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Declining body sizes in North American birds associated with climate change


Van Buskirk, J; Mulvihill, R S; Lebermann, R C (2010). Declining body sizes in North American birds associated with climate change. Oikos, 119(6):1047-1055.

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 α-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

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 α-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.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Institute of Evolutionary Biology and Environmental Studies
Dewey Decimal Classification:570 Life sciences; biology
590 Animals (Zoology)
Language:English
Date:2010
Deposited On:14 Jul 2010 20:07
Last Modified:21 Nov 2017 14:53
Publisher:Wiley-Blackwell
ISSN:0030-1299
Publisher DOI:https://doi.org/10.1111/j.1600-0706.2009.18349.x

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