Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol

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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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Autor principal: Florin-Christensen, J.
Otros Autores: D'Alessio, C., Arighi, C., Caramelo, J., Florin-Christensen, M., Delfino, J.M
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Academic Press Inc. 1998
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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100 1 |a Florin-Christensen, J. 
245 1 0 |a Micellar lipoproteins as the possible storage and translocation form of intracellular diacylglycerol 
260 |b Academic Press Inc.  |c 1998 
270 1 0 |m Florin-Christensen, J.; Institute of Neuroscience (INEUCI), Ciudad Universitaria, Pabellon II, 4 Piso, RA-1428 Buenos Aires, Argentina; email: florin@mail.retina.ar 
506 |2 openaire  |e Política editorial 
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504 |a Florin-Christensen, J., Florin-Christensen, M., Delfino, J.M., Rasmussen, H., (1993) Biochem. J., 289, pp. 783-788 
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520 3 |a 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.  |l eng 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: TW00257-02 
536 |a Detalles de la financiación: Fondo para la Investigación Científica y Tecnológica, PICT 0124 
536 |a Detalles de la financiación: This work was supported by grants from NIH-FIRCA Award (Grant No TW00257-02), FONCYT (PICT 0124), University of Buenos Aires, and FundacioÂn Antorchas. 
593 |a Institute of Neuroscience (INEUCI), Ciudad Universitaria, Pabellón II, RA-1428, Buenos Aires, Argentina 
593 |a Inst. Biochem. Biophys. (IQUIFIB), Junín 956, RA-1113, Buenos Aires, Argentina 
690 1 0 |a DIACYLGLYCEROL 
690 1 0 |a LIPOPROTEIN 
690 1 0 |a PROTEIN KINASE C ACTIVATOR 
690 1 0 |a SEPHAROSE 
690 1 0 |a ANIMAL CELL 
690 1 0 |a ARTICLE 
690 1 0 |a BINDING AFFINITY 
690 1 0 |a COLUMN CHROMATOGRAPHY 
690 1 0 |a CYTOPLASM 
690 1 0 |a INTRACELLULAR TRANSPORT 
690 1 0 |a LIPID TRANSPORT 
690 1 0 |a LIVER CYTOSOL 
690 1 0 |a MICELLE 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN INTERACTION 
690 1 0 |a RAT 
690 1 0 |a ANIMALIA 
690 1 0 |a INSECTA 
690 1 0 |a MAMMALIA 
700 1 |a D'Alessio, C. 
700 1 |a Arighi, C. 
700 1 |a Caramelo, J. 
700 1 |a Florin-Christensen, M. 
700 1 |a Delfino, J.M. 
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