Document Detail


NADH oxidase activity (NOX) and enlargement of HeLa cells oscillate with two different temperature-compensated period lengths of 22 and 24 minutes corresponding to different NOX forms.
MedLine Citation:
PMID:  11420117     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
NOX proteins are cell surface-associated and growth-related hydroquinone (NADH) oxidases with protein disulfide-thiol interchange activity. A defining characteristic of NOX proteins is that the two enzymatic activities alternate to generate a regular period length of about 24 min. HeLa cells exhibit at least two forms of NOX. One is tumor-associated (tNOX) and is inhibited by putative quinone site inhibitors (e.g., capsaicin or the antitumor sulfonylurea, LY181984). Another is constitutive (CNOX) and refractory to inhibition. The periodic alternation of activities and drug sensitivity of the NADH oxidase activity observed with intact HeLa cells was retained in isolated plasma membranes and with the solubilized and partially purified enzyme. At least two activities were present. One had a period length of 24 min and the other had a period length of 22 min. The lengths of both the 22 and the 24 min periods were temperature compensated (approximately the same when measured at 17, 27 or 37 degrees C) whereas the rate of NADH oxidation approximately doubled with each 10 degrees C rise in temperature. The rate of increase in cell area of HeLa cells when measured by video-enhanced light microscopy also exhibited a complex period of oscillations reflective of both 22 and 24 min period lengths. The findings demonstrate the presence of a novel oscillating NOX activity at the surface of cancer cells with a period length of 22 min in addition to the constitutive NOX of non-cancer cells and tissues with a period length of 24 min.
Authors:
S Wang; R Pogue; D M Morré; D J Morré
Related Documents :
10503877 - In vivo interaction of nucleophosmin/b23 and protein c23 during cell cycle progression ...
15081347 - Synthesis, crystal structure and antiproliferative evaluation of some new substituted b...
11502877 - Inhibition of thymidylate synthase activity by antisense oligodeoxynucleotide and possi...
9822827 - Roles of integrins and fibronectin in the entry of streptococcus pyogenes into cells vi...
22407427 - Dynamic analysis of epidermal cell divisions identifies specific roles for cop10 in ara...
18088997 - Development and evolution of the insect mushroom bodies: towards the understanding of c...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1539     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2001 Jun 
Date Detail:
Created Date:  2001-06-22     Completed Date:  2001-07-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  192-204     Citation Subset:  IM; S    
Affiliation:
Department of Foods and Nutrition, Purdue University, West Lafayette, IN, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Activity Cycles / physiology
Cell Membrane / enzymology,  metabolism*
Hela Cells / physiology*
Humans
Isoenzymes / metabolism*
Multienzyme Complexes / metabolism*
NAD / metabolism*
NADH, NADPH Oxidoreductases / metabolism*
Oxidation-Reduction
Temperature
Time Factors
Chemical
Reg. No./Substance:
0/Isoenzymes; 0/Multienzyme Complexes; 53-84-9/NAD; EC 1.6.-/NADH oxidase; EC 1.6.-/NADH, NADPH Oxidoreductases
Investigator
Investigator/Affiliation:
D J Morre / Purdue U, W Lafayette, IN

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


Previous Document:  Palmitoylation of the canine histamine H2 receptor occurs at Cys(305) and is important for cell surf...
Next Document:  Block copolymers modify the internalization of micelle-incorporated probes into neural cells.