Source:http://linkedlifedata.com/resource/pubmed/id/11278568
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
2001-5-23
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pubmed:databankReference | |
pubmed:abstractText |
Enterocyte terminal differentiation occurs at the crypt-villus junction through the transcriptional activation of cell-specific genes, many of which code for proteins of the brush border membrane such as intestinal alkaline phosphatase, sucrase-isomaltase, or the microvillar structural protein villin. Several studies have shown that this sharp increase in specific mRNA levels is intimately associated with arrest of cell proliferation. We isolated several clones from a guinea pig intestine cDNA library. They encode new proteins characterized by an original structure associating a carboxyl-terminal B30.2/RFP-like domain and a long leucine zipper at the amino terminus. The first member of this novel gene family codes for a 65-kDa protein termed enterophilin-1, which is specifically expressed in enterocytes before their final differentiation. Enterophilin-1 is the most abundant in the small intestine but is still present in significant amounts in colonic enterocytes. In Caco-2 cells, a similar 65-kDa protein was recognized by a specific anti-enterophilin-1 antibody, and its expression was positively correlated with cell differentiation status. In addition, transfection of HT-29 cells with enterophilin-1 full-length cDNA slightly inhibited cell growth and promoted an increase in alkaline phosphatase activity. Taken together, these data identify enterophilins as a new family of proteins associated with enterocyte differentiation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18352-60
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11278568-Amino Acid Sequence,
pubmed-meshheading:11278568-Animals,
pubmed-meshheading:11278568-Carrier Proteins,
pubmed-meshheading:11278568-Cell Differentiation,
pubmed-meshheading:11278568-Cells, Cultured,
pubmed-meshheading:11278568-Cloning, Molecular,
pubmed-meshheading:11278568-DNA, Complementary,
pubmed-meshheading:11278568-Enterocytes,
pubmed-meshheading:11278568-Leucine Zippers,
pubmed-meshheading:11278568-Molecular Sequence Data,
pubmed-meshheading:11278568-Proteins,
pubmed-meshheading:11278568-Sequence Alignment
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pubmed:year |
2001
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pubmed:articleTitle |
Enterophilins, a new family of leucine zipper proteins bearing a b30.2 domain and associated with enterocyte differentiation.
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pubmed:affiliation |
Institut Fédératif de Recherche Claude de Préval, Université Paul Sabatier and Centre Hospitalo-Universitaire de Toulouse, INSERM Unité 326, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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