Document Detail


Cyclosporin A up-regulates and activates protein kinase C-zeta in EBV-infected and EBV-transformed human B-cells.
MedLine Citation:
PMID:  18486150     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Protein Kinase C (PKC) is a family of enzymes that plays a key role in cell signaling pathways leading to cellular activation and proliferation. Conventional PKC (cPKC) is dependent on calcium for activation. We have proposed that cyclosporin A (CsA), despite being a calcineurin inhibitor, will activate PKC in B cells, thus promoting Epstein-Barr virus (EBV)-induced transformation. Here we show that CsA promoted atypical PKC isoform PKC-zeta in B cells. MATERIALS AND METHODS: Western-blot was used to assay PKC-zeta protein level in EBV-B cells. Confocal microscopy was used to assay PKC-zeta translocation from cytosol to cell membrane, a known process of PKC activation. RESULTS: CsA (500 ng/mL) time dependently increased PKC-zeta from control of 7055 units to 7145, 10,805, 10,914, and 12,705 units, respectively, after 15 min, 1 h, 12 h, and 24 h of incubation in EBV-transformed human B-cell line (LCL). CsA increased PKC-zeta expression was inhibited 50% by Vit.E (40 microM) indicating that this effect may be due to oxidative stress induced by CsA. Indeed, after oxidant H(2)O(2) (0.1 mM) treatment, PKC-zeta protein level in LCL cells increased 124%, 257%, 349%, and 359% after 15 min, 1 h, 12 h, and 24 h of culture compared with control. Addition of Vit.E (40 microM) in H(2)O(2) (0.1 mM) treatment and then with Vit.E in the culture decreased PKC-zeta level in LCL cells 26%, 20%, 41%, and 60% after 15 min, 1 h, 12 h, and 24 h of culture. In confocal microscopy in Jurkat T cell line, phorbol 12-myristate 13-acetate (PMA) activated cPKC isoform PKCalpha after 30 min treatment and activated PKC-zeta after 60 min treatment. CsA inhibited PMA activation of PKC-alpha, but not PKC-zeta. CsA alone did not activate PKC-alpha or PKC-zeta in Jurkat T cells. In LCL and in EBV-infected human B-cells, PMA stimulated PKC-alpha activation after 30 min treatment and stimulated PKC-zeta activation after 60 min treatment. CsA inhibited PMA activation of PKC-alpha, but not PKC-zeta. In addition, CsA activated PKC-zeta in the EBV-transformed and EBV-infected human B cells. CONCLUSION: These experiments show that CsA-induced oxidative stress caused PKC-zeta up-regulation in LCL cells, and show the differential effect of CsA in the PKC signaling pathways in T cells versus B cells. CsA-induced PKC-zeta activation may be an important signaling step in EBV-induced post-transplant lymphoproliferative disorders.
Authors:
Changguo Chen; Thomas D Johnston; Hoonbae Jeon; Roberto Gedaly; Patrick McHugh; Dinesh Ranjan
Publication Detail:
Type:  Journal Article     Date:  2008-04-08
Journal Detail:
Title:  The Journal of surgical research     Volume:  153     ISSN:  1095-8673     ISO Abbreviation:  J. Surg. Res.     Publication Date:  2009 May 
Date Detail:
Created Date:  2009-04-13     Completed Date:  2009-05-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0376340     Medline TA:  J Surg Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  156-61     Citation Subset:  IM    
Affiliation:
Department of Surgery, University of Kentucky, College of Medicine, Lexington, KY 40536, USA.
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MeSH Terms
Descriptor/Qualifier:
B-Lymphocytes / drug effects*,  virology
Cells, Cultured
Cyclosporine / pharmacology*
Epstein-Barr Virus Infections / metabolism*
Herpesvirus 4, Human*
Humans
Immunosuppressive Agents / pharmacology*
Oxidative Stress
Protein Isoforms
Protein Kinase C / metabolism*
Signal Transduction
Up-Regulation
Chemical
Reg. No./Substance:
0/Immunosuppressive Agents; 0/Protein Isoforms; 59865-13-3/Cyclosporine; EC 2.7.11.1/protein kinase C zeta; EC 2.7.11.13/Protein Kinase C

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