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Volume 272, Number 23, Issue of June 6, 1997 pp. 14950-14953
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Protein Kinase C- Activity Modulates Transepithelial Permeability and Cell Junctions in the LLC-PK₁ Epithelial Cell Line

(Received for publication, February 18, 1997, and in revised form, March 26, 1997)

Dan Rosson , Thomas G. O'Brien , Jennifer A. Kampherstein , Zoltan Szallasi ^¶ , Krisztina Bogi ^¶ , Peter M. Blumberg ^¶ and James M. Mullin

From the  Lankenau Medical Research Center, Wynnewood, Pennsylvania 19096-3411 and the ^¶ Laboratory of Cellular Carcinogenesis and Tumor Promotion, NCI, National Institutes of Health, Bethesda, Maryland 20892-4255

Modulation of protein kinase C (PKC) by 12-O-tetradecanoylphorbol-13-acetate (TPA) disrupts the cell-cell junctions of the epithelial cell line LLC-PK₁. To examine the role of specific PKC isoforms in this process we have created modified LLC-PK₁ subclones that express wild-type and dominant negative versions of PKC- under control of the tetracycline-responsive expression system. Overexpression of wild-type PKC- rendered the cells more sensitive to the effects of TPA on transepithelial permeability as measured by loss of transepithelial resistance across the cell sheet. Conversely, expression of a dominant negative PKC- rendered the cells more resistant to the effects of TPA as measured both by loss of transepithelial resistance as well as cell scattering. The properties of both subclones could be modulated by the addition of tetracycline, which suppressed the effect of the exogenous genes. These results indicate that the  isoform of PKC is at least one of the isoforms that regulate tight junctions and other cell-cell junctions of LLC-PK₁ epithelia.

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