Apolipoprotein A-II is catabolized in the kidney as a function of its plasma concentration
We investigated in vivo catabolism of apolipoprotein A-II (apo A-II), a major determinant of plasma HDL levels. Like apoA-I, murine apoA-II (mapoA-II) and human apoA-II (hapoA-II) were reabsorbed in the first segment of kidney proximal tubules of control and hapoA-II-transgenic mice, respectively. A...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2007-10-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520424605 |
| _version_ | 1818920460864192512 |
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| author | Sonia Dugué-Pujol Xavier Rousset Danielle Château Danièle Pastier Christophe Klein Jeannine Demeurie Charlotte Cywiner-Golenzer Michèle Chabert Pierre Verroust Jean Chambaz François-Patrick Châtelet Athina-Despina Kalopissis |
| author_facet | Sonia Dugué-Pujol Xavier Rousset Danielle Château Danièle Pastier Christophe Klein Jeannine Demeurie Charlotte Cywiner-Golenzer Michèle Chabert Pierre Verroust Jean Chambaz François-Patrick Châtelet Athina-Despina Kalopissis |
| author_sort | Sonia Dugué-Pujol |
| collection | DOAJ |
| description | We investigated in vivo catabolism of apolipoprotein A-II (apo A-II), a major determinant of plasma HDL levels. Like apoA-I, murine apoA-II (mapoA-II) and human apoA-II (hapoA-II) were reabsorbed in the first segment of kidney proximal tubules of control and hapoA-II-transgenic mice, respectively. ApoA-II colocalized in brush border membranes with cubilin and megalin (the apoA-I receptor and coreceptor, respectively), with mapoA-I in intracellular vesicles of tubular epithelial cells, and was targeted to lysosomes, suggestive of degradation. By use of three transgenic lines with plasma hapoA-II concentrations ranging from normal to three times higher, we established an association between plasma concentration and renal catabolism of hapoA-II. HapoA-II was rapidly internalized in yolk sac epithelial cells expressing high levels of cubilin and megalin, colocalized with cubilin and megalin on the cell surface, and effectively competed with apoA-I for uptake, which was inhibitable by anti-cubilin antibodies. Kidney cortical cells that only express megalin internalized LDL but not apoA-II, apoA-I, or HDL, suggesting that megalin is not an apoA-II receptor. We show that apoA-II is efficiently reabsorbed in kidney proximal tubules in relation to its plasma concentration. |
| first_indexed | 2024-12-20T01:22:07Z |
| format | Article |
| id | doaj.art-07e229707e2444f58477b2dbc9d2309b |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-20T01:22:07Z |
| publishDate | 2007-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-07e229707e2444f58477b2dbc9d2309b2022-12-21T19:58:23ZengElsevierJournal of Lipid Research0022-22752007-10-01481021512161Apolipoprotein A-II is catabolized in the kidney as a function of its plasma concentrationSonia Dugué-Pujol0Xavier Rousset1Danielle Château2Danièle Pastier3Christophe Klein4Jeannine Demeurie5Charlotte Cywiner-Golenzer6Michèle Chabert7Pierre Verroust8Jean Chambaz9François-Patrick Châtelet10Athina-Despina Kalopissis11Institut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, France; Ecole Pratique des Hautes Etudes, Laboratoire de Pharmacologie Cellulaire et Moléculaire, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U538, CHU Saint Antoine, Paris, F-75012, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, France; Ecole Pratique des Hautes Etudes, Laboratoire de Pharmacologie Cellulaire et Moléculaire, Paris, F-75006, FranceInstitut National de la Santé et de la Recherche Médicale, U538, CHU Saint Antoine, Paris, F-75012, FranceInstitut National de la Santé et de la Recherche Médicale, U872, Equipe 6, Paris, F-75006 France; Université Pierre et Marie Curie-Paris 6, UMR S 872, Equipe 6, Paris, F-75006, France; Centre de Recherche des Cordeliers, Université Paris Descartes, UMR S 872, Equipe 6, Paris, F-75006, FranceWe investigated in vivo catabolism of apolipoprotein A-II (apo A-II), a major determinant of plasma HDL levels. Like apoA-I, murine apoA-II (mapoA-II) and human apoA-II (hapoA-II) were reabsorbed in the first segment of kidney proximal tubules of control and hapoA-II-transgenic mice, respectively. ApoA-II colocalized in brush border membranes with cubilin and megalin (the apoA-I receptor and coreceptor, respectively), with mapoA-I in intracellular vesicles of tubular epithelial cells, and was targeted to lysosomes, suggestive of degradation. By use of three transgenic lines with plasma hapoA-II concentrations ranging from normal to three times higher, we established an association between plasma concentration and renal catabolism of hapoA-II. HapoA-II was rapidly internalized in yolk sac epithelial cells expressing high levels of cubilin and megalin, colocalized with cubilin and megalin on the cell surface, and effectively competed with apoA-I for uptake, which was inhibitable by anti-cubilin antibodies. Kidney cortical cells that only express megalin internalized LDL but not apoA-II, apoA-I, or HDL, suggesting that megalin is not an apoA-II receptor. We show that apoA-II is efficiently reabsorbed in kidney proximal tubules in relation to its plasma concentration.http://www.sciencedirect.com/science/article/pii/S0022227520424605high density lipoproteincubilinmegalinproximal tubuleyolk sac cellsmouse kidney cortical cells |
| spellingShingle | Sonia Dugué-Pujol Xavier Rousset Danielle Château Danièle Pastier Christophe Klein Jeannine Demeurie Charlotte Cywiner-Golenzer Michèle Chabert Pierre Verroust Jean Chambaz François-Patrick Châtelet Athina-Despina Kalopissis Apolipoprotein A-II is catabolized in the kidney as a function of its plasma concentration Journal of Lipid Research high density lipoprotein cubilin megalin proximal tubule yolk sac cells mouse kidney cortical cells |
| title | Apolipoprotein A-II is catabolized in the kidney as a function of its plasma concentration |
| title_full | Apolipoprotein A-II is catabolized in the kidney as a function of its plasma concentration |
| title_fullStr | Apolipoprotein A-II is catabolized in the kidney as a function of its plasma concentration |
| title_full_unstemmed | Apolipoprotein A-II is catabolized in the kidney as a function of its plasma concentration |
| title_short | Apolipoprotein A-II is catabolized in the kidney as a function of its plasma concentration |
| title_sort | apolipoprotein a ii is catabolized in the kidney as a function of its plasma concentration |
| topic | high density lipoprotein cubilin megalin proximal tubule yolk sac cells mouse kidney cortical cells |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520424605 |
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