Dynamic changes of glycolipid domains within the plasma membranes of cultured rat cerebellar granule cells have been investigated. For this purpose, a pyrene-labelled derivative of G(M1) ganglioside has been incorporated in the cell plasma membrane, and the rate of excimer formation, directly related to the formation of domains, has been studied by a fluorescence imaging technique (excimer-formation imaging). Fluorescence imaging showed that upon addition of 100 microM glutamate, indirectly inducing the activation of protein kinase C (PKC), glycolipid concentration within domains increases in cell bodies. Comparable effects were exerted by the addition of PMA, directly inducing the activation of PKC. On the contrary, the phorbol ester was not effective in the presence of the specific PKC inhibitor, bisindolylmaleimide. These results suggest that glycolipid-enriched domains are dynamic supramolecular structures affected by membrane-associated events, such as PKC activation. Dynamic changes of domains could be important in modulating their postulated participation in a series of functions, including signal transduction and lipid/protein sorting

Pitto, M., Palestini, P., Ferraretto, A., Flati, S., Pavan, A., Ravasi, D., et al. (1999). Dynamics of glycolipid domains in the plasma membrane of living cultured neurons, following protein kinase C activation: a study performed by excimer-formation imaging. BIOCHEMICAL JOURNAL, 344(1), 177-184 [10.1042/0264-6021:3440177].

Dynamics of glycolipid domains in the plasma membrane of living cultured neurons, following protein kinase C activation: a study performed by excimer-formation imaging

PITTO, MARINA;PALESTINI, PAOLA NOVERINA ADA;MASSERINI, MASSIMO ERNESTO;
1999

Abstract

Dynamic changes of glycolipid domains within the plasma membranes of cultured rat cerebellar granule cells have been investigated. For this purpose, a pyrene-labelled derivative of G(M1) ganglioside has been incorporated in the cell plasma membrane, and the rate of excimer formation, directly related to the formation of domains, has been studied by a fluorescence imaging technique (excimer-formation imaging). Fluorescence imaging showed that upon addition of 100 microM glutamate, indirectly inducing the activation of protein kinase C (PKC), glycolipid concentration within domains increases in cell bodies. Comparable effects were exerted by the addition of PMA, directly inducing the activation of PKC. On the contrary, the phorbol ester was not effective in the presence of the specific PKC inhibitor, bisindolylmaleimide. These results suggest that glycolipid-enriched domains are dynamic supramolecular structures affected by membrane-associated events, such as PKC activation. Dynamic changes of domains could be important in modulating their postulated participation in a series of functions, including signal transduction and lipid/protein sorting
Articolo in rivista - Articolo scientifico
Protein Kinase C; Cells, Cultured; Microscopy, Fluorescence; Endocytosis; Glycolipids; Rats; Animals; Tetradecanoylphorbol Acetate; Fluorescent Dyes; Enzyme Activation; Cerebellum; Membrane Fluidity; Fluorescence Polarization; Neurons; Spectrometry, Fluorescence; Membrane Lipids; Cell Membrane
English
1999
344
1
177
184
none
Pitto, M., Palestini, P., Ferraretto, A., Flati, S., Pavan, A., Ravasi, D., et al. (1999). Dynamics of glycolipid domains in the plasma membrane of living cultured neurons, following protein kinase C activation: a study performed by excimer-formation imaging. BIOCHEMICAL JOURNAL, 344(1), 177-184 [10.1042/0264-6021:3440177].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/21490
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