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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Autores principales: Florin-Christensen, J., D'Alessio, C., Arighi, C., Caramelo, J., Florin-Christensen, M., Delfino, J.M.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0006291X_v243_n3_p669_FlorinChristensen
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spelling 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
collection 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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