The transient increase of tight junction permeability induced by bryostatin 1 correlates with rapid downregulation of protein kinase C-alpha

Exp Cell Res. 2000 Nov 25;261(1):239-49. doi: 10.1006/excr.2000.5035.

Abstract

The role of PKC-alpha in altered epithelial barrier permeability following the activation of PKC by TPA (12-O-tetradecanoyl phorbol 13-acetate) and bryostatin 1 in LLC-PK1 cells was investigated in this study. Like TPA, bryostatin 1 binds to and activates PKC but unlike TPA, it is not a tumor promoter. TPA at 10(-7) M induced a sustained 95% decrease in transepithelial electrical resistance (R(t)) across LLC-PK1 epithelial cell sheets, while 10(-7) M bryostatin 1 caused only a 30% decrease in R(t), which spontaneously reversed after 5 h. Simultaneous exposure of cell sheets to 10(-7) M TPA and 10(-7) M bryostatin 1 blunted the increase in epithelial permeability observed with 10(-7) M TPA alone. Co-incubation of cell sheets with bryostatin 1 and MG-132, a proteasomal inhibitor, caused a further decrease in R(t) at the 6-h time point and inhibited the recovery in R(t) seen with bryostatin 1 alone at this time point. TPA caused a rapid translocation of PKC-alpha from the cytosol to the membrane of the cell where it remained elevated. Bryostatin 1 treatment resulted in a slower translocation of PKC-alpha from the cytosol to the membrane and a much more rapid downregulation of PKC-alpha, with disappearance from this compartment after only 6 h. The classical PKC inhibitor Go6976 prevented the decrease in R(t) seen with TPA. Treatment of cells with TPA and bryostatin 1 resulted in a PKC-alpha translocation and downregulation profile which more closely resembled that seen with bryostatin 1 alone. Co-incubation of cells with MG-132 and bryostatin 1 caused a slower downregulation of PKC-alpha from the membrane fraction. Bryostatin 1 treatment of cells expressing a dominant/negative form of PKC-alpha resulted in a slower and less extensive decrease in R(t) compared to the corresponding control cells. For both TPA and bryostatin 1, the level of PKC-alpha in the membrane-associated fraction of the treated cells correlated closely with increased transepithelial permeability. Due to its transient effect on tight junction permeability, bryostatin 1 offers a novel pharmacological tool to investigate junctional physiology.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Biological Transport
  • Bryostatins
  • Carbazoles / pharmacology
  • Cell Line
  • Cell Membrane Permeability / drug effects*
  • Cell Membrane Permeability / physiology
  • Cysteine Endopeptidases / metabolism
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology
  • Epithelial Cells / cytology
  • Epithelial Cells / drug effects
  • Epithelial Cells / physiology
  • Indoles / pharmacology
  • Isoenzymes / metabolism*
  • Kinetics
  • Lactones / pharmacology*
  • Leupeptins / pharmacology
  • Macrolides
  • Mannitol / pharmacokinetics
  • Membrane Potentials / drug effects
  • Multienzyme Complexes / metabolism
  • Polyethylene Glycols / pharmacokinetics
  • Proteasome Endopeptidase Complex
  • Protein Kinase C / metabolism*
  • Protein Kinase C-alpha
  • Tetradecanoylphorbol Acetate / pharmacology
  • Tight Junctions / drug effects
  • Tight Junctions / physiology*

Substances

  • Bryostatins
  • Carbazoles
  • Enzyme Inhibitors
  • Indoles
  • Isoenzymes
  • Lactones
  • Leupeptins
  • Macrolides
  • Multienzyme Complexes
  • Go 6976
  • bryostatin 1
  • Mannitol
  • Polyethylene Glycols
  • Protein Kinase C
  • Protein Kinase C-alpha
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • Tetradecanoylphorbol Acetate
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde