LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 4 of total 4

Search options

  1. Article ; Online: Mouse mammary tumor virus in human breast cancer red herring or smoking gun?

    Mason, Andrew L / Gilady, Susanna Y / Mackey, John R

    The American journal of pathology

    2011  Volume 179, Issue 4, Page(s) 1588–1590

    MeSH term(s) Breast Neoplasms/pathology ; Breast Neoplasms/virology ; Disease Progression ; Female ; Genes, env/genetics ; Humans ; Mammary Tumor Virus, Mouse/genetics
    Language English
    Publishing date 2011-08-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2943-9
    ISSN 1525-2191 ; 0002-9440
    ISSN (online) 1525-2191
    ISSN 0002-9440
    DOI 10.1016/j.ajpath.2011.08.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.76: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).

    Gilady, Susanna Y / Bui, Michael / Lynes, Emily M / Benson, Matthew D / Watts, Russell / Vance, Jean E / Simmen, Thomas

    Cell stress & chaperones

    2010  Volume 15, Issue 5, Page(s) 619–629

    Abstract: Protein secretion from the endoplasmic reticulum (ER) requires the enzymatic activity of chaperones and oxidoreductases that fold polypeptides and form disulfide bonds within newly synthesized proteins. The best-characterized ER redox relay depends on ... ...

    Abstract Protein secretion from the endoplasmic reticulum (ER) requires the enzymatic activity of chaperones and oxidoreductases that fold polypeptides and form disulfide bonds within newly synthesized proteins. The best-characterized ER redox relay depends on the transfer of oxidizing equivalents from molecular oxygen through ER oxidoreductin 1 (Ero1) and protein disulfide isomerase to nascent polypeptides. The formation of disulfide bonds is, however, not the sole function of ER oxidoreductases, which are also important regulators of ER calcium homeostasis. Given the role of human Ero1alpha in the regulation of the calcium release by inositol 1,4,5-trisphosphate receptors during the onset of apoptosis, we hypothesized that Ero1alpha may have a redox-sensitive localization to specific domains of the ER. Our results show that within the ER, Ero1alpha is almost exclusively found on the mitochondria-associated membrane (MAM). The localization of Ero1alpha on the MAM is dependent on oxidizing conditions within the ER. Chemical reduction of the ER environment, but not ER stress in general leads to release of Ero1alpha from the MAM. In addition, the correct localization of Ero1alpha to the MAM also requires normoxic conditions, but not ongoing oxidative phosphorylation.
    MeSH term(s) Blotting, Western ; Cell Line ; HeLa Cells ; Humans ; Intracellular Membranes/metabolism ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Microscopy, Fluorescence ; Mitochondria/metabolism ; Oxidoreductases/genetics ; Oxidoreductases/metabolism
    Chemical Substances Membrane Glycoproteins ; ERO1A protein, human (EC 1.-) ; Oxidoreductases (EC 1.-)
    Language English
    Publishing date 2010-02-26
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1362749-1
    ISSN 1466-1268 ; 1355-8145
    ISSN (online) 1466-1268
    ISSN 1355-8145
    DOI 10.1007/s12192-010-0174-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4797: 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)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Rab32 modulates apoptosis onset and mitochondria-associated membrane (MAM) properties.

    Bui, Michael / Gilady, Susanna Y / Fitzsimmons, Ross E B / Benson, Matthew D / Lynes, Emily M / Gesson, Kevin / Alto, Neal M / Strack, Stefan / Scott, John D / Simmen, Thomas

    The Journal of biological chemistry

    2010  Volume 285, Issue 41, Page(s) 31590–31602

    Abstract: The mitochondria-associated membrane (MAM) has emerged as an endoplasmic reticulum (ER) signaling hub that accommodates ER chaperones, including the lectin calnexin. At the MAM, these chaperones control ER homeostasis but also play a role in the onset of ...

