Possible role of alteration in pH, but not in ionic strength, in the modulation of Ca(2+)-dependent and diacylglycerol-induced association of protein kinase C-alpha with plasma membrane.
In an attempt to elucidate the mechanism of the membrane binding of protein kinase C-alpha (PKC-alpha), effects of pH and ionic strength were examined on Ca(2+)-dependent and diacylglycerol-induced association of this PKC with rat liver plasma membrane. In the absence of diacylglycerol, the membrane-bound PKC-alpha increased according to the changes in pH from 6 to 8. However, these reactions were not seriously influenced by alterations in ionic strength (0-240 mM NaCl). In the presence of diacylglycerol, this pH-modulated binding of PKC-alpha to plasma membrane was more effective under lower Ca2+ concentration at pH 8. These results suggest that alkaline pH conditions seem to be important for preferable association of PKC-alpha with plasma membrane.
Nishino
N
N
Department of Pathological Biochemistry, School of Life Sciences, Faculty of Medicine, Tottori University, Yonago, Japan.
Sugimoto
I
I
Hashimoto
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004075:Diglycerides / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000166:cytology / Q000201:enzymology; D008969:Molecular Sequence Data; D009994:Osmolar Concentration; D011485:Protein Binding; D011493:Protein Kinase C / Q000378:metabolism*; D051571:Protein Kinase C-alpha; D051381:Rats
D004075:Diglycerides; D007527:Isoenzymes; D011493:Protein Kinase C; D051571:Protein Kinase C-alpha; D002118:Calcium