Paradoxical interactions between modifiers and elastase-2
Research article published in The FEBS journal (2010)
Abstract
The serine endopeptidase elastase-2 from human polymorphonuclear leukocytes is associated with physiological remodeling and pathological degradation of the extracellular matrix. Glycosaminoglycans bound to the matrix or released after proteolytic processing of the core proteins of proteoglycans are potential ligands of elastase-2. In vitro, this interaction results in enzyme inhibition at low concentrations of glycosaminoglycans. However, inhibition is reversed and even abolished at high concentrations of the ligands. This behavior, which can be interpreted by a mechanism involving at least two molecules of glycosaminoglycan binding the enzyme at different sites, may cause interference with the natural protein inhibitors of elastase-2, particularly the alpha-1 peptidase inhibitor. Depending on their concentration, glycosaminoglycans can either stimulate or antagonize the formation of the enzyme-inhibitor complex and thus affect proteolytic activity. This interference with elastase-2 inhibition in the extracellular space may be part of a finely-tuned control mechanism in the microenvironment of the enzyme during remodeling and degradation of the extracellular matrix.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Summary
The serine endopeptidase elastase-2 from human polymorphonuclear leukocytes is associated with physiological remodeling and pathological degradation of the extracellular matrix.
Why This Matters for Hirudotherapy
This in vitro study investigated how glycosaminoglycans interact with human elastase-2 from polymorphonuclear leukocytes, demonstrating that these ligands inhibit the enzyme at low concentrations but reverse or abolish inhibition at higher concentrations. The authors propose a mechanism involving at least two glycosaminoglycan binding sites and suggest this interaction may interfere with natural protein inhibitors such as alpha-1 peptidase inhibitor, thereby modulating proteolytic activity in the extracellular matrix during remodeling and degradation. The abstract provides no data on leeches, the leech secretome, hirudin, or any leech-derived compounds, and its focus is exclusively on human enzymes and human matrix components. Therefore, this article has no apparent relevance to the American Society of Hirudotherapy based on its abstract.
Citation
Paradoxical interactions between modifiers and elastase-2
Schenker P et al. · The FEBS journal, 2010
Added to ASH library: May 27, 2026 · Site last updated: June 18, 2026