    Abstract The mitochondria-associated membrane (MAM) has emerged as an endoplasmic reticulum (ER) signaling hub that accommodates ER chaperones, including the lectin calnexin. At the MAM, these chaperones control ER homeostasis but also play a role in the onset of ER stress-mediated apoptosis, likely through the modulation of ER calcium signaling. These opposing roles of MAM-localized chaperones suggest the existence of mechanisms that regulate the composition and the properties of ER membrane domains. Our results now show that the GTPase Rab32 localizes to the ER and mitochondria, and we identify this protein as a regulator of MAM properties. Consistent with such a role, Rab32 modulates ER calcium handling and disrupts the specific enrichment of calnexin on the MAM, while not affecting the ER distribution of protein-disulfide isomerase and mitofusin-2. Furthermore, Rab32 determines the targeting of PKA to mitochondrial and ER membranes and through its overexpression or inactivation increases the phosphorylation of Bad and of Drp1. Through a combination of its functions as a PKA-anchoring protein and a regulator of MAM properties, the activity and expression level of Rab32 determine the speed of apoptosis onset.
    MeSH term(s) Apoptosis/physiology ; Calcium/metabolism ; Calnexin/genetics ; Calnexin/metabolism ; Cyclic AMP-Dependent Protein Kinases/genetics ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; GTP Phosphohydrolases ; HeLa Cells ; Humans ; Intracellular Membranes/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein Disulfide-Isomerases/genetics ; Protein Disulfide-Isomerases/metabolism ; Unfolded Protein Response/physiology ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
    Chemical Substances Membrane Proteins ; Mitochondrial Proteins ; Molecular Chaperones ; Calnexin (139873-08-8) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; GTP Phosphohydrolases (EC 3.6.1.-) ; MFN2 protein, human (EC 3.6.1.-) ; Rab32 protein, human (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2) ; Protein Disulfide-Isomerases (EC 5.3.4.1) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2010-07-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; 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.M110.101584
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article: Rab32 Modulates Apoptosis Onset and Mitochondria-associated Membrane (MAM) Properties

    Bui, Michael / Gilady, Susanna Y / Fitzsimmons, Ross E.B / Benson, Matthew D / Lynes, Emily M / Gesson, Kevin / Alto, Neal M / Strack, Stefan / Scott, John D / Simmen, Thomas

    Journal of biological chemistry. 2010 Oct. 8, v. 285, no. 41

    2010  

    Abstract: The mitochondria-associated membrane (MAM) has emerged as an endoplasmic reticulum (ER) signaling hub that accommodates ER chaperones, including the lectin calnexin. At the MAM, these chaperones control ER homeostasis but also play a role in the onset of ...

    Abstract The mitochondria-associated membrane (MAM) has emerged as an endoplasmic reticulum (ER) signaling hub that accommodates ER chaperones, including the lectin calnexin. At the MAM, these chaperones control ER homeostasis but also play a role in the onset of ER stress-mediated apoptosis, likely through the modulation of ER calcium signaling. These opposing roles of MAM-localized chaperones suggest the existence of mechanisms that regulate the composition and the properties of ER membrane domains. Our results now show that the GTPase Rab32 localizes to the ER and mitochondria, and we identify this protein as a regulator of MAM properties. Consistent with such a role, Rab32 modulates ER calcium handling and disrupts the specific enrichment of calnexin on the MAM, while not affecting the ER distribution of protein-disulfide isomerase and mitofusin-2. Furthermore, Rab32 determines the targeting of PKA to mitochondrial and ER membranes and through its overexpression or inactivation increases the phosphorylation of Bad and of Drp1. Through a combination of its functions as a PKA-anchoring protein and a regulator of MAM properties, the activity and expression level of Rab32 determine the speed of apoptosis onset.
    Language English
    Dates of publication 2010-1008
    Size p. 31590-31602.
    Publishing place American Society for Biochemistry and Molecular Biology
    Document type Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 4' 65/118: Show issues
    Z 6.2: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top