Eglin c, a pharmacologically active elastase inhibitor
Pharmacology article published in European Journal of Respiratory Diseases Supplement (1985)
Abstract
Eglin c is an elastase/cathepsin G inhibitor from leech Hirudo medicinalis. The gene for this 70 aminoacid peptide was synthesized chemically, cloned and expressed by E. coli. Here we report biochemical and pharmacological studies. The rate of complex formation between Eglin c and human leukocyte elastase (HLE) or human cathepsin G (H. Cat. G) was determined and compared to those of a number of other proteinase/proteinase-inhibitor interactions (alpha 1 PI and alpha 2M). The association rate constants of Eglin c with the leukocyte enzymes are of the same order of magnitude as those with the naturally occurring inhibitors alpha 1 PI and alpha 2M. The association rate constant of Eglin c (extracted from leech) and Eglin c (biotechnology product) with HLE was found to be identical. The equilibrium constants Ki of the Eglin c/HLE and the Eglin c/H. Cat. G interactions are in the order of 10(-10) M. In an experiment with the hamster emphysema model, 0.5 mg or 2 mg of Eglin c applied intratracheally one hour before an HLE-insult completely protected the animals against emphysema and no signs of toxicity due to Eglin c were observed.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Zusammenfassung
Biochemical and pharmacological characterization of recombinant leech eglin c versus natural eglin c, showing identical association rate constants with human leukocyte elastase and complete protection against HLE-induced emphysema in hamsters.
Warum dies für die Hirudotherapie relevant ist
This study characterizes eglin c, an elastase/cathepsin G inhibitor from Hirudo medicinalis, including its chemical gene synthesis, cloning, and expression in E. coli. The abstract reports that association rate constants with human leukocyte elastase and cathepsin G are comparable to natural inhibitors (α1-PI, α2M), equilibrium constants (Ki) are on the order of 10⁻¹⁰ M, and recombinant eglin c was identical in activity to leech-extracted eglin c. In a hamster emphysema model, intratracheal eglin c completely protected against HLE-induced emphysema with no toxicity. This is relevant to ASH's domain as it characterizes a pharmacologically active component of the leech secretome beyond hirudin, demonstrating the breadth of bioactive molecules in leech saliva. However, the study is preclinical (animal model) and involves a recombinant protein rather than whole-organism leech therapy.
Zitation
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