Linked Life Data

15921655

Source:http://linkedlifedata.com/resource/pubmed/id/15921655

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-6-13
pubmed:abstractText
Collagen II is the major protein component of articular cartilage and forms the collagen fibril network, which provides the tensile strength of cartilage. Collagen II synthesis is enhanced by ascorbic acid (vitamin C) at both a transcriptional and post-transcriptional level. While the importance of ascorbic acid in the synthesis of collagen has been established, the mechanism by which this essential nutrient is transported into chondrocytes has not been investigated previously. We have characterized the transport of the reduced form of ascorbic acid in passaged primary human chondrocytes to discern the physiologically relevant pathways of ascorbic acid transport in cartilage. We have found that chondrocytes are robust concentrators of ascorbic acid, capable of transporting the reduced form, and concentrating total ascorbic acid, in the reduced form and its metabolites, 960-fold over the concentration in the extracellular milieu. Chondrocyte transport of ascorbic acid was sodium and temperature dependent, stereoselective for the L-forms, and inhibited by the anion transport inhibitor, sulfinpyrazone. Chondrocytes preferentially expressed the full-length and functional isoform of sodium-dependent vitamin C transporter 2 (SVCT2). When this transcript was suppressed with sequence-specific siRNAs, the active transport component of ascorbic acid was abolished. Thus, we provide the first evidence that SVCT2 mediates the secondary active and concentrative transport of ascorbic acid in human chondrocytes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
1712
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
212-21
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:15921655-Amino Acids, pubmed-meshheading:15921655-Ascorbic Acid, pubmed-meshheading:15921655-Cartilage, pubmed-meshheading:15921655-Cell Survival, pubmed-meshheading:15921655-Chondrocytes, pubmed-meshheading:15921655-Chromatography, High Pressure Liquid, pubmed-meshheading:15921655-Dehydroascorbic Acid, pubmed-meshheading:15921655-Glucose, pubmed-meshheading:15921655-Humans, pubmed-meshheading:15921655-Kinetics, pubmed-meshheading:15921655-Organic Anion Transporters, Sodium-Dependent, pubmed-meshheading:15921655-RNA, pubmed-meshheading:15921655-RNA Interference, pubmed-meshheading:15921655-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:15921655-Sodium, pubmed-meshheading:15921655-Sodium-Coupled Vitamin C Transporters, pubmed-meshheading:15921655-Sulfinpyrazone, pubmed-meshheading:15921655-Symporters, pubmed-meshheading:15921655-Temperature, pubmed-meshheading:15921655-Time Factors
pubmed:year
2005
pubmed:articleTitle
Chondrocyte transport and concentration of ascorbic acid is mediated by SVCT2.
pubmed:affiliation
Department of Pathology, Duke University Medical Center, Box 3416, Durham, NC 27710, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural