Comparison of neutrophil elastases and of neutrophil protease inhibitors in the horse and man.
Abstract: Neutral neutrophil protease, elastase activities, and cytosol protease inhibitors of these enzymes of horses and man were compared. Human neutrophils had 5 times the elastase activity of equine neutrophils, and neutral protease activity was approximately 50% greater in human neutrophils than that in equine neutrophils. Cytosol inhibitors for elastase and neutral proteases were not found in human neutrophils, whereas large amounts were found in equine neutrophils. Using fibrinogen-agarose electrophoresis, 4 cytosol inhibitors of different enzyme specificities were detected. These cytosol inhibitors were differentiated on the basis of different electrophoretic migration and on the basis of differences in enzyme specificity.
Publication Date: 1985-12-01 PubMed ID: 3853453
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article compares the activities of neutrophil elastase (a type of enzyme) and neutrophil protease inhibitors (substances that reduce the activity of certain enzymes) in horses and humans. The findings indicate that human neutrophils exhibit higher elastase and neutral protease activity than equine neutrophils. In contrast, cytosol inhibitors for these enzymes were found in substantial amounts in equine neutrophils, but not in human neutrophils.
Overview of Enzymes and Inhibitors
- The study focuses on two biological substances: neutrophil elastases and neutrophil protease inhibitors. Neutrophil elastases are enzymes found in neutrophils, white blood cells that aid in immune response. Neutrophil protease inhibitors, on the other hand, deter the activity of proteases, enzymes that break down proteins and peptides.
- The enzyme activity refers to the rate at which these enzymes execute their biochemical tasks. In this context, the researchers compared the effectiveness of these enzymes in human and horse neutrophils.
Findings on Neutrophil Elastase and Neutral Protease Activity
- The researchers found that human neutrophils had approximately 5 times greater elastase activity than equine neutrophils. This implies that human neutrophils are more efficient at processing certain substances assisted by elastase than horse neutrophils.
- Moreover, neutral protease activity was about 50% higher in human neutrophils than in horse neutrophils. This demonstrates that human neutrophils have a heightened capability to break down proteins, facilitated by neutral proteases.
Findings on Cytosol Inhibitors
- Cytosol inhibitors are substances found in the cytoplasm of cells that reduce enzyme activity. Interestingly, the study found these inhibitors in large amounts in horse neutrophils but not in human neutrophils.
- Using a method called fibrinogen-agarose electrophoresis, the researchers identified four different cytosol inhibitors in the equine neutrophils. These inhibitors were differentiated based on their migration during electrophoresis and their specific enzyme targets.
- The presence of these inhibitors in horse neutrophils, but not in human neutrophils, is important as it highlights the variation in cellular mechanisms between different species. These differences could influence how these organisms respond to various biological events, such as infection or inflammation.
Cite This Article
APA
von Fellenberg