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  1. Article ; Online: New therapies for Pompe disease: are we closer to a cure?

    Puertollano, Rosa / Raben, Nina

    The Lancet. Neurology

    2021  Volume 20, Issue 12, Page(s) 973–975

    MeSH term(s) Enzyme Replacement Therapy ; Glycogen Storage Disease Type II/drug therapy ; Humans
    Language English
    Publishing date 2021-11-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2081241-3
    ISSN 1474-4465 ; 1474-4422
    ISSN (online) 1474-4465
    ISSN 1474-4422
    DOI 10.1016/S1474-4422(21)00358-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5955: 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)

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  2. Article ; Online: Intravital imaging of muscle damage and response to therapy in a model of Pompe disease.

    Meena, Naresh K / Ng, Yeap / Randazzo, Davide / Weigert, Roberto / Puertollano, Rosa / Raben, Nina

    Clinical and translational medicine

    2024  Volume 14, Issue 3, Page(s) e1561

    MeSH term(s) Humans ; Glycogen Storage Disease Type II/diagnostic imaging ; Glycogen Storage Disease Type II/drug therapy ; Diagnostic Imaging ; Intravital Microscopy ; Muscles
    Language English
    Publishing date 2024-03-06
    Publishing country United States
    Document type Letter ; Research Support, N.I.H., Intramural ; Comment
    ZDB-ID 2697013-2
    ISSN 2001-1326 ; 2001-1326
    ISSN (online) 2001-1326
    ISSN 2001-1326
    DOI 10.1002/ctm2.1561
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: AAV-mediated delivery of secreted acid α-glucosidase with enhanced uptake corrects neuromuscular pathology in Pompe mice.

    Meena, Naresh K / Randazzo, Davide / Raben, Nina / Puertollano, Rosa

    JCI insight

    2023  Volume 8, Issue 16

    Abstract: Gene therapy is under advanced clinical development for several lysosomal storage disorders. Pompe disease, a debilitating neuromuscular illness affecting infants, children, and adults with different severity, is caused by a deficiency of lysosomal ... ...

    Abstract Gene therapy is under advanced clinical development for several lysosomal storage disorders. Pompe disease, a debilitating neuromuscular illness affecting infants, children, and adults with different severity, is caused by a deficiency of lysosomal glycogen-degrading enzyme acid α-glucosidase (GAA). Here, we demonstrated that adeno-associated virus-mediated (AAV-mediated) systemic gene transfer reversed glycogen storage in all key therapeutic targets - skeletal and cardiac muscles, the diaphragm, and the central nervous system - in both young and severely affected old Gaa-knockout mice. Furthermore, the therapy reversed secondary cellular abnormalities in skeletal muscle, such as those in autophagy and mTORC1/AMPK signaling. We used an AAV9 vector encoding a chimeric human GAA protein with enhanced uptake and secretion to facilitate efficient spread of the expressed protein among multiple target tissues. These results lay the groundwork for a future clinical development strategy in Pompe disease.
    MeSH term(s) Child ; Mice ; Humans ; Animals ; alpha-Glucosidases/genetics ; Glycogen Storage Disease Type II/genetics ; Glycogen Storage Disease Type II/therapy ; Glycogen Storage Disease Type II/pathology ; Dependovirus/genetics ; Dependovirus/metabolism ; Genetic Vectors/genetics ; Mice, Knockout ; Glycogen/metabolism
    Chemical Substances alpha-Glucosidases (EC 3.2.1.20) ; Glycogen (9005-79-2)
    Language English
    Publishing date 2023-08-22
    Publishing country United States
    Document type Journal Article
    ISSN 2379-3708
    ISSN (online) 2379-3708
    DOI 10.1172/jci.insight.170199
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Pompe Disease: New Developments in an Old Lysosomal Storage Disorder.

    Meena, Naresh K / Raben, Nina

    Biomolecules

    2020  Volume 10, Issue 9

    Abstract: Pompe disease, also known as glycogen storage disease type II, is caused by the lack or deficiency of a single enzyme, lysosomal acid alpha-glucosidase, leading to severe cardiac and skeletal muscle myopathy due to progressive accumulation of glycogen. ... ...

