Abstract:
:We synthesized the zwitterionic amphiphile cholesterylphosphorylethylpyridinium. This substance activated protein kinase C (PKC) in a micelle-based assay, but in a vesicle assay it was inhibitory. An analog of this compound, in which the pyridine ring is saturated and the nitrogen methylated, showed similar behaviour with PKC. Replacing cholesterol by an aliphatic alcohol lowered the extent of activation in the micelle assay. These results demonstrate that, with some membrane additives, the vesicle and micelle assays give opposite results. Results from the membrane-based vesicle assay for PKC are in accord with the generalization that zwitterionic amphiphiles that raise the bilayer to hexagonal phase transition temperature in model membranes are inhibitors of PKC.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Epand RM,Stafford A,Wang J,Epand RFdoi
10.1016/0014-5793(92)80629-ukeywords:
subject
Has Abstractpub_date
1992-06-15 00:00:00pages
245-8issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(92)80629-Ujournal_volume
304pub_type
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