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pubmed-article:16128292pubmed:dateCreated2005-8-30lld:pubmed
pubmed-article:16128292pubmed:abstractTextProduction of albumin and urea by mouse hepatocytes on poly(vinylalcohol-co-ethylamine) (PVA-EA) membranes containing immobilized extracellular matrix (ECM) proteins was investigated for 7 days. The amount of ECM proteins (collagen, vitronectin and laminin) immobilized on PVA-EA and PVA-ECM membranes was determined to range from 1.09 microg/cm2 to 1.60 microg/cm2. Hepatocytes cultured on PVA-ECM membranes in serum-free media showed higher albumin production than those cultured on PVA-EA membranes after a 7-day incubation under the conditions in this study. Urea production by hepatocytes on PVA-ECM membranes was also determined to be higher than that on PVA-EA membranes up until day 5 of incubation in serum-free media, whereas no difference of urea production by hepatocytes on different PVA-ECM membranes and PVA-EA membranes was observed at 7 days of incubation. The effect of ECM proteins in PVA-ECM membranes on hepatocyte function (such as albumin and urea production) was observed in hepatocytes cultured in serum-free media up to day 5 of incubation. The ECM proteins immobilized on the PVA-ECM membranes contributed not only to the long-term stable production of albumin and urea by hepatocytes, but also the improved surviVal (viability) of hepatocytes on PVA-ECM membranes.lld:pubmed
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pubmed-article:16128292pubmed:pagination847-60lld:pubmed
pubmed-article:16128292pubmed:dateRevised2008-2-20lld:pubmed
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pubmed-article:16128292pubmed:articleTitleAlbumin and urea production by hepatocytes cultured on extracellular matrix proteins-conjugated poly(vinyl alcohol) membranes.lld:pubmed
pubmed-article:16128292pubmed:affiliationDepartment of Applied Chemistry, Seikei University, 3-3-1 Kichijoji Kitamachi, Musashino, Tokyo 180-8633, Japan. higuchi@ch.seikei.ac.jplld:pubmed
pubmed-article:16128292pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16128292pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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