Involvement of PKCdelta and PKD in pulmonary microvascular endothelial cell hyperpermeability.
Am J Physiol Cell Physiol
; 286(1): C105-11, 2004 Jan.
Article
em En
| MEDLINE
| ID: mdl-13679307
ABSTRACT
The involvement of PKC, the isoforms of which are categorized into three subtypes conventional (alpha, betaI, betaII, and gamma), novel [delta, epsilon, eta, and mu (also known as PKD), theta], and atypical (zeta and 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 phorbol 12-myristate 13-acetate (PMA) and diacylglycerol (DAG). Isoform activity was demonstrated by cytosol-to-membrane translocation after PMA treatment and phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein after PMA and DAG treatment. Specific isoforms were inhibited by using both antisense oligonucleotides and pharmacological agents. The data showed partial cytosol-to-membrane translocation of isoforms alpha, betaI, and epsilon and complete translocation of PKCdelta and PKD in response to PMA. Furthermore, antisense treatment and pharmacological studies indicated that the novel isoform PKCdelta and PKD are both required for PMA- and DAG-induced MARCKS phosphorylation and hyperpermeability in pulmonary microvascular endothelial cells, whereas isoforms alpha, betaI, and epsilon were dispensable with regard to these same phenomena.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteína Quinase C
/
Permeabilidade Capilar
/
Endotélio Vascular
/
Circulação Pulmonar
/
Peptídeos e Proteínas de Sinalização Intracelular
/
Proteínas de Membrana
Limite:
Animals
Idioma:
En
Revista:
Am J Physiol Cell Physiol
Assunto da revista:
FISIOLOGIA
Ano de publicação:
2004
Tipo de documento:
Article
País de afiliação:
Estados Unidos