Efficient therapy for refractory Pompe disease by mannose 6-phosphate analogue grafting on acid α-glucosidase
| Autor: | Marcel Garcia, Morgane Daurat, Alain Morère, Marc Perez, Alice Harmois, Marie Maynadier, Afitz Da Silva, Khaled El Cheikh, Catherine Caillaud, Ilaria Basile, Bernard Pau, Magali Gary-Bobo, Henry-Vincent Charbonné, Anastasia Godefroy |
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| Přispěvatelé: | Nanomedsyn, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Sciences Pour l'Oenologie (SPO), Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD [Nouvelle-Calédonie])-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), CHU Necker - Enfants Malades [AP-HP], BP Conseil, Agence Nationale de la Recherche [N13-RPIB-0012-03], French Ministere de l'Enseignement superieur, de la Recherche et de l'Innovation [NA1211012J/AE AN 11 CC], Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD [Nouvelle-Calédonie])-Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Université Montpellier 1 (UM1)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP) |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Adult alpha acid glucosidase réponse immunitaire Pharmaceutical Science Mannose Mannose 6-phosphate Pharmacology law.invention Myoblasts 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine law Glycogen storage disease type II Lysosomal storage disease medicine Animals Humans délivrance controlée Muscle Skeletal Mannosephosphates Cells Cultured chemistry.chemical_classification Mice Knockout mannose 6-phosphate receptor targeting Glycogen Storage Disease Type II alpha-Glucosidases Enzyme replacement therapy Fibroblasts medicine.disease immunologic reactions 3. Good health maladie de Pompe enzyme 030104 developmental biology Enzyme chemistry lysosomal storage disease Immunology Recombinant DNA [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology 030217 neurology & neurosurgery Glycogen enzyme replacement therapy thérapie |
| Zdroj: | Journal of Controlled Release Journal of Controlled Release, Elsevier, 2018, 269, pp.15-23. ⟨10.1016/j.jconrel.2017.10.043⟩ |
| ISSN: | 0168-3659 |
| DOI: | 10.1016/j.jconrel.2017.10.043⟩ |
| Popis: | Pompe disease is a rare disorder due to deficiency of the acid a-glucosidase (GAA) treated by enzyme replacement therapy. The present authorized treatment with rhGAA, the recombinant human enzyme, provides an important benefit in the infantile onset; however, the juvenile and adult forms of the disease corresponding to > 80% of the patients are less responsive to this treatment. This resistance has been mainly attributed to an insufficiency of mannose 6-phosphate residues in rhGAA to address lysosomes through the cation-independent mannose 6-phosphate receptor (CI-M6PR). As yet, several attempts to improve the enzyme delivery by increasing the number of mannose 6-phosphate on the enzyme were poorly effective on the late onset form of the disease. Here, we show that chemical conjugation of a synthetic analogue of the mannose 6-phosphate, named AMFA, onto rhGAA improves the affinity for CI-M6PR and the uptake of the enzyme in fibroblasts and myoblasts of adult Pompe patients. More importantly, only the conjugated rhGAA-AMFA was effective in aged Pompe mice when compared to rhGAA. Weekly treatment with 5-20 mg.kg(-1) rhGAA-AMFA provided major improvements of the motor function and of the myofiber structure, whereas rhGAA was inactive. Finally, AMFA addition did not induce supplementary immune response to the enzyme. This modified enzyme, displaying a muscle recovery in aged Pompe mice that was never attained before, could be considered as a potential therapy for the late onset Pompe disease. |
| Databáze: | OpenAIRE |
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