scholarly journals Macrocyclic Diterpenoids from Euphorbiaceae as A Source of Potent and Selective Inhibitors of Chikungunya Virus Replication

Molecules ◽  
2019 ◽  
Vol 24 (12) ◽  
pp. 2336 ◽  
Author(s):  
Simon Remy ◽  
Marc Litaudon
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Virus Replication ◽  
Mechanism Of Action ◽  
Chikungunya Virus ◽  
Cytopathic Effect ◽  
Structural Diversity ◽  
Biological Properties ◽  
Kinase C ◽  
Structure Activity

Macrocyclic diterpenoids produced by plants of the Euphorbiaceae family are of considerable interest due to their high structural diversity; and their therapeutically relevant biological properties. Over the last decade many studies have reported the ability of macrocyclic diterpenoids to inhibit in cellulo the cytopathic effect induced by the chikungunya virus. This review; which covers the years 2011 to 2019; lists all macrocyclic diterpenoids that have been evaluated for their ability to inhibit viral replication. The structure–activity relationships and the probable involvement of protein kinase C in their mechanism of action are also detailed.

Mechanism of action of growth hormone in adipocytes: a role for protein kinase C?

1993 ◽  
Vol 21 (4) ◽  
pp. 376S-376S
Author(s):  
RICHARD G. VERNON ◽  
SYLVIA LINDSAY-WATT ◽  
ERIC FINLEY
Keyword(s):  
Growth Hormone ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Mechanism Of Action ◽  
Kinase C

Design, synthesis, and structure–activity relationship of new isobenzofuranone ligands of protein kinase C

2004 ◽  
Vol 14 (11) ◽  
pp. 2963-2967 ◽  
Author(s):  
Yoshiyasu Baba ◽  
Yosuke Ogoshi ◽  
Go Hirai ◽  
Takeshi Yanagisawa ◽  
Kumiko Nagamatsu ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Design Synthesis ◽  
Kinase C ◽  
Structure Activity ◽  
Relationship Of

Overexpression of RHO Inhibitor and PAK as Possible Treatments For Restoring Sharp Features in Cancer Cells

2001 ◽  
Vol 7 (S2) ◽  
pp. 576-577
Author(s):  
Heckman C. A. ◽  
Urban J. M. ◽  
Wales T. S. ◽  
Cayer M. L. ◽  
Barnes J. A. ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Mechanism Of Action ◽  
Tumor Promoter ◽  
Shape Features ◽  
Cell Edge ◽  
Kinase C ◽  
Bona Fide ◽  
Rho Family

The mechanism of action of the tumor promoter, phorbol 12-myristate 13-acetate (PMA), depends on its ability to substitute for an endogenous second messenger, diacylglycerol, and thereby activate certain members of an enzyme family known as protein kinase C. Previous work from this laboratory showed that the quantitative shape phenotype of cells treated with PMA resembled the phenotype of bona fidecancer cells. The effect of PMA on this phenotype was transient, and was restricted to a period of two- to five-hours after exposure to PMA. When the shape phenotype was dissected into components by relating different variable's values to shape features, several of the altered values appeared to rely upon a declining number of sharp features, such as filopodia and microspikes, at the cell edge.Filopodia and microspikes are in turn regulated by a GTPase of the Rho family, Cdc42, which modulates actin architecture.

scholarly journals Interleukin-3, GM-CSF, and TPA induce distinct phosphorylation events in an interleukin 3-dependent multipotential cell line

Blood ◽  
1989 ◽  
Vol 73 (2) ◽  
pp. 406-418 ◽  
Author(s):  
PH Sorensen ◽  
AL Mui ◽  
SC Murthy ◽  
G Krystal
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Protein ◽  
Cell Line ◽  
Mechanism Of Action ◽  
Interleukin 3 ◽  
Gm Csf ◽  
Kinase C ◽  
Macrophage Colony ◽  
Hemopoietic Growth Factor

The mechanism of action of the hemopoietic growth factor, murine interleukin-3 (mIL-3), was investigated using an mIL-3-dependent multipotential hematopoietic cell line, B6SUtA1. Murine granulocyte- macrophage colony-stimulating factor (mGM-CSF) was as potent as mIL-3 in stimulating these cells. In addition, sodium orthovanadate, an inhibitor of phosphotyrosine phosphatase, and 12-O-tetradecanoyl- phorbol-13-acetate (TPA), a known activator of protein kinase C, also stimulated DNA synthesis in these cells, suggesting that protein phosphorylation might be involved in the mechanism of action of mIL-3 and mGM-CSF. To assess this possibility, intact B6SUtA1 cells exposed for brief periods to mIL-3, mGM-CSF, and TPA were analyzed for changes in phosphorylation patterns using metabolic 32P-labeling and antibodies to phosphotyrosine. Both mIL-3 and mGM-CSF induced the serine-specific phosphorylation of a 68-Kd cytosolic protein, whereas all three agents stimulated the serine-specific phosphorylation of a 68-Kd membrane protein. Furthermore, mIL-3 stimulated tyrosine phosphorylation of the 68-Kd membrane protein, as well as of 140-, 90-, 55, and 40-Kd proteins. The 90-Kd protein was also tyrosine phosphorylated in response to mGM-CSF. These phosphotyrosine containing proteins were not detected in TPA-treated cells. These results indicate that protein phosphorylations on tyrosine and serine residues occur in B6SUtA1 cells following short-term incubation with mIL-3 or mGM-CSF and that most of these phosphorylation events are mediated by kinases other than protein kinase C (PkC).

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