| Dihydroheptaprenyl and dihydrodecaprenyl monophosphates induce apoptosis mediated by activation of caspase-3-like protease. | |
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MedLine Citation:
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PMID: 9461254 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Dolichyl phosphate, an essential carrier lipid in the biosynthesis of N-linked glycoprotein, has been found to induce apoptosis in rat glioma C6 cells and human monoblastic leukemia U937 cells. In the present study, dolichyl phosphate and structurally related compounds were examined regarding their apoptosis-inducing activities in U937 cells. Dihydroheptaprenyl and dihydrodecaprenyl phosphates, of which isoprene units are shorter than that of dolichyl phosphate, induced apoptosis in U937 cells. This phenomenon occurred in a dose- and time-dependent manner, as seen with dolichyl phosphate-induced apoptosis. Derivatives of the same isoprene units of dolichyl phosphate, such as dolichol, dolichal or dolichoic acid, did not induce DNA fragmentation. Farnesyl phosphate and geranylgeranyl phosphate also failed to induce apoptosis. During apoptosis, the caspase family of cysteine proteases play important roles. We observed that apoptosis induced by dihydroprenyl phosphate was mediated by caspase-3-like (CPP32-like) activation but not by caspase-1-like (ICE-like) activation. This caspase-3-like activation was inhibited by a specific inhibitor of caspase-3, DEVD-CHO, but not by an caspase-1 inhibitor YVAD-CHO. We interpret these results to mean that dihydroprenyl phosphates with more than seven isoprene units have apoptosis-inducing activity and that their signal is mediated by caspase-3-like activation. |
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Authors:
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E Yasugi; K Nakata; Y Yokoyama; K Kano; T Dohi; M Oshima |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1389 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1998 Jan |
Date Detail:
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Created Date: 1998-03-05 Completed Date: 1998-03-05 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 132-40 Citation Subset: IM |
Affiliation:
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Division of Biochemistry and Nutrition, Research Institute, International Medical Center of Japan, Tokyo. yasugi@imcj.go.jp |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Apoptosis
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drug effects* Caspase 1 Caspase 3 Caspases* Coumarins / metabolism Cysteine Endopeptidases / metabolism* Cysteine Proteinase Inhibitors / pharmacology DNA Fragmentation / drug effects Dolichol Phosphates / pharmacology Enzyme Activation Humans Leukemia / metabolism Molecular Structure Oligopeptides / metabolism, pharmacology Polyisoprenyl Phosphates / pharmacology* Tumor Cells, Cultured |
| Chemical | |
Reg. No./Substance:
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0/Coumarins; 0/Cysteine Proteinase Inhibitors; 0/Dolichol Phosphates; 0/Oligopeptides; 0/Polyisoprenyl Phosphates; 0/acetyl-aspartyl-glutamyl-valyl-aspartyl-amino-4-methylcoumarin; 0/aspartyl-glutamyl-valyl-aspartal; 12698-55-4/dolichol monophosphate; 84744-41-2/dihydroheptaprenyl phosphate; 99103-20-5/dihydrodecaprenyl phosphate; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/Casp3 protein, rat; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.36/Caspase 1 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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