    Abstract Pompe disease, also known as glycogen storage disease type II, is caused by the lack or deficiency of a single enzyme, lysosomal acid alpha-glucosidase, leading to severe cardiac and skeletal muscle myopathy due to progressive accumulation of glycogen. The discovery that acid alpha-glucosidase resides in the lysosome gave rise to the concept of lysosomal storage diseases, and Pompe disease became the first among many monogenic diseases caused by loss of lysosomal enzyme activities. The only disease-specific treatment available for Pompe disease patients is enzyme replacement therapy (ERT) which aims to halt the natural course of the illness. Both the success and limitations of ERT provided novel insights in the pathophysiology of the disease and motivated the scientific community to develop the next generation of therapies that have already progressed to the clinic.
    MeSH term(s) Autophagy/genetics ; Enzyme Replacement Therapy/methods ; Genetic Therapy/methods ; Glycogen/metabolism ; Glycogen Storage Disease Type II/enzymology ; Glycogen Storage Disease Type II/genetics ; Glycogen Storage Disease Type II/therapy ; Humans ; Lysosomal Storage Diseases/enzymology ; Lysosomal Storage Diseases/genetics ; Lysosomal Storage Diseases/therapy ; Lysosomes/metabolism ; Muscle, Skeletal/metabolism ; alpha-Glucosidases/deficiency ; alpha-Glucosidases/genetics ; alpha-Glucosidases/therapeutic use
    Chemical Substances Glycogen (9005-79-2) ; alpha-Glucosidases (EC 3.2.1.20)
    Language English
    Publishing date 2020-09-18
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom10091339
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Editorial for focused issue "Pompe disease: from basics to current and emerging therapies".

    Puertollano, Rosa / Raben, Nina

    Annals of translational medicine

    2019  Volume 7, Issue 13, Page(s) 275

    Language English
    Publishing date 2019-08-01
    Publishing country China
    Document type Journal Article
    ZDB-ID 2893931-1
    ISSN 2305-5847 ; 2305-5839
    ISSN (online) 2305-5847
    ISSN 2305-5839
    DOI 10.21037/atm.2019.05.57
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  6. Article: Pompe disease: how to solve many problems with one solution.

    Puertollano, Rosa / Raben, Nina

    Annals of translational medicine

    2018  Volume 6, Issue 15, Page(s) 313

    Language English
    Publishing date 2018-08-29
    Publishing country China
    Document type Editorial ; Comment
    ZDB-ID 2893931-1
    ISSN 2305-5847 ; 2305-5839
    ISSN (online) 2305-5847
    ISSN 2305-5839
    DOI 10.21037/atm.2018.06.52
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: SnapShot: Lysosomal Storage Diseases.

    Martina, José A / Raben, Nina / Puertollano, Rosa

    Cell

    2020  Volume 180, Issue 3, Page(s) 602–602.e1

    Abstract: Lysosomal storage diseases (LSDs) represent a group of monogenic inherited metabolic disorders characterized by the progressive accumulation of undegraded substrates inside lysosomes, resulting in aberrant lysosomal activity and homeostasis. This ... ...

    Abstract Lysosomal storage diseases (LSDs) represent a group of monogenic inherited metabolic disorders characterized by the progressive accumulation of undegraded substrates inside lysosomes, resulting in aberrant lysosomal activity and homeostasis. This SnapShot summarizes the intracellular localization and function of proteins implicated in LSDs. Common aspects of LSD pathogenesis and the major current therapeutic approaches are noted. To view this SnapShot, open or download the PDF.
    MeSH term(s) Animals ; Autophagy ; Enzymes/metabolism ; Eukaryotic Cells/metabolism ; Homeostasis ; Humans ; Lysosomal Storage Diseases/classification ; Lysosomal Storage Diseases/metabolism ; Lysosomal Storage Diseases/pathology ; Lysosomal Storage Diseases/therapy ; Lysosomal Membrane Proteins/metabolism ; Lysosomes/metabolism
    Chemical Substances Enzymes ; Lysosomal Membrane Proteins
    Language English
    Publishing date 2020-02-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2020.01.017
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: 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)
    Zs.MG 58: Show issues

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  8. Article ; Online: Impaired autophagy: The collateral damage of lysosomal storage disorders.

    Myerowitz, Rachel / Puertollano, Rosa / Raben, Nina

    EBioMedicine

    2020  Volume 63, Page(s) 103166

    Abstract: Lysosomal storage disorders (LSDs), which number over fifty, are monogenically inherited and caused by mutations in genes encoding proteins that are involved in lysosomal function. Lack of the functional protein results in storage of a distinctive ... ...

