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Titolo:
Modulation of phospholipase D by hexadecylphosphorylcholine: a putative novel mechanism for its antitumoral activity
Autore:
Lucas, L; Hernandez-Alcoceba, R; Penalva, V; Lacal, JC;
Indirizzi:
CSIC, Inst Invest Biomed, Madrid, Spain CSIC Madrid SpainCSIC, Inst Invest Biomed, Madrid, Spain
Titolo Testata:
ONCOGENE
fascicolo: 9, volume: 20, anno: 2001,
pagine: 1110 - 1117
SICI:
0950-9232(20010301)20:9<1110:MOPDBH>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHOLINE KINASE INHIBITORS; XENOPUS-LAEVIS OOCYTES; CANINE KIDNEY-CELLS; PHOSPHATIDYLCHOLINE BIOSYNTHESIS; ANALOG HEXADECYLPHOSPHOCHOLINE; GROWTH-FACTORS; SIGNAL-TRANSDUCTION; D ACTIVATION; PROTEIN; RAS;
Keywords:
phospholipase D; antitumor drug; hexadecylphosphorylcholine; choline kinase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Lacal, JC CSIC, Inst Invest Biomed, Arturo Duperier 4, Madrid, Spain CSIC Arturo Duperier 4 Madrid Spain Duperier 4, Madrid, Spain
Citazione:
L. Lucas et al., "Modulation of phospholipase D by hexadecylphosphorylcholine: a putative novel mechanism for its antitumoral activity", ONCOGENE, 20(9), 2001, pp. 1110-1117

Abstract

Hexadecylphosphorylcholine (HePC, D-18506, INN: Mitelfosine) belongs to the family of alkylphosphocholines with anticancer activity. Previous reportshave related its antitumoral activity to their ability to interfere with phospholipid metabolism, However a clear mechanism of action has not been established yet, We have investigated the effect of HePC on two enzymes recently reported to play a role in cell growth proliferation, phospholipase D (PLD) and choline kinase (ChoK). Our results demonstrate that treatment withHePC induces a rapid stimulation of PLD, that may be achieved by PKC dependent or independent mechanisms, depending on the cell line investigated. Both PLD1 and PLD2 isoenzymes are sensitive to HePC activation. By contrast, no effect was observed by HePC on Cho, a new target for anticancer drug development. Furthermore, in all cell lines tested, a chronic exposure of the cells to HePC abrogates PLD activation by either phorbol esters or HePC itself with no effect on total cellular PLD levels. This is reflected in a strong inhibition of PLD activity. We suggest that the inhibitory effects on PLD by HePC may be related to its antitumoral action.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 09:00:23