rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1994-2-4
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pubmed:abstractText |
We made a mutated progastrin cDNA construct that contains a cleavage site (-Arg(-4)-Arg(-3)-Lys(-2)-Arg-1) specific for the Kex2-like endoprotease furin, located ahead of the bioactive gastrin. For expressing the mutated progastrin cDNA, we used two non-endocrine cell lines, CHO and COS-7. CHO cells exhibit amidating enzyme activity and levels of amidation enzyme mRNA as high as those in the pituitary-derived endocrine cell line GH3, whereas COS-7 cells have far less amidating activity and lower amounts of mRNA. Mutant progastrin-expressing CHO cells produced mostly amidated gastrin. Gel filtration showed the size of this gastrin corresponded to that of the synthetic human gastrin-17. In contrast, COS-7 cells produced glycine-extended gastrin and only a small amount of amidated gastrin. The difference in the amount of amidated gastrin products produced by the two non-endocrine cell lines is due to differing amounts of the amidation enzyme contained in each cell line.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Furin,
http://linkedlifedata.com/resource/pubmed/chemical/Gastrins,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Subtilisins,
http://linkedlifedata.com/resource/pubmed/chemical/big gastrin,
http://linkedlifedata.com/resource/pubmed/chemical/peptidylglycine monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
337
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8276107-Amino Acid Sequence,
pubmed-meshheading:8276107-Animals,
pubmed-meshheading:8276107-Binding Sites,
pubmed-meshheading:8276107-CHO Cells,
pubmed-meshheading:8276107-Cell Line,
pubmed-meshheading:8276107-Cercopithecus aethiops,
pubmed-meshheading:8276107-Chromatography, Gel,
pubmed-meshheading:8276107-Cricetinae,
pubmed-meshheading:8276107-DNA, Complementary,
pubmed-meshheading:8276107-Furin,
pubmed-meshheading:8276107-Gastrins,
pubmed-meshheading:8276107-Gene Expression,
pubmed-meshheading:8276107-Humans,
pubmed-meshheading:8276107-Kidney,
pubmed-meshheading:8276107-Mixed Function Oxygenases,
pubmed-meshheading:8276107-Molecular Sequence Data,
pubmed-meshheading:8276107-Multienzyme Complexes,
pubmed-meshheading:8276107-Mutagenesis,
pubmed-meshheading:8276107-Protein Precursors,
pubmed-meshheading:8276107-RNA, Messenger,
pubmed-meshheading:8276107-Rats,
pubmed-meshheading:8276107-Subtilisins,
pubmed-meshheading:8276107-Transfection
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pubmed:year |
1994
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pubmed:articleTitle |
Production of bioactive gastrin from the non-endocrine cell lines CHO and COS-7.
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pubmed:affiliation |
Division of Molecular Endocrinology, Gunma University, Maebashi, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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