Cell Signal Transduction, Second Messengers and Protein Phosphorylation in Health and Disease

1994 ◽  
pp. 1-22
Author(s):  
Angel Martín Municio
Keyword(s):  
Signal Transduction ◽  
Protein Phosphorylation ◽  
Second Messengers ◽  
Cell Signal ◽  
Health And Disease ◽  
Cell Signal Transduction

Calcium ions as second messengers in guard cell signal transduction

1997 ◽  
Vol 100 (1) ◽  
pp. 16-29 ◽  
Author(s):  
Martin R. McAinsh ◽  
Colin Brownlee ◽  
Alistair M. Hetherington
Keyword(s):  
Signal Transduction ◽  
Calcium Ions ◽  
Guard Cell ◽  
Second Messengers ◽  
Cell Signal ◽  
Cell Signal Transduction

Calcium ions as second messengers in guard cell signal transduction

1997 ◽  
Vol 100 (1) ◽  
pp. 16-29 ◽  
Author(s):  
Martin R. McAinsh ◽  
Colin Brownlee ◽  
Alistair M. Hetherington
Keyword(s):  
Signal Transduction ◽  
Calcium Ions ◽  
Guard Cell ◽  
Second Messengers ◽  
Cell Signal ◽  
Cell Signal Transduction

scholarly journals Polyunsaturated Fatty Acids Inhibit T Cell Signal Transduction by Modification of Detergent-insoluble Membrane Domains

1998 ◽  
Vol 143 (3) ◽  
pp. 637-644 ◽  
Author(s):  
Thomas M. Stulnig ◽  
Markus Berger ◽  
Thomas Sigmund ◽  
Daniel Raederstorff ◽  
Hannes Stockinger ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Fatty Acids ◽  
T Cells ◽  
T Cell ◽  
Polyunsaturated Fatty Acids ◽  
Membrane Domains ◽  
Protein Tyrosine ◽  
Cell Signal ◽  
Family Protein ◽  
Cell Signal Transduction

Polyunsaturated fatty acids (PUFAs) exert immunosuppressive effects, but the molecular alterations leading to T cell inhibition are not yet elucidated. Signal transduction seems to involve detergent-resistant membrane domains (DRMs) acting as functional rafts within the plasma membrane bilayer with Src family protein tyrosine kinases being attached to their cytoplasmic leaflet. Since DRMs include predominantly saturated fatty acyl moieties, we investigated whether PUFAs could affect T cell signaling by remodeling of DRMs. Jurkat T cells cultured in PUFA-supplemented medium showed a markedly diminished calcium response when stimulated via the transmembrane CD3 complex or glycosyl phosphatidylinositol (GPI)- anchored CD59. Immunofluorescence studies indicated that CD59 but not Src family protein tyrosine kinase Lck remained in a punctate pattern after PUFA enrichment. Analysis of DRMs revealed a marked displacement of Src family kinases (Lck, Fyn) from DRMs derived from PUFA-enriched T cells compared with controls, and the presence of Lck in DRMs strictly correlated with calcium signaling. In contrast, GPI-anchored proteins (CD59, CD48) and ganglioside GM1, both residing in the outer membrane leaflet, remained in the DRM fraction. In conclusion, PUFA enrichment selectively modifies the cytoplasmic layer of DRMs and this alteration could underlie the inhibition of T cell signal transduction by PUFAs.

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