Source:http://linkedlifedata.com/resource/pubmed/id/15051835
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2004-3-30
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pubmed:abstractText |
An important dietary source of vitamin B-6, pyridoxine-5'-beta-D-glucoside (PNG), exhibits only partial bioavailability, which is limited by the extent of enzymatic cleavage of the beta-glucosidic bond to release metabolically available pyridoxine (PN). This laboratory showed that the intestinal hydrolysis of PNG is catalyzed by cytosolic PNG hydrolase (PNGH) and brush border lactase-phlorizin hydrolase (LPH). LPH-catalyzed PNG hydrolysis in vitro is competitively inhibited by lactose. In the present study, the uptake and hydrolysis of PNG were examined in Caco-2 human colon carcinoma cells, which express a functional LPH but exhibit no PNGH activity. PNG uptake at 37 degrees C was linear over 5-500 micromol/L PNG. Uptake was not significantly reduced when Na(+) was substituted with K(+), Li(+), or Tris in the medium. Increasing PNG concentration in the medium did not change intracellular concentrations of PN, pyridoxamine (PM), pyridoxamine 5'-phosphate (PMP), or pyridoxal 5'-phosphate (PLP); however, intracellular pyridoxal (PL) concentration increased. Intracellular PNG concentration was not significantly reduced in the presence of lactose, but the concentration of PL declined in proportion to extracellular lactose (P = 0.01). These results indicate that PNG can be absorbed intact in a Na(+)-independent process and is taken up by passive diffusion. The presence of lactose in this in vitro model of intestinal uptake reduced the enzymatic hydrolysis of PNG by lactase.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5'-O-(glucopyranosyl)pyridoxine,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosides,
http://linkedlifedata.com/resource/pubmed/chemical/Lactase,
http://linkedlifedata.com/resource/pubmed/chemical/Lactose,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxal,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxine,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0022-3166
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
134
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
842-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15051835-Caco-2 Cells,
pubmed-meshheading:15051835-Glucosides,
pubmed-meshheading:15051835-Humans,
pubmed-meshheading:15051835-Hydrolysis,
pubmed-meshheading:15051835-Kinetics,
pubmed-meshheading:15051835-Lactase,
pubmed-meshheading:15051835-Lactose,
pubmed-meshheading:15051835-Pyridoxal,
pubmed-meshheading:15051835-Pyridoxine,
pubmed-meshheading:15051835-Sodium
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pubmed:year |
2004
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pubmed:articleTitle |
Uptake, hydrolysis, and metabolism of pyridoxine-5'-beta-D-glucoside in Caco-2 cells.
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pubmed:affiliation |
Food Science and Human Nutrition Department, University of Florida, Gainesville, FL, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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