Document Detail


The selective protein kinase C beta inhibitor enzastaurin induces apoptosis in cutaneous T-cell lymphoma cell lines through the AKT pathway.
MedLine Citation:
PMID:  16645590     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Enzastaurin displays pro-apoptotic properties against a spectrum of malignancies and is currently being investigated in clinical trials. We have investigated the effects of enzastaurin on the viability of the cutaneous T-cell lymphoma cell lines HuT-78 and HH by using 3-(4,5-dimethylthiazol-2-yl)-5(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium assay, cell cycle analysis, propidium iodide and annexin-V staining, and caspase-3-mediated proteolytic activation. Enzastaurin-treatment decreased cell viability, increased annexin V-FITC-positive cells, and increased the proportion of sub-G1 populations in both cell lines that was not reversed by the T-cell growth stimulating cytokines IL-2, IL-7, IL-15. Enzastaurin-induced cell death involved caspase-3-activated cleavage of poly(ADP-ribose) polymerase that was inhibited by the pan-caspase inhibitor ZVAD-fmk, whereas the increase in sub-G1 population was only partially inhibited by ZVAD-fmk. Furthermore, enzastaurin downregulated AKT activity and its downstream effectors GSK3beta and ribosomal protein S6. The phosphatidylinositol 3-kinase (PI3K)/AKT pathway has been implicated in the growth and survival of hematologic malignancies and inhibition of this pathway is considered as a therapeutic target. Protein kinase C activation contributes to PI3K/AKT activation, but it is unknown how enzastaurin may interfere with signaling through this pathway. These results demonstrate that enzastaurin, at clinically achievable concentrations, induces apoptosis and affects AKT signaling, and provide a rationale for further in vivo studies addressing the therapeutic efficacy in cutaneous T-cell lymphoma patients.
Authors:
Christiane Querfeld; Mujahid A Rizvi; Timothy M Kuzel; Joan Guitart; Alfred Rademaker; Simran S Sabharwal; Nancy L Krett; Steven T Rosen
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-04-27
Journal Detail:
Title:  The Journal of investigative dermatology     Volume:  126     ISSN:  0022-202X     ISO Abbreviation:  J. Invest. Dermatol.     Publication Date:  2006 Jul 
Date Detail:
Created Date:  2006-06-16     Completed Date:  2006-08-01     Revised Date:  2011-11-02    
Medline Journal Info:
Nlm Unique ID:  0426720     Medline TA:  J Invest Dermatol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1641-7     Citation Subset:  IM    
Affiliation:
Department of Dermatology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA. c-querfeld@northwestern.edu
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MeSH Terms
Descriptor/Qualifier:
Apoptosis / drug effects*,  physiology
Caspases / analysis,  physiology
Cell Cycle / drug effects,  physiology
Cell Line, Tumor
Cell Proliferation / drug effects
Cell Survival / drug effects
Enzyme Activation / drug effects,  physiology
Enzyme Inhibitors / pharmacology*
Gene Expression Regulation, Neoplastic / drug effects
Glycogen Synthase Kinase 3 / metabolism
Humans
Indoles / pharmacology*
Lymphoma, T-Cell, Cutaneous / enzymology,  pathology*
Phosphorylation / drug effects
Poly(ADP-ribose) Polymerases / analysis,  physiology
Protein Kinase C / antagonists & inhibitors*
Proto-Oncogene Proteins c-akt / genetics,  physiology*
Ribosomal Protein S6 / analysis
Signal Transduction / physiology*
Skin Neoplasms / enzymology,  pathology*
Chemical
Reg. No./Substance:
0/Enzyme Inhibitors; 0/Indoles; 0/Ribosomal Protein S6; 0/enzastaurin; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 2.7.1.-/protein kinase C beta; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 2.7.11.1/glycogen synthase kinase 3 beta; EC 2.7.11.13/Protein Kinase C; EC 2.7.11.26/Glycogen Synthase Kinase 3; EC 3.4.22.-/Caspases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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