulation of autofluorescent pigments, called ceroids. Recent data suggest that the pathogenesis of NCL is associated with the appearance of fragmented mitochondria with altered functions. However, even if an impairement in the autophagic pathway has often been evoked, the molecular mechanisms leading to mitochondrial fragmentation in response to a lysosomal dysfunction are still poorly understood. In this study, we show that fibroblasts that are deficient for the TPP-1 (tripeptidyl peptidase-1), a lysosomal hydrolase encoded by the gene mutated in the LINCL (late infantile NCL, CLN2 form) also exhibit a fragmented mitochondrial network. This morphological alteration is accompanied by an increase in the expression of the protein BNIP3 (Bcl2/adenovirus E1B 19 kDa interacting protein 3) as well as a decrease in the abundance of mitofusins 1 and 2, two proteins involved in mitochondrial fusion. Using RNAi (RNA interference) and quantitative analysis of the mitochondrial morphology, we show that the inhibition of BNIP3 expression does not result in an increase in the reticulation of the mitochondrial population in LINCL cells. However, this protein seems to play a key role in cell response to mitochondrial oxidative stress as it sensitizes mitochondria to antimycin A-induced fragmentation. To our knowledge, our results bring the first evidence of a mechanism that links TPP-1 deficiency and oxidative stress-induced changes in mitochondrial morphology.
    MeSH term(s) Aminopeptidases/deficiency ; Aminopeptidases/genetics ; Autophagy/genetics ; Cells, Cultured ; Ceroid/metabolism ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/deficiency ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/genetics ; Fibroblasts/metabolism ; Fibroblasts/pathology ; Humans ; Lysosomes/metabolism ; Lysosomes/pathology ; Mitochondria/drug effects ; Mitochondria/metabolism ; Mitochondria/pathology ; Neuronal Ceroid-Lipofuscinoses/metabolism ; Neuronal Ceroid-Lipofuscinoses/pathology ; Oxidative Stress/genetics ; Serine Proteases/deficiency ; Serine Proteases/genetics
    Chemical Substances Ceroid ; Serine Proteases (EC 3.4.-) ; Aminopeptidases (EC 3.4.11.-) ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (EC 3.4.14.-) ; tripeptidyl-peptidase 1 (EC 3.4.14.9)
    Language English
    Publishing date 2013-02-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 764946-0
    ISSN 1573-4935 ; 0144-8463
    ISSN (online) 1573-4935
    ISSN 0144-8463
    DOI 10.1042/BSR20120104
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1676: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Different molecular mechanisms involved in spontaneous and oxidative stress-induced mitochondrial fragmentation in tripeptidyl peptidase-1 (TPP-1)-deficient fibroblasts

    Guillaume Van Beersel / Eliane Tihon / Stéphane Demine / Isabelle Hamer / Michel Jadot / Thierry Arnould

    Bioscience Reports, Vol 33, Iss 2, p e

    2013  Volume 00023

    Abstract: NCLs (neuronal ceroid lipofuscinoses) form a group of eight inherited autosomal recessive diseases characterized by the intralysosomal accumulation of autofluorescent pigments, called ceroids. Recent data suggest that the pathogenesis of NCL is ... ...

    Abstract NCLs (neuronal ceroid lipofuscinoses) form a group of eight inherited autosomal recessive diseases characterized by the intralysosomal accumulation of autofluorescent pigments, called ceroids. Recent data suggest that the pathogenesis of NCL is associated with the appearance of fragmented mitochondria with altered functions. However, even if an impairement in the autophagic pathway has often been evoked, the molecular mechanisms leading to mitochondrial fragmentation in response to a lysosomal dysfunction are still poorly understood. In this study, we show that fibroblasts that are deficient for the TPP-1 (tripeptidyl peptidase-1), a lysosomal hydrolase encoded by the gene mutated in the LINCL (late infantile NCL, CLN2 form) also exhibit a fragmented mitochondrial network. This morphological alteration is accompanied by an increase in the expression of the protein BNIP3 (Bcl2/adenovirus E1B 19 kDa interacting protein 3) as well as a decrease in the abundance of mitofusins 1 and 2, two proteins involved in mitochondrial fusion. Using RNAi (RNA interference) and quantitative analysis of the mitochondrial morphology, we show that the inhibition of BNIP3 expression does not result in an increase in the reticulation of the mitochondrial population in LINCL cells. However, this protein seems to play a key role in cell response to mitochondrial oxidative stress as it sensitizes mitochondria to antimycin A-induced fragmentation. To our knowledge, our results bring the first evidence of a mechanism that links TPP-1 deficiency and oxidative stress-induced changes in mitochondrial morphology.
    Keywords Bcl2/adenovirus E1B 19 kDa protein interacting protein 3 (BNIP3) ; confocal microscopy ; late infantile neuronal ceroid lipofuscinosis (LINCL) ; mitochondrion ; mitofusins ; Biology (General) ; QH301-705.5 ; Science ; Q ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
    Subject code 580
    Language English
    Publishing date 2013-02-01T00:00:00Z
    Publisher Portland Press Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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