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Enzyme Linked Immunosorbent Assays (ELISA) for the Quantitative Determination of Human Leukocyte Collagenase and Gelatinase

Enzyme Linked Immunosorbent Assays (ELISA) for the Quantitative Determination of Human Leukocyte... Introduction Inflammatory processes are associated with the release of proteolytic enzymes from phagocytic leukocytes (1). In addition to the serine proteinases, cathepsin G and elastase, leukocytes have been shown to contain the metalloenzymes collagenase1) and gelatinase1) (2--4). All these proteases are äble to degrade connective tissüe components and thus might be involved in pathological conditions such äs rheumathoid arthritis, tumour invasion, gout, pr emphysema (5). Although elastase is able to degrade collagen (6, 7), collagenase and gelatinase are the specific enzymes that are mainly responsible for the coliagen breakdown mediated by leukocytes (8, 9). * In order to study the release and function of these enzymes in body fluids and tissues, a highly sensitive and specific assay procedure is a prerequisite. Collagenase and gelatinase concentrations are commonly determined by measuring their proteolytic activity against natural or synthetic Substrates (for a review see I.e. (10, 11)). The assay of Substrate degradation is achieved by using radioactive, fluorescent (12) or chromophore labelled Substrates, äs well äs by measuring the change in physical parameters such äs viscosity or UV-absorbance (13). Substrate degradation was also detected by reacting the cleavage products with fluorescamine, which allows the assay of the amino groups generated http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Clinical Chemistry and Laboratory Medicine de Gruyter

Enzyme Linked Immunosorbent Assays (ELISA) for the Quantitative Determination of Human Leukocyte Collagenase and Gelatinase

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Publisher
de Gruyter
Copyright
Copyright © 2009 Walter de Gruyter
ISSN
1434-6621
eISSN
1437-4331
DOI
10.1515/cclm.1989.27.6.351
Publisher site
See Article on Publisher Site

Abstract

Introduction Inflammatory processes are associated with the release of proteolytic enzymes from phagocytic leukocytes (1). In addition to the serine proteinases, cathepsin G and elastase, leukocytes have been shown to contain the metalloenzymes collagenase1) and gelatinase1) (2--4). All these proteases are äble to degrade connective tissüe components and thus might be involved in pathological conditions such äs rheumathoid arthritis, tumour invasion, gout, pr emphysema (5). Although elastase is able to degrade collagen (6, 7), collagenase and gelatinase are the specific enzymes that are mainly responsible for the coliagen breakdown mediated by leukocytes (8, 9). * In order to study the release and function of these enzymes in body fluids and tissues, a highly sensitive and specific assay procedure is a prerequisite. Collagenase and gelatinase concentrations are commonly determined by measuring their proteolytic activity against natural or synthetic Substrates (for a review see I.e. (10, 11)). The assay of Substrate degradation is achieved by using radioactive, fluorescent (12) or chromophore labelled Substrates, äs well äs by measuring the change in physical parameters such äs viscosity or UV-absorbance (13). Substrate degradation was also detected by reacting the cleavage products with fluorescamine, which allows the assay of the amino groups generated

Journal

Clinical Chemistry and Laboratory Medicine – de Gruyter

Published: Jan 1, 1989

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