Polyamines and the catalytic domain of protein kinase C.
The effect of polyamines on the catalytic domain of protein kinase C from rat brain was investigated. It was found that the addition of spermine strongly inhibited phosphorylation activity toward histone H1 as substrate. This tetramine, at millimolar concentrations, was most potently effective while triamines and diamines were almost uneffective, therefore the inhibitory action appeared to be structural specific. Data shown here suggest that polyamine by interacting with the catalytic domain of the enzyme may contribute to its regulation.
Mezzetti
G
G
Istituto di Chimica Biologica, Università di Modena, Italy.
Monti
M G
MG
Moruzzi
M S
MS
D000818:Animals; D001921:Brain / Q000201:enzymology; D002103:Cadaverine / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology; D002850:Chromatography, Gel; D006657:Histones / Q000378:metabolism; D010446:Peptide Fragments / Q000037:antagonists & inhibitors / Q000378:metabolism; D010743:Phospholipids / Q000494:pharmacology; D010766:Phosphorylation; D011073:Polyamines / Q000494:pharmacology*; D011493:Protein Kinase C / Q000037:antagonists & inhibitors*; D011700:Putrescine / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000494:pharmacology; D013329:Structure-Activity Relationship
D006657:Histones; D010446:Peptide Fragments; D010743:Phospholipids; D011073:Polyamines; D013096:Spermine; D011493:Protein Kinase C; D002103:Cadaverine; D002118:Calcium; D013095:Spermidine; D011700:Putrescine