Source:http://linkedlifedata.com/resource/pubmed/id/21505192
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
24
|
| pubmed:dateCreated |
2011-6-17
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| pubmed:abstractText |
Alpha-2-antiplasmin (?2AP) undergoes both N- and C-terminal cleavages, which significantly modify its activities. Compared with other Ser protease inhibitors (serpins), ?2AP contains an ~50-residue-extended C-terminus, which binds plasmin(ogen). We developed 2 new ELISAs to measure the antigen levels of free total ?2AP and free C-terminally intact ?2AP to investigate whether ?2AP antigen levels or ?2AP C-terminal cleavage were associated with myocardial infarction (MI) in 320 male MI survivors and 169 age-matched controls. Patients had 15.2% reduced total ?2AP antigen levels compared with controls (93.8 vs 110.6 U/dL, P < .001), with a 10.1-fold (95% confidence interval [CI]: 5.5-18.9) increased MI risk for levels in the 1st quartile compared with the 4th quartile. The percentage of C-terminal cleavage did not differ between patients and controls (38.7% and 38.1%, respectively, P = .44). In addition, all individuals were genotyped for the polymorphism Arg407Lys, which is located near the start of the extended C-terminus. Arg407Lys was not associated with ?2AP C-terminal cleavage, total ?2AP antigen levels, or MI risk (odds ratios compared with Arg/Arg: Arg/Lys 0.74, 95% CI: 0.50-1.10; Lys/Lys 0.77, 95% CI: 0.31-1.92). Our data show that levels of free full-length ?2AP were decreased in MI, that the percentage of C-terminally cleaved ?2AP was unaltered, and that Arg407Lys did not influence ?2AP levels or MI risk.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
1528-0020
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
16
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| pubmed:volume |
117
|
| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6694-701
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| pubmed:meshHeading |
pubmed-meshheading:21505192-Adult,
pubmed-meshheading:21505192-Amino Acid Sequence,
pubmed-meshheading:21505192-Amino Acid Substitution,
pubmed-meshheading:21505192-Arginine,
pubmed-meshheading:21505192-Case-Control Studies,
pubmed-meshheading:21505192-Genotype,
pubmed-meshheading:21505192-Humans,
pubmed-meshheading:21505192-Lysine,
pubmed-meshheading:21505192-Male,
pubmed-meshheading:21505192-Middle Aged,
pubmed-meshheading:21505192-Molecular Sequence Data,
pubmed-meshheading:21505192-Mutation, Missense,
pubmed-meshheading:21505192-Myocardial Infarction,
pubmed-meshheading:21505192-Polymorphism, Single Nucleotide,
pubmed-meshheading:21505192-Protein Processing, Post-Translational,
pubmed-meshheading:21505192-Protein Structure, Tertiary,
pubmed-meshheading:21505192-Sequence Homology, Amino Acid,
pubmed-meshheading:21505192-Validation Studies as Topic,
pubmed-meshheading:21505192-alpha-2-Antiplasmin
|
| pubmed:year |
2011
|
| pubmed:articleTitle |
Proteolytic and genetic variation of the alpha-2-antiplasmin C-terminus in myocardial infarction.
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| pubmed:affiliation |
Division of Cardiovascular & Diabetes Research, Section on Mechanisms of Thrombosis, Faculty of Medicine and Health, University of Leeds, Leeds, UK.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|