Relevant bibliographies by topics / Lysobisphosphatidic Acid

Academic literature on the topic 'Lysobisphosphatidic Acid'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Lysobisphosphatidic Acid"

1

Chevallier, Julien, Zeina Chamoun, Guowei Jiang, Glenn Prestwich, Naomi Sakai, Stefan Matile, Robert G. Parton, and Jean Gruenberg. "Lysobisphosphatidic Acid Controls Endosomal Cholesterol Levels." Journal of Biological Chemistry 283, no. 41 (July 21, 2008): 27871–80. http://dx.doi.org/10.1074/jbc.m801463200.

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2

Jiang, Guowei, Yong Xu, Thomas Falguières, Jean Gruenberg, and Glenn D. Prestwich. "Concise Synthesis of Ether Analogues of Lysobisphosphatidic Acid." Organic Letters 7, no. 18 (September 2005): 3837–40. http://dx.doi.org/10.1021/ol051194w.

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3

Goursot, A., T. Mineva, C. Bissig, J. Gruenberg, and D. R. Salahub. "Structure, Dynamics, and Energetics of Lysobisphosphatidic Acid (LBPA) Isomers." Journal of Physical Chemistry B 114, no. 47 (December 2, 2010): 15712–20. http://dx.doi.org/10.1021/jp108361d.

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4

Jiang, Guowei, Yong Xu, and Glenn D. Prestwich. "Practical Enantiospecific Syntheses of Lysobisphosphatidic Acid and Its Analogues." Journal of Organic Chemistry 71, no. 3 (February 2006): 934–39. http://dx.doi.org/10.1021/jo051894e.

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5

Kobayashi, Toshihide, Marie-Hélène Beuchat, Margaret Lindsay, Sonia Frias, Richard D. Palmiter, Hitoshi Sakuraba, Robert G. Parton, and Jean Gruenberg. "Late endosomal membranes rich in lysobisphosphatidic acid regulate cholesterol transport." Nature Cell Biology 1, no. 2 (May 15, 1999): 113–18. http://dx.doi.org/10.1038/10084.

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6

Holopainen, Juha M., Tim Söderlund, Juha-Matti Alakoskela, Matti Säily, Ove Eriksson, and Paavo K. J. Kinnunen. "Intermolecular interactions of lysobisphosphatidic acid with phosphatidylcholine in mixed bilayers." Chemistry and Physics of Lipids 133, no. 1 (January 2005): 51–67. http://dx.doi.org/10.1016/j.chemphyslip.2004.08.004.

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7

Besson, Nelly, Francoise Hullin-Matsuda, Asami Makino, Motohide Murate, Michel Lagarde, Jean-Francois Pageaux, Toshihide Kobayashi, and Isabelle Delton-Vandenbroucke. "Selective incorporation of docosahexaenoic acid into lysobisphosphatidic acid in cultured THP-1 macrophages." Lipids 41, no. 2 (February 2006): 189–96. http://dx.doi.org/10.1007/s11745-006-5087-5.

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8

Alessandri, C., M. Bombardieri, L. Di Prospero, P. Conigliaro, F. Conti, G. Labbadia, R. Misasi, M. Sorice, and G. Valesini. "Anti-lysobisphosphatidic acid antibodies in patients with antiphospholipid syndrome and systemic lupus erythematosus." Clinical and Experimental Immunology 140, no. 1 (April 2005): 173–80. http://dx.doi.org/10.1111/j.1365-2249.2005.02727.x.

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9

Patel, Avnish, Bjorn-Patrick Mohl, and Polly Roy. "Entry of Bluetongue Virus Capsid Requires the Late Endosome-specific Lipid Lysobisphosphatidic Acid." Journal of Biological Chemistry 291, no. 23 (April 1, 2016): 12408–19. http://dx.doi.org/10.1074/jbc.m115.700856.

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10

Salvioli, Rosa, Massimo Tatti, Susanna Scarpa, Sabrina Maria Moavero, Fiorella Ciaffoni, Federica Felicetti, Christine R. Kaneski, Roscoe O. Brady, and Anna Maria Vaccaro. "The N370S (Asn370→Ser) mutation affects the capacity of glucosylceramidase to interact with anionic phospholipid-containing membranes and saposin C." Biochemical Journal 390, no. 1 (August 9, 2005): 95–103. http://dx.doi.org/10.1042/bj20050325.

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Abstract:
The properties of the endolysosomal enzyme GCase (glucosylceramidase), carrying the most prevalent mutation observed in Gaucher patients, namely substitution of an asparagine residue with a serine at amino acid position 370 [N370S (Asn370→Ser) GCase], were investigated in the present study. We previously demonstrated that Sap (saposin) C, the physiological GCase activator, promotes the association of GCase with anionic phospholipid-containing membranes, reconstituting in this way the enzyme activity. In the present study, we show that, in the presence of Sap C and membranes containing high levels of anionic phospholipids, both normal and N370S GCases are able to associate with the lipid surface and to express their activity. Conversely, when the amount of anionic phospholipids in the membrane is reduced (∼20% of total lipids), Sap C is still able to promote binding and activation of the normal enzyme, but not of N370S GCase. The altered interaction of the mutated enzyme with anionic phospholipid-containing membranes and Sap C was further demonstrated in Gaucher fibroblasts by confocal microscopy, which revealed poor co-localization of N370S GCase with Sap C and lysobisphosphatidic acid, the most abundant anionic phospholipid in endolysosomes. Moreover, we found that N370S Gaucher fibroblasts accumulate endolysosomal free cholesterol, a lipid that might further interfere with the interaction of the enzyme with Sap C and lysobisphosphatidic acid-containing membranes. In summary, our results show that the N370S mutation primarily affects the interaction of GCase with its physiological activators, namely Sap C and anionic phospholipid-containing membranes. We thus propose that the poor contact between N370S GCase and its activators may be responsible for the low activity of the mutant enzyme in vivo.
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