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rdf:type |
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lifeskim:mentions |
umls-concept:C0003280,
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0017262,
umls-concept:C0033684,
umls-concept:C0052098,
umls-concept:C0185117,
umls-concept:C0679058,
umls-concept:C0871161,
umls-concept:C1547699,
umls-concept:C2700640,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
1989-6-26
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pubmed:databankReference |
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pubmed:abstractText |
As a factor Xa inhibitor, antistasin is a potent anti-coagulant and anti-metastatic agent that is found in the salivary gland of the Mexican leech Haementaria officinalis. cDNA clones that encode antistasin have been isolated. Subsequent sequence analysis and comparison with the amino acid sequence of the mature protein indicates that antistasin is produced as a pre-protein containing a 17-amino acid signal peptide. Antistasin exists as at least two variants. By sequence analysis of multiple cDNA clones, we found two additional sites for amino acid substitutions, confirming variants that differ from each other by amino acid changes at a minimum of four residues. These sequence variations appear to be the result of allelic variation rather than gene duplication as deduced from DNA blot analyses. Sequence data suggest that antistasin may have evolved from a smaller ancestral gene by a duplication event giving rise to a two-fold structural homology between the N- and C-terminal halves of the molecule. Insect cells transfected with a recombinant baculovirus expressed antistasin which was biologically active and had an electrophoretic mobility identical to that of the native molecule.
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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/Anticoagulants,
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Factor Xa,
http://linkedlifedata.com/resource/pubmed/chemical/Invertebrate Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Salivary Proteins and Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/antistasin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
47-57
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2470652-Amino Acid Sequence,
pubmed-meshheading:2470652-Animals,
pubmed-meshheading:2470652-Anticoagulants,
pubmed-meshheading:2470652-Antineoplastic Agents,
pubmed-meshheading:2470652-Base Sequence,
pubmed-meshheading:2470652-Blotting, Southern,
pubmed-meshheading:2470652-Cloning, Molecular,
pubmed-meshheading:2470652-Culture Media,
pubmed-meshheading:2470652-DNA,
pubmed-meshheading:2470652-Factor Xa,
pubmed-meshheading:2470652-Gene Expression Regulation,
pubmed-meshheading:2470652-Genetic Variation,
pubmed-meshheading:2470652-Immunoblotting,
pubmed-meshheading:2470652-Invertebrate Hormones,
pubmed-meshheading:2470652-Leeches,
pubmed-meshheading:2470652-Molecular Sequence Data,
pubmed-meshheading:2470652-Neoplasm Metastasis,
pubmed-meshheading:2470652-Protein Biosynthesis,
pubmed-meshheading:2470652-RNA,
pubmed-meshheading:2470652-RNA, Messenger,
pubmed-meshheading:2470652-Salivary Proteins and Peptides,
pubmed-meshheading:2470652-Serine Endopeptidases,
pubmed-meshheading:2470652-Serine Proteinase Inhibitors,
pubmed-meshheading:2470652-Transcription, Genetic
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pubmed:year |
1989
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pubmed:articleTitle |
Cloning and expression of cDNA encoding antistasin, a leech-derived protein having anti-coagulant and anti-metastatic properties.
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pubmed:affiliation |
Department of Cellular, Merck Sharp & Dohme Research Laboratories, West Point, PA.
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pubmed:publicationType |
Journal Article
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