Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol
Previous work indicated that diacylglycerol (DG) molecules translocate across the cytoplasm of mammalian cells, a process relevant to the signalling role of this lipid as protein kinase C activator. Here we investigated the possible mechanism underlying DG translocation. We examined the interaction...
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todo:paper_0006291X_v243_n3_p669_FlorinChristensen2023-10-03T14:03:45Z Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol Florin-Christensen, J. D'Alessio, C. Arighi, C. Caramelo, J. Florin-Christensen, M. Delfino, J.M. diacylglycerol lipoprotein protein kinase C activator sepharose animal cell article binding affinity column chromatography cytoplasm intracellular transport lipid transport liver cytosol micelle nonhuman priority journal protein interaction rat Animalia Insecta Mammalia Previous work indicated that diacylglycerol (DG) molecules translocate across the cytoplasm of mammalian cells, a process relevant to the signalling role of this lipid as protein kinase C activator. Here we investigated the possible mechanism underlying DG translocation. We examined the interaction between 1,2-di-[1-14C]oleoyl-sn-glycerol and rat liver cytosol (rlc) using assays based on Lipidex-1000 and on coelution on Sepharose CL 6B. We measured high DG binding activity and found that it resides in cytosolic proteins and not in cytosolic lipids. Chromatography of rlc proteins on Sepharose CL 6B showed profiles in which the activity measured by either method coincided. Further, we showed that the DG-rlc protein interaction results in the stabilization of DG in a micellar form, eluting in the void volume of Sepharose CL 6B. Such stabilized micelles are reminiscent of insect lipophorins and may represent a new, thus far unrecognized, mode of lipid transport within living cells. Fil:Florin-Christensen, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:D'Alessio, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Arighi, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Florin-Christensen, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0006291X_v243_n3_p669_FlorinChristensen |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
diacylglycerol lipoprotein protein kinase C activator sepharose animal cell article binding affinity column chromatography cytoplasm intracellular transport lipid transport liver cytosol micelle nonhuman priority journal protein interaction rat Animalia Insecta Mammalia |
spellingShingle |
diacylglycerol lipoprotein protein kinase C activator sepharose animal cell article binding affinity column chromatography cytoplasm intracellular transport lipid transport liver cytosol micelle nonhuman priority journal protein interaction rat Animalia Insecta Mammalia Florin-Christensen, J. D'Alessio, C. Arighi, C. Caramelo, J. Florin-Christensen, M. Delfino, J.M. Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol |
topic_facet |
diacylglycerol lipoprotein protein kinase C activator sepharose animal cell article binding affinity column chromatography cytoplasm intracellular transport lipid transport liver cytosol micelle nonhuman priority journal protein interaction rat Animalia Insecta Mammalia |
description |
Previous work indicated that diacylglycerol (DG) molecules translocate across the cytoplasm of mammalian cells, a process relevant to the signalling role of this lipid as protein kinase C activator. Here we investigated the possible mechanism underlying DG translocation. We examined the interaction between 1,2-di-[1-14C]oleoyl-sn-glycerol and rat liver cytosol (rlc) using assays based on Lipidex-1000 and on coelution on Sepharose CL 6B. We measured high DG binding activity and found that it resides in cytosolic proteins and not in cytosolic lipids. Chromatography of rlc proteins on Sepharose CL 6B showed profiles in which the activity measured by either method coincided. Further, we showed that the DG-rlc protein interaction results in the stabilization of DG in a micellar form, eluting in the void volume of Sepharose CL 6B. Such stabilized micelles are reminiscent of insect lipophorins and may represent a new, thus far unrecognized, mode of lipid transport within living cells. |
format |
JOUR |
author |
Florin-Christensen, J. D'Alessio, C. Arighi, C. Caramelo, J. Florin-Christensen, M. Delfino, J.M. |
author_facet |
Florin-Christensen, J. D'Alessio, C. Arighi, C. Caramelo, J. Florin-Christensen, M. Delfino, J.M. |
author_sort |
Florin-Christensen, J. |
title |
Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol |
title_short |
Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol |
title_full |
Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol |
title_fullStr |
Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol |
title_full_unstemmed |
Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol |
title_sort |
micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol |
url |
http://hdl.handle.net/20.500.12110/paper_0006291X_v243_n3_p669_FlorinChristensen |
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