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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1992-7-24
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pubmed:abstractText |
The cloning of the cDNA encoding von Willebrand factor (vWF) has revealed that it is synthesized as a large precursor (pre-pro-vWF) molecule and it is now clear that the prosequence or vWAgII is responsible for the intracellular multimerization of vWF. We have cloned the complete vWF cDNA and expressed it using a recombinant vaccinia virus as vector. We have characterized the structure and function of the recombinant vWF (rvWF) secreted from five different cell types: baby hamster kidney (BHK), Chinese hamster ovary (CHO), human fibroblasts (143B), mouse fibroblasts (L) and primary embryonic chicken cells. Forty-eight hours after infection, the quantity of vWF antigen found in the cell supernatant varied from 3 to 12 U/dl depending on the cell type. By SDS-agarose gel electrophoresis, the percentage of high molecular weight forms of vWF varied from 39 to 49% relative to normal plasma for BHK, CHO, 143B and chicken cells but was less than 10% for L cells. In all cell types, the two anodic subbands of each multimer were missing. The two cathodic subbands were easily detected only in BHK and L cells. By SDS-PAGE of reduced samples, pro-vWF was present in similar quantity to the fully processed vWF subunit in L cells, present in moderate amounts in BHK and CHO and in very low amounts in 143B and chicken cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Factor VIII,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/von Willebrand Factor
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0340-6245
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
67
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
154-60
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1615470-Animals,
pubmed-meshheading:1615470-Blood Platelets,
pubmed-meshheading:1615470-Cells, Cultured,
pubmed-meshheading:1615470-Collagen,
pubmed-meshheading:1615470-DNA,
pubmed-meshheading:1615470-Factor VIII,
pubmed-meshheading:1615470-Genetic Vectors,
pubmed-meshheading:1615470-Humans,
pubmed-meshheading:1615470-Protein Processing, Post-Translational,
pubmed-meshheading:1615470-Recombinant Proteins,
pubmed-meshheading:1615470-Vaccinia virus,
pubmed-meshheading:1615470-von Willebrand Factor
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pubmed:year |
1992
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pubmed:articleTitle |
Processing and characterization of recombinant von Willebrand factor expressed in different cell types using a vaccinia virus vector.
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pubmed:affiliation |
Transgène S.A., Strasbourg, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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