Cloning and expression of cDNA encoding antistasin, a leech-derived protein having anti-coagulant and anti-metastatic properties
Research article published in Gene (1989)
Abstract
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.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Summary
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.
Why This Matters for Hirudotherapy
This study isolated and characterized cDNA clones encoding antistasin, a factor Xa inhibitor with anticoagulant and anti-metastatic properties from the salivary gland of the Mexican leech Haementaria officinalis. Sequence analysis revealed that antistasin is produced as a pre-protein with a 17-amino acid signal peptide, exists as at least two variants due to allelic variation, and may have evolved via duplication of a smaller ancestral gene. Baculovirus-expressed recombinant antistasin was biologically active with electrophoretic mobility identical to the native molecule. This is directly relevant to ASH's domain, as it characterizes a potent anticoagulant from the leech salivary secretome at the molecular level and demonstrates functional recombinant expression. However, the study is preclinical molecular biology with no in vivo or clinical hirudotherapy data, so therapeutic relevance remains indirect.
Citation
Cloning and expression of cDNA encoding antistasin, a leech-derived protein having anti-coagulant and anti-metastatic properties.
Han JH et al. · Gene, 1989
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