    Abstract Lysosomal storage disorders (LSDs), which number over fifty, are monogenically inherited and caused by mutations in genes encoding proteins that are involved in lysosomal function. Lack of the functional protein results in storage of a distinctive material within the lysosomes, which for years was thought to determine the pathophysiology of the disorder. However, our current view posits that the primary storage material disrupts the normal role of the lysosome in the autophagic pathway resulting in the secondary storage of autophagic debris. It is this "collateral damage" which is common to the LSDs but nonetheless intricately nuanced in each. We have selected five LSDs resulting from defective proteins that govern widely different lysosomal functions including glycogen degradation (Pompe), lysosomal transport (Cystinosis), lysosomal trafficking (Danon), glycolipid degradation (Gaucher) and an unidentified function (Batten) and argue that despite the disparate functions, these proteins, when mutant, all impair the autophagic process uniquely.
    MeSH term(s) Animals ; Autophagy/genetics ; Biomarkers ; Cystinosis/etiology ; Cystinosis/metabolism ; Cystinosis/pathology ; Disease Management ; Disease Susceptibility ; Humans ; Lysosomal Storage Diseases/diagnosis ; Lysosomal Storage Diseases/etiology ; Lysosomal Storage Diseases/metabolism ; Lysosomal Storage Diseases/therapy ; Lysosomes/metabolism ; Organ Specificity/genetics
    Chemical Substances Biomarkers
    Language English
    Publishing date 2020-12-17
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 2851331-9
    ISSN 2352-3964
    ISSN (online) 2352-3964
    DOI 10.1016/j.ebiom.2020.103166
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 7090: 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)

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  9. Article: Pros and cons of different ways to address dysfunctional autophagy in Pompe disease.

    Lim, Jeong-A / Meena, Naresh Kumar / Raben, Nina

    Annals of translational medicine

    2019  Volume 7, Issue 13, Page(s) 279

    Abstract: Autophagy is a major intracellular self-digestion process that brings cytoplasmic materials to the lysosome for degradation. Defective autophagy has been linked to a broad range of human disorders, including cancer, diabetes, neurodegeneration, ... ...

    Abstract Autophagy is a major intracellular self-digestion process that brings cytoplasmic materials to the lysosome for degradation. Defective autophagy has been linked to a broad range of human disorders, including cancer, diabetes, neurodegeneration, autoimmunity, cardiovascular diseases, and myopathies. In Pompe disease, a severe neuromuscular disorder, disturbances in autophagic process manifest themselves as progressive accumulation of undegraded cellular debris in the diseased muscle cells. A growing body of evidence has connected this defect to the decline in muscle function and muscle resistance to the currently available treatment-enzyme replacement therapy (ERT). Both induction and inhibition of autophagy have been tested in pre-clinical studies in a mouse model of the disease. Here, we discuss strengths and weaknesses of different approaches to address autophagic dysfunction in the context of Pompe disease.
    Language English
    Publishing date 2019-08-01
    Publishing country China
    Document type Journal Article ; Review
    ZDB-ID 2893931-1
    ISSN 2305-5847 ; 2305-5839
    ISSN (online) 2305-5847
    ISSN 2305-5839
    DOI 10.21037/atm.2019.03.51
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Enzyme Replacement Therapy Can Reverse Pathogenic Cascade in Pompe Disease.

    Meena, Naresh Kumar / Ralston, Evelyn / Raben, Nina / Puertollano, Rosa

    Molecular therapy. Methods & clinical development

    2020  Volume 18, Page(s) 199–214

    Abstract: Pompe disease, a deficiency of glycogen-degrading lysosomal acid alpha-glucosidase (GAA), is a disabling multisystemic illness that invariably affects skeletal muscle in all patients. The patients still carry a heavy burden of the disease, despite the ... ...

    Abstract Pompe disease, a deficiency of glycogen-degrading lysosomal acid alpha-glucosidase (GAA), is a disabling multisystemic illness that invariably affects skeletal muscle in all patients. The patients still carry a heavy burden of the disease, despite the currently available enzyme replacement therapy. We have previously shown that progressive entrapment of glycogen in the lysosome in muscle sets in motion a whole series of "extra-lysosomal" events including defective autophagy and disruption of a variety of signaling pathways. Here, we report that metabolic abnormalities and energy deficit also contribute to the complexity of the pathogenic cascade. A decrease in the metabolites of the glycolytic pathway and a shift to lipids as the energy source are observed in the diseased muscle. We now demonstrate in a pre-clinical study that a recently developed replacement enzyme (recombinant human GAA; AT-GAA; Amicus Therapeutics) with much improved lysosome-targeting properties reversed or significantly improved all aspects of the disease pathogenesis, an outcome not observed with the current standard of care. The therapy was initiated in GAA-deficient mice with fully developed muscle pathology but without obvious clinical symptoms; this point deserves consideration.
    Language English
    Publishing date 2020-06-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2872938-9
    ISSN 2329-0501 ; 2329-0501
    ISSN (online) 2329-0501
    ISSN 2329-0501
    DOI 10.1016/j.omtm.2020.05.026
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 7107: Show issues Location:
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