Source:http://linkedlifedata.com/resource/pubmed/id/10767986
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2000-5-4
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pubmed:abstractText |
The large scale production of recombinant collagen for use in biomaterials requires an efficient expression system capable of processing a large (> 400 Kd) multisubunit protein requiring post-translational modifications. To investigate whether the mammary gland of transgenic animals fulfills these requirements, transgenic mice were generated containing the alpha S1-casein mammary gland-specific promoter operatively linked to 37 Kb of the human alpha 1(I) procollagen structural gene and 3' flanking region. The frequency of transgenic lines established was 12%. High levels of soluble triple helical homotrimeric [(alpha 1)3] type I procollagen were detected (up to 8 mg/ml) exclusively in the milk of six out of 9 lines of lactating transgenic mice. The transgene-derived human procollagen chains underwent efficient assembly into a triple helical structure. Although proline or lysine hydroxylation has never been described for any milk protein, procollagen was detected with these post-translational modifications. The procollagen was stable in milk; minimal degradation was observed. These results show that the mammary gland is capable of expressing a large procollagen gene construct, efficiently assembling the individual polypeptide chains into a stable triple helix, and secreting the intact molecule into the milk.
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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/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Procollagen,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
0962-8819
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
415-27
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10767986-Amino Acids,
pubmed-meshheading:10767986-Animals,
pubmed-meshheading:10767986-Dimerization,
pubmed-meshheading:10767986-Female,
pubmed-meshheading:10767986-Gene Expression Regulation,
pubmed-meshheading:10767986-Humans,
pubmed-meshheading:10767986-Lysine,
pubmed-meshheading:10767986-Mammary Glands, Animal,
pubmed-meshheading:10767986-Mice,
pubmed-meshheading:10767986-Mice, Transgenic,
pubmed-meshheading:10767986-Milk,
pubmed-meshheading:10767986-Procollagen,
pubmed-meshheading:10767986-Proline,
pubmed-meshheading:10767986-Promoter Regions, Genetic,
pubmed-meshheading:10767986-Protein Processing, Post-Translational,
pubmed-meshheading:10767986-Recombinant Proteins,
pubmed-meshheading:10767986-Transgenes
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pubmed:year |
1999
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pubmed:articleTitle |
Production of recombinant human type I procollagen homotrimer in the mammary gland of transgenic mice.
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pubmed:affiliation |
Cohesion Technologies, Palo Alto, CA 94303, USA. dtoman@cson.com
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pubmed:publicationType |
Journal Article
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