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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1992-12-30
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M85175,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M85176,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M85177,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M93264,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X65179,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X65180,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X65181,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X68289,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X68290,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X68291
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pubmed:abstractText |
Mouse plasma alpha-2-macroglobulin (m alpha 2M) was isolated and the N-terminal amino-acid sequences determined after separation of the 165-kDa and 35-kDa subunits. These sequences were compared to the protein sequence predicted by the cDNA, which was cloned from a mouse liver library and sequenced. From these data it is evident that both subunits are encoded by one mRNA of approximately 5 kb expressed predominantly in liver. The smaller subunit, with the N-terminal sequence DLSSSDLT, comprises the C-terminal 257 residues of m alpha 2M and is derived from a single-chain precursor probably by proteolytic processing at an arginine residue in the sequence PTRDLSS. Analysis of the predicted protein further showed all the salient features of a proteinase inhibitor of the macroglobulin family: a bait region that deviates from all known sequences in this family, a very conserved internal thiolester site and conserved cysteine residues and putative N-glycosylation sites. The synthesis of m alpha 2M in adult liver was demonstrated by Northern blotting and in fetal liver by in-situ hybridization. Transient transfection of COS cells with the cDNA under control of a viral promoter demonstrated the secretion and partial processing of m alpha 2M in the culture medium. In plasma the level of m alpha 2M was found to be stable as expected for the murine counterpart of human plasma alpha-2-macroglobulin. The possibilities of using the mouse as a genetic model to study this proteinase inhibitor in vivo are discussed.
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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 |
Nov
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
210
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
319-27
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:1280217-Amino Acid Sequence,
pubmed-meshheading:1280217-Animals,
pubmed-meshheading:1280217-Base Sequence,
pubmed-meshheading:1280217-Blotting, Northern,
pubmed-meshheading:1280217-Cloning, Molecular,
pubmed-meshheading:1280217-DNA,
pubmed-meshheading:1280217-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1280217-In Situ Hybridization,
pubmed-meshheading:1280217-Mice,
pubmed-meshheading:1280217-Molecular Sequence Data,
pubmed-meshheading:1280217-Plasmids,
pubmed-meshheading:1280217-RNA,
pubmed-meshheading:1280217-Sequence Homology, Amino Acid,
pubmed-meshheading:1280217-alpha-Macroglobulins
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pubmed:year |
1992
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pubmed:articleTitle |
The primary sequence and the subunit structure of mouse alpha-2-macroglobulin, deduced from protein sequencing of the isolated subunits and from molecular cloning of the cDNA.
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pubmed:affiliation |
Center for Human Genetics, Katholieke Universiteit Leuven, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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