TY - JOUR
T1 - Substrate-specific stimulation of protein kinase C by polyvalent anions
AU - Bazzi, Mohammad D.
AU - Nelsestuen, Gary L
N1 - Funding Information:
Acknowledgement. This work was supported in part by grant HL15728 from the National
PY - 1987/8/31
Y1 - 1987/8/31
N2 - The activity of protein kinase C (PKC) toward arginine-rich substrates was greatly stimulated by sulfate and phosphate, but not by monovalent anions. This stimulation did not require phospholipid, calcium, or diacylglycerol, and appeared to mimic the stimulation by phospholipid. Anionic proteins such as bovine serum albumin also promoted PKC activity toward certain substrates that were characterized by either high arginine or high lysine content. The mechanism of both of these stimulations appeared to be related to formation of a substrate-PKC complex which is essential to phosphorylation by PKC. Polyvalent anions bind the cationic substrate and, together with PKC, form an aggregate which allows phosphorylation. Potential physiological relevance of this stimulation is discussed.
AB - The activity of protein kinase C (PKC) toward arginine-rich substrates was greatly stimulated by sulfate and phosphate, but not by monovalent anions. This stimulation did not require phospholipid, calcium, or diacylglycerol, and appeared to mimic the stimulation by phospholipid. Anionic proteins such as bovine serum albumin also promoted PKC activity toward certain substrates that were characterized by either high arginine or high lysine content. The mechanism of both of these stimulations appeared to be related to formation of a substrate-PKC complex which is essential to phosphorylation by PKC. Polyvalent anions bind the cationic substrate and, together with PKC, form an aggregate which allows phosphorylation. Potential physiological relevance of this stimulation is discussed.
UR - https://www.scopus.com/pages/publications/0023615528
UR - https://www.scopus.com/inward/citedby.url?scp=0023615528&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(87)80113-4
DO - 10.1016/S0006-291X(87)80113-4
M3 - Article
C2 - 3632667
AN - SCOPUS:0023615528
SN - 0006-291X
VL - 147
SP - 248
EP - 253
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -