Document Detail


Expression and activity of NAD(P)H:quinone oxidoreductase (NMO1) in human osteoblastic cells.
MedLine Citation:
PMID:  11165937     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
NAD(P)H:quinone oxidoreductase (NMO1; EC 1.6.99.2), also called DT-diaphorase, is involved in the reduction of coenzyme Q, an important cellular lipophilic antioxidant that can function as an intermediate electron carrier in plasma membrane-associated electron transport regulating cell growth. We examined the ability of normal human trabecular osteoblastic cells to express NAD(P)H:quinone oxidoreductase (NMO1) and studied its modulation during cell proliferation and growth arrest. We found that confluent primary human trabecular osteoblastic cells derived from healthy individuals constitutively express NMO1 activity, measured using 2-6 dichlorophenol indophenol (DCI) or menadione (vitamin K3) as substrate, and NADPH or NADH as electron donor. We also found that NMO1 activity was related to osteoblastic cell growth. NMO1 activity increased with osteoblastic cell density. Confluent growth-arrested cells expressed an eightfold higher NMO1 specific activity than proliferative human osteoblastic cells. Reverse-transcription polymerase chain reaction analysis showed that NMO1 mRNA levels did not differ in growth-arrested confluent cell and growing cells, suggesting that the increased NMO1 activity with cell density was due to posttranslational events. Harvesting and replating the cells at low density resulted in a 93.4% loss of NMO1 enzymatic activity. Removal of serum from high-density growth-arrested cells resulted in a 48.5% decrease in NMO1 activity. NMO1 activity does not appear to be related to induction of osteoblast differentiation because treatment with the differentiating agent 1,25(OH)(2) vitamin D(3) had no effect on NMO1 activity. The finding that human osteoblastic cells express NMO1 constitutively and that NMO1 activity increases with density-dependent growth inhibition suggest a role for NAD(P)H:quinone oxidoreductase in the control of growth arrest in normal human osteoblastic cells.
Authors:
P Collin; A Lomri; P J Marie
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Bone     Volume:  28     ISSN:  8756-3282     ISO Abbreviation:  Bone     Publication Date:  2001 Jan 
Date Detail:
Created Date:  2001-02-22     Completed Date:  2001-06-07     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8504048     Medline TA:  Bone     Country:  United States    
Other Details:
Languages:  eng     Pagination:  9-13     Citation Subset:  IM    
Affiliation:
Laboratoire de Biologie et Biochimie Cellulaire du Vieillissement, Université Paris, Paris, France.
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MeSH Terms
Descriptor/Qualifier:
Aged
Cell Division / drug effects,  physiology
Cells, Cultured
Culture Media, Serum-Free / pharmacology
Enzyme Activation
Female
Gene Expression Regulation, Enzymologic
Humans
Male
Middle Aged
NAD(P)H Dehydrogenase (Quinone) / genetics*,  metabolism*
Osteoblasts / cytology,  enzymology*
RNA, Messenger / analysis
Steroid Hydroxylases / pharmacology
Chemical
Reg. No./Substance:
0/Culture Media, Serum-Free; 0/RNA, Messenger; EC 1.14.-/Steroid Hydroxylases; EC 1.14.-/vitamin D 1-alpha hydroxylase; EC 1.6.5.2/NAD(P)H Dehydrogenase (Quinone)

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