Fluorimetric studies of protein kinase C interactions with phospholipids.
Dansyl-phosphatidylserine (D-PS) was used as a fluorescence probe to study interactions between protein kinase C (PKC) with phospholipid vesicles. It was found that D-PS fluorescence (520 nm) was enhanced by PKC (excited at 285 nm). The fluorescence energy transfer, indicative of a close association of PKC with D-PS vesicles, was differentially modulated by various phospholipids, depending upon their effects on PKC activation state and the manners in which they were present. PKC inhibitors (e.g. polymyxin B and ether lipids) potently inhibited the PKC-enhanced D-PS fluorescence. It is suggested that certain spatial arrangements between PKC and its phospholipid cofactor are essential for the enzyme activation and that D-PS would be a useful probe to study fluorimetrically such interactions.
Rodriguez-Paris
J M
JM
Department of Pharmacology, Emory University, Atlanta, Georgia 30322.
Shoji
M
M
Yeola
S
S
Liotta
D
D
Vogler
W R
WR
Kuo
J F
JF
D000818:Animals; D002308:Cardiolipins; D003619:Dansyl Compounds; D004735:Energy Transfer; D010712:Phosphatidic Acids; D010716:Phosphatidylinositols; D010718:Phosphatidylserines; D010743:Phospholipids; D011493:Protein Kinase C; D051381:Rats; D013050:Spectrometry, Fluorescence
D002308:Cardiolipins; D003619:Dansyl Compounds; D010712:Phosphatidic Acids; D010716:Phosphatidylinositols; D010718:Phosphatidylserines; D010743:Phospholipids; D011493:Protein Kinase C