| Biotin uptake into human peripheral blood mononuclear cells increases early in the cell cycle, increasing carboxylase activities. | |
| | |
MedLine Citation:
|
PMID: 12097659 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Cells respond to proliferation with increased accumulation of biotin, suggesting that proliferation enhances biotin demand. Here we determined whether peripheral blood mononuclear cells (PBMC) increase biotin uptake at specific phases of the cell cycle, and whether biotin is utilized to increase biotinylation of carboxylases. Biotin uptake was quantified in human PBMC that were arrested chemically at specific phases of the cell cycle, i.e., biotin uptake increased in the G1 phase of the cycle [658 +/- 574 amol biotin/(10(6) cells x 30 min)] and remained increased during phases S, G2, and M compared with quiescent controls [200 +/- 62 amol biotin/(10(6) cells x 30 min)]. The abundance of the sodium-dependent multivitamin transporter (SMVT, which transports biotin) was similar at all phases of the cell cycle, suggesting that transporters other than SMVT or splicing variants of SMVT may account for the increased biotin uptake observed in proliferating cells. Activities of biotin-dependent 3-methylcrotonyl-CoA carboxylase and propionyl-CoA carboxylase were up to two times greater in proliferating PBMC compared with controls. The abundance of mRNA encoding 3-methylcrotonyl-CoA carboxylase and propionyl-CoA carboxylase paralleled carboxylase activities, suggesting that PBMC respond to proliferation with increased expression of genes encoding carboxylases. Similarly, expression of the gene encoding holocarboxylase synthetase (which catalyzes binding of biotin to carboxylases) increased in response to proliferation, suggesting that cellular capacity to biotinylate carboxylases was increased. In summary, these findings suggest that PBMC respond to proliferation with increased biotin uptake early in the cell cycle, and that biotin is utilized to increase activities of two of the four biotin-requiring carboxylases. |
| | |
Authors:
|
J Steven Stanley; Donald M Mock; Jacob B Griffin; Janos Zempleni |
Related Documents
:
|
12086719 - Effects of superporous hydrogels on paracellular drug permeability and cytotoxicity stu... 12479629 - An in vitro model of ciprofloxacin and minocycline transport by oral epithelial cells. 12869649 - A human serotonin transporter mutation causes constitutive activation of transport acti... 7031439 - On the uptake of nystatin by saccharomyces cerevisiae. 2 effects of ph, ionic strength,... 7725349 - Inhibitors of renal chloride transport do not block toxicant-induced chloride influx in... 1793879 - Specific binding and internalization of monoclonal antibody hi98-daunorubicin conjugate... 1203879 - Survival and phase sensitivity of hela cells treated with dianhydrogalactitol (nsc-1323... 15157459 - Fumonisins: fungal toxins that shed light on sphingolipid function. 20601539 - Placental-derived mesenchyme influences chorionic gonadotropin and progesterone secreti... |
Publication Detail:
|
Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
|
Title: The Journal of nutrition Volume: 132 ISSN: 0022-3166 ISO Abbreviation: J. Nutr. Publication Date: 2002 Jul |
Date Detail:
|
Created Date: 2002-07-04 Completed Date: 2002-07-26 Revised Date: 2013-03-13 |
Medline Journal Info:
|
Nlm Unique ID: 0404243 Medline TA: J Nutr Country: United States |
Other Details:
|
Languages: eng Pagination: 1854-9 Citation Subset: IM |
Affiliation:
|
Arkansas Children's Hospital Research Institute, Little Rock, AR, USA. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Adult Biotin / pharmacokinetics* Carbon-Carbon Ligases / genetics, metabolism* Carbon-Nitrogen Ligases / genetics Carboxy-Lyases / genetics, metabolism* Cell Cycle / physiology Female Humans Male Methylmalonyl-CoA Decarboxylase Middle Aged Monocytes / cytology*, metabolism* RNA, Messenger / metabolism Reference Values Symporters / metabolism Thymidine / pharmacokinetics Time Factors |
| Grant Support | |
ID/Acronym/Agency:
|
DK 36823/DK/NIDDK NIH HHS; DK 60447/DK/NIDDK NIH HHS; R37 DK036823/DK/NIDDK NIH HHS; R37 DK036823-23/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
|
0/RNA, Messenger; 0/Symporters; 0/biotin transporter; 50-89-5/Thymidine; 58-85-5/Biotin; EC 4.1.1.-/Carboxy-Lyases; EC 4.1.1.41/Methylmalonyl-CoA Decarboxylase; EC 6.3.-/Carbon-Nitrogen Ligases; EC 6.3.4.-/holocarboxylase synthetases; EC 6.4.-/Carbon-Carbon Ligases; EC 6.4.1.4/methylcrotonoyl-CoA carboxylase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Flavonoid phytochemicals regulate activator protein-1 signal transduction pathways in endometrial an...
Next Document: Supplemental zinc lowers measures of iron status in young women with low iron reserves.