[Insulin-degrading neutral protease from plasma membranes of rat liver cells and erythrocytes].
Insulin-degrading neutral proteinase with molecular weight of 70 kDa was partly purified from the rat liver and erythrocyte plasma membranes. Incubation of membranes with [gamma-32P]ATP resulted in the enzyme phosphorylation. Intensity of this process greatly increased in the presence of insulin (100 microU/ml), and correlated with the elevation of the insulin-degrading activity in proteinase. Ca2+, Mn2+, dithiothreitol, cysteine were shown to have a stimulatory effect on insulin degradation; p-chloromercuribenzoate significantly repressed this process. Phenylmethylsulphonyl fluoride and soybean trypsin inhibitor did not affect the activity of the proteinase. It was concluded that the investigated enzyme was a calpain and may participate in the mechanism of insulin action.
Sologub
L I
LI
Kusen'
S I
SI
Pashkovskaia
I S
IS
Gurskaia
N I
NI
Sen'kus'
Ia T
IaT
Antoniak
G L
GL
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D002853:Chromatography, Liquid; D003545:Cysteine / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000378:metabolism*; D008099:Liver / Q000166:cytology / Q000201:enzymology*; D008345:Manganese / Q000494:pharmacology; D011506:Proteins / Q000032:analysis; D051381:Rats
D007328:Insulin; D011506:Proteins; D008345:Manganese; D010450:Endopeptidases; D003545:Cysteine; D002118:Calcium; D004229:Dithiothreitol
Insulinrasshchepliaiushchaia neĭtral'naia proteinaza plazmaticheskikh membran kletok pecheni i éritrotsitov krys.