Document Detail


Phosphatidylcholine-specific phospholipase C activation in epithelial ovarian cancer cells.
MedLine Citation:
PMID:  18701477     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Elucidation of the mechanisms responsible for aberrant phosphatidylcholine (PC) metabolism in cancer cells may allow identification of novel biomarkers of tumor progression and design of new targeted anticancer therapies. We recently reported up-regulation of PC-specific phospholipases in epithelial ovarian cancer cells (EOC) compared with nontumoral (normal or immortalized) counterparts (EONT). In the present study, we focused, in the same cell systems, on levels, subcellular localization, and activity of PC-specific phospholipase C (PC-PLC), for which a key role in cell proliferation, differentiation, and apoptosis has been shown in several mammalian cells. A 66-kDa PC-PLC isoform, detected in nuclear and cytoplasmic compartments of both EOC and EONT cells, accumulated on the external plasma membrane of cancer cells only, where it colocalized with beta1 integrin, in nonraft membrane domains. PC-PLC activity was 3-fold higher in total cell lysates and 5-fold higher in membrane-enriched fractions of EOC compared with EONT cells. Serum deprivation induced in EOC, but not in EONT, cells a 3-fold decrease in PC-PLC activity, associated with a 40% drop in S-phase fraction. The recovery of both variables to their original levels in serum-restimulated (or lysophosphatidic acid-restimulated) EOC cells was strongly delayed, for at least 24 h, in the presence of the PC-PLC inhibitor tricyclodecan-9-yl-potassium xanthate (D609). The S-phase of serum-restimulated EONT cells was not sensitive to D609. These findings warrant further investigations on the role of PC-PLC and on the effects of its inhibition on the pathways responsible for constitutive EOC cell stimulation and cell proliferation.
Authors:
Francesca Spadaro; Carlo Ramoni; Delia Mezzanzanica; Silvia Miotti; Paola Alberti; Serena Cecchetti; Egidio Iorio; Vincenza Dolo; Silvana Canevari; Franca Podo
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cancer research     Volume:  68     ISSN:  1538-7445     ISO Abbreviation:  Cancer Res.     Publication Date:  2008 Aug 
Date Detail:
Created Date:  2008-08-14     Completed Date:  2008-10-02     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984705R     Medline TA:  Cancer Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6541-9     Citation Subset:  IM    
Affiliation:
Section of Molecular and Cellular Imaging, Department of Cell Biology and Neurosciences, Istituto Superiore di Sanità, Rome, Italy.
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MeSH Terms
Descriptor/Qualifier:
Adenocarcinoma, Clear Cell / enzymology,  secondary
Adenocarcinoma, Mucinous / enzymology,  secondary
Apoptosis / physiology
Bridged Compounds / pharmacology
Carcinoma, Endometrioid / enzymology,  secondary
Cell Membrane / enzymology,  pathology
Cell Nucleus / enzymology,  pathology
Culture Media, Serum-Free / pharmacology
Cystadenocarcinoma, Serous / enzymology,  secondary
Cytoplasm / enzymology*,  pathology
Enzyme Activation
Epithelium / enzymology,  pathology
Female
Flow Cytometry
Humans
Membrane Microdomains
Ovarian Neoplasms / enzymology*,  pathology
Ovary / enzymology,  pathology
Phosphodiesterase Inhibitors / pharmacology
Phospholipase D / metabolism
S Phase / physiology
Telomerase / metabolism
Thiones / pharmacology
Type C Phospholipases / antagonists & inhibitors,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/Bridged Compounds; 0/Culture Media, Serum-Free; 0/Phosphodiesterase Inhibitors; 0/Thiones; 83373-60-8/tricyclodecane-9-yl-xanthogenate; EC 2.7.7.49/TERT protein, human; EC 2.7.7.49/Telomerase; EC 3.1.4.-/Type C Phospholipases; EC 3.1.4.3/phosphatidylcholine-specific phospholipase C; EC 3.1.4.4/Phospholipase D

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


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