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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-34738

Schenker, P; Baici, A (2010). Paradoxical interactions between modifiers and elastase-2. FEBS Journal, 277(11):2486-2495.

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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.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
DDC:570 Life sciences; biology
Deposited On:13 Jul 2010 18:26
Last Modified:03 Feb 2014 07:39
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1111/j.1742-4658.2010.07663.x
PubMed ID:20553487
Citations:Web of Science®. Times Cited: 4
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Scopus®. Citation Count: 5

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