Title : Involvement of PKCdelta and PKD in pulmonary microvascular endothelial cell hyperpermeability.

Pub. Date : 2004 Jan

PMID : 13679307






3 Functional Relationships(s)
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1 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. Diglycerides myristoylated alanine rich protein kinase C substrate Homo sapiens
2 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. Diglycerides myristoylated alanine rich protein kinase C substrate Homo sapiens
3 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. Diglycerides myristoylated alanine rich protein kinase C substrate Homo sapiens