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Am J Physiol Cell Physiol (September 17, 2003). doi:10.1152/ajpcell.00340.2003
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Submitted on August 7, 2003
Accepted on September 8, 2003

Involvement of PKC{delta} and PKD in pulmonary microvascular endothelial cell hyperpermeability

John H Tinsley1*, Nicole R Teasdale1, and Sarah Y Yuan1

1 Surgery, Texas A&M University System Health Science Center, Temple, TX, USA

* To whom correspondence should be addressed. E-mail: jht{at}tamu.edu.

The involvement of PKC, whose isoforms are categorized into three subtypes: conventional ({alpha}, {beta}I, {beta}II, {gamma}) novel ({delta}, {epsilon}, {eta}, µ (also known as PKD), {theta}), and atypical ({zeta}, {iota}/{lambda}) in the regulation of endothelial monolayer integrity is well documented. However, isoform activity varies among different cell types. Our goal was to reveal isoform specific PKC activity in the microvascular endothelium in response to PMA and diacylglycerol (DAG). Isoform activity was demonstrated by cytosol to membrane translocation following PMA treatment and phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein following PMA and DAG treatment. Specific isoforms were inhibited using both antisense oligonucleotides and pharmacological agents. The data showed partial cytosol to membrane translocation of isoforms {alpha}, {beta}I, and {epsilon}, and complete translocation of PKC{delta} and PKD in response to PMA. Furthermore, antisense treatment and pharmacological studies indicated that the novel isoform PKC{delta} and PKD are both required for PMA- and DAG-induced MARCKs phosphorylation and hyperpermeability in pulmonary microvascular endothelial cells while isoforms {alpha}, {beta}I, and {epsilon} were dispensable with regard to these same phenomena.




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