Immunological identification of protein kinase C-α and protein kinase C-δ in cultured rat mesangial cells: Diffferential sensitivity of the two isoforms towards the protein kinase inhibitor H7

Jean Paul Oudinet, Denis Feliers, Miroslava Pavlovic-Hournac

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)559-569
Number of pages11
JournalCellular Signalling
Volume4
Issue number5
DOIs
StatePublished - 1992
Externally publishedYes

Fingerprint

Mesangial Cells
Protein Kinase Inhibitors
Protein Kinase C
Protein Isoforms
Histones
Proteins
Phosphorylation
Calcium
protein kinase C kinase
Durapatite
Chromatography
Phospholipids
High Pressure Liquid Chromatography

Keywords

  • H
  • Mesangial cells
  • protein kinase C isoforms

ASJC Scopus subject areas

  • Cell Biology

Cite this

Immunological identification of protein kinase C-α and protein kinase C-δ in cultured rat mesangial cells : Diffferential sensitivity of the two isoforms towards the protein kinase inhibitor H7. / Oudinet, Jean Paul; Feliers, Denis; Pavlovic-Hournac, Miroslava.

In: Cellular Signalling, Vol. 4, No. 5, 1992, p. 559-569.

Research output: Contribution to journalArticle

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abstract = "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.",
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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.

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