TY - JOUR
T1 - Immunological identification of protein kinase C-α and protein kinase C-δ in cultured rat mesangial cells
T2 - Diffferential sensitivity of the two isoforms towards the protein kinase inhibitor H7
AU - Oudinet, Jean Paul
AU - Feliers, Denis
AU - Pavlovic-Hournac, Miroslava
PY - 1992/9
Y1 - 1992/9
N2 - Rat mesangial cells contain both calcium-dependent protein kinase C (PKC) activity, which phosphorylates histone H1 and endogenous proteins, and calcium-independent, phospholipid-dependent PKC activity, which phosphorylates only endogenous proteins. The calcium-dependent PKC was identified as PKC α by immunoblot analysis and hydroxyapatite chromatography (HPLC). The calcium-insensitive, phospholipid-dependent isoform was identified as PKC δ using similar techniques. The inhibition of the two PKC isoforms by the protein kinase inhibitor H7 [1-(iso-quinolinyl sulphonyl)-2-methyl piperazine] was examined using both histone H1 and endogenous proteins as substrates. Phosphorylations catalysed by the calcium-dependent PKC isomform α were almost 90% inhibited when histone H1 was used, and only 55% when endogenous protein were the substrate. In contrast, the phosphorylation of endogenous proteins catalysed by the calcium-insensitive, phopholipid-dependent PKC δ was not significantly affected by the inhibitor.
AB - Rat mesangial cells contain both calcium-dependent protein kinase C (PKC) activity, which phosphorylates histone H1 and endogenous proteins, and calcium-independent, phospholipid-dependent PKC activity, which phosphorylates only endogenous proteins. The calcium-dependent PKC was identified as PKC α by immunoblot analysis and hydroxyapatite chromatography (HPLC). The calcium-insensitive, phospholipid-dependent isoform was identified as PKC δ using similar techniques. The inhibition of the two PKC isoforms by the protein kinase inhibitor H7 [1-(iso-quinolinyl sulphonyl)-2-methyl piperazine] was examined using both histone H1 and endogenous proteins as substrates. Phosphorylations catalysed by the calcium-dependent PKC isomform α were almost 90% inhibited when histone H1 was used, and only 55% when endogenous protein were the substrate. In contrast, the phosphorylation of endogenous proteins catalysed by the calcium-insensitive, phopholipid-dependent PKC δ was not significantly affected by the inhibitor.
KW - H
KW - Mesangial cells
KW - protein kinase C isoforms
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U2 - 10.1016/0898-6568(92)90025-4
DO - 10.1016/0898-6568(92)90025-4
M3 - Article
C2 - 1419492
AN - SCOPUS:0026630446
VL - 4
SP - 559
EP - 569
JO - Cellular Signalling
JF - Cellular Signalling
SN - 0898-6568
IS - 5
ER -