Cell surface adenylate kinase activity regulates the F1-ATPase/P2Y13-mediated HDL endocytosis pathway on human hepatocytes
| Autor: | Laurent O. Martinez, Bertrand Perret, François Tercé, Pierre Vantourout, Xavier Collet, Aurélie C.S. Fabre, Corinne Rolland, Eric Champagne, Ronald Barbaras |
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| Přispěvatelé: | Centre de Physiopathologie Toulouse Purpan (CPTP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), This study was supported by the Association Pour la Recherche sur le Cancer (ARC-3495), the Alliance Program from Egide and the British Council, Peres, Christine |
| Rok vydání: | 2006 |
| Předmět: |
ATPase
Endocytosis Pathway MESH: Lipoproteins HDL MESH: Hepatocytes chemistry.chemical_compound Adenosine Triphosphate MESH: Adenosine Triphosphate Cells Cultured [SDV.MHEP.EM] Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism Adenosine Triphosphatases 0303 health sciences biology 030302 biochemistry & molecular biology Reverse cholesterol transport [SDV.MHEP.EM]Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism Endocytosis 3. Good health Cell biology Adenosine Diphosphate MESH: Adenylate Kinase Biochemistry MESH: Endocytosis Molecular Medicine lipids (amino acids peptides and proteins) Lipoproteins HDL MESH: Cells Cultured MESH: Cell Line Tumor Adenylate kinase Article 03 medical and health sciences Cellular and Molecular Neuroscience Cell Line Tumor MESH: Adenosine Triphosphatases Extracellular MESH: Receptors Purinergic P2 Humans Molecular Biology 030304 developmental biology Pharmacology MESH: Humans MESH: Adenosine Diphosphate Receptors Purinergic P2 Adenylate Kinase Cell Biology Culture Media Adenosine diphosphate chemistry Nucleoside-Diphosphate Kinase MESH: Culture Media Hepatocytes biology.protein Adenosine triphosphate MESH: Nucleoside-Diphosphate Kinase |
| Zdroj: | Cellular and Molecular Life Sciences Cellular and Molecular Life Sciences, 2006, 63 (23), pp.2829-37. ⟨10.1007/s00018-006-6325-y⟩ Cellular and Molecular Life Sciences, Springer Verlag, 2006, 63 (23), pp.2829-37. ⟨10.1007/s00018-006-6325-y⟩ |
| ISSN: | 1420-9071 1420-682X |
| DOI: | 10.1007/s00018-006-6325-y |
| Popis: | International audience; We have previously demonstrated on human hepatocytes that apolipoprotein A-I binding to an ecto-F(1)-ATPase stimulates the production of extracellular ADP that activates a P2Y(13)-mediated high-density lipoprotein (HDL) endocytosis pathway. Therefore, we investigated the mechanisms controlling the extracellular ATP/ADP level in hepatic cell lines and primary cultures to determine their impact on HDL endocytosis. Here we show that addition of ADP to the cell culture medium induced extracellular ATP production that was due to adenylate kinase [see text] and nucleoside diphosphokinase [see text] activities, but not to ATP synthase activity. We further observed that in vitro modulation of both ecto-NDPK and AK activities could regulate the ADP-dependent HDL endocytosis. But interestingly, only AK appeared to naturally participate in the pathway by consuming the ADP generated by the ecto-F(1)-ATPase. Thus controlling the extracellular ADP level is a potential target for reverse cholesterol transport regulation. |
| Databáze: | OpenAIRE |
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