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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1997-3-13
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pubmed:abstractText |
We previously reported that lactose handling was significantly improved during late-phase pregnancy in women with a genetically determined adult-type hypolactasia. However, the adaptive mechanisms underlying the enhanced lactose digestion during pregnancy are not clear. Progesterone therapy has been associated in animals with increased intestinal lactase activity. To investigate the potential role of progesterone and estrogen as modulators of human lactase activity during pregnancy, we employed the human-derived intestinal epithelial Caco-2 cell line. Measurements of lactase and sucrase activities were performed in parallel with DNA content in progesterone- and estrogen-treated cells after 5, 10, and 30 days of confluency. Caco-2 monolayer DNA content was observed to increase with duration of culture to an equivalent extent in both hormone-treated and control cultures. Lactase and sucrase activities were similarly unaltered by incubation with either progesterone or estrogen, at any time point tested. These data demonstrate that gestational hormones do not influence intestinal cell number nor disaccharidase activity in Caco-2 cells, at the doses tested. Although these studies were carried out in a malignant cell line, our data suggest that the improved lactose handling observed during pregnancy is probably related to prolonged intestinal transit.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharidases,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogens,
http://linkedlifedata.com/resource/pubmed/chemical/Lactase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Progesterone,
http://linkedlifedata.com/resource/pubmed/chemical/Sucrase,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0008-4212
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1126-31
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9022832-Caco-2 Cells,
pubmed-meshheading:9022832-Cell Membrane,
pubmed-meshheading:9022832-DNA,
pubmed-meshheading:9022832-Disaccharidases,
pubmed-meshheading:9022832-Estrogens,
pubmed-meshheading:9022832-Female,
pubmed-meshheading:9022832-Humans,
pubmed-meshheading:9022832-Lactase,
pubmed-meshheading:9022832-Membrane Proteins,
pubmed-meshheading:9022832-Progesterone,
pubmed-meshheading:9022832-Sucrase,
pubmed-meshheading:9022832-beta-Galactosidase
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pubmed:year |
1996
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pubmed:articleTitle |
Caco-2 cell disaccharidase activities are unaffected by gestational hormones.
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pubmed:affiliation |
Hôpital Ste-Justine, Department of Pediatrics, Université de Montréal, QC, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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