Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.13 (protein kinase C)
 49,245 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

During an HCMV infection, transcription of viral and cellular genes are mutually regulated. Several cellular proteins have been implicated in the regulation of the HCMV major immediate early promoter (MIEP) which have been shown to respond to cAMP as well as activation of protein kinase C (PKC). We have examined the effect of an ongoing HCMV infection at the mRNA level for the catalytic and regulatory subunits of protein kinase A (PKA) and alpha and beta isoforms of PKC. There was a moderate elevation for PKA C alpha and RI alpha at immediate early times (0.5-2 h) after HCMV infection. Later in the infection cycle (24-72 h), mRNA level for PKA regulatory subunit RI alpha and PKC alpha were decreased compared with control cells. Messenger RNA levels for the PKA RII alpha and RII beta as well as PKC beta were not affected by HCMV infection. During the infection cycle the PKA subunits and PKC isoforms appeared to be independently regulated. It was also evident that the basal mRNA levels of PKA subunits and the PKC isoforms were sufficient for the PKA and PKC activity required during an HCMV infection in permissive fibroblast cells.
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PMID:Expression of protein kinase A and protein kinase C during ongoing human cytomegalovirus infection. 798 13

Internalization of the urokinase-type plasminogen activator (uPA) requires two receptors, the uPA receptor (uPAR) and the low density lipoprotein receptor-related protein (LRP)/alpha2-macroglobulin (alpha2M) receptor. Here, we address whether protein kinases are involved in the internalization of uPA by human melanoma cells. Initially, we found that the internalization of uPA was significantly inhibited by the serine/threonine protein kinase inhibitors staurosporine, K-252a and H-89, but not by the tyrosine kinase inhibitors, genistein and lavendustin A. Internalization of uPA was also inhibited by a pseudosubstrate peptide for cAMP-dependent protein kinase (PKA), but not by a pseudosubstrate peptide for protein kinase C. We confirmed a requirement for PKA-activity and implicated a specific isoform by using an antisense oligonucleotide against the regulatory subunit RI alpha of PKA which suppresses PKA-I activity. Exposure of cells to this oligonucleotide led to a specific, dose-dependent decrease in RI alpha protein and to a significant inhibition in the rate of uPA internalization. We further demonstrate that treatment of melanoma cells with either H-89 or PKA RI alpha antisense oligonucleotides also resulted in a decreased internalization of two other ligands of LRP, activated alpha2M and lactoferrin, indicating that PKA activity is associated with LRP. Finally, we demonstrate that PKA activity is also required for the internalization of transferrin, but not for the internalization of the epidermal growth factor or adenovirus 2, suggesting that in melanoma cells, PKA activity is not generally required for clathrin-mediated endocytosis, but is rather associated with specific internalization receptors.
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PMID:Receptor-mediated endocytosis of urokinase-type plasminogen activator is regulated by cAMP-dependent protein kinase. 921 25