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1 Department of Surgery, Beth Israel Deaconess Medical Center, Boston, MA, USA
2 Department of Surgery, University of Cincinnati Medical Center, Cincinnati, OH, USA
3 Department of Surgery, University of Cincinnati Medical Center, Cincinnati, OH, USA; Department of Surgery, Beth Israel Deaconess Medical Center, Boston, MA, USA
* To whom correspondence should be addressed. E-mail: jeffrey.matthews{at}uc.edu.
Protein kinase C (PKC) is known to regulate epithelial barrier function. However, the effect of specific PKC isozymes, as well as their mechanism of action, is largely unknown. We determined that the non-phorbol ester PKC agonist bryostatin-1 increased transepithelial electrical resistance (TER), a marker of barrier function, in confluent T84 epithelia. Bryostatin-1, which has been shown to selectively activate PKC
, 
, and 
(34), was associated with a shift in the subcellular distribution of the tight junction proteins claudin-1 and ZO-2 from a detergent-soluble fraction into a detergent-insoluble fraction. Bryostatin-1 also led to the appearance of a higher molecular-weight form of occludin previously shown to correspond to protein phosphorylation. These changes were attenuated by the conventional and novel PKC inhibitor GO6850 but not the conventional PKC inhibitor GO6976 or the PKC inhibitor rottlerin, implicating a novel isozyme, likely PKC. The results suggest that enhanced epithelial barrier function induced by bryostatin-1 involves a PKC-dependent signaling pathway leading to recruitment of claudin-1 and ZO-2, and phosphorylation of occludin, into the tight junctional complex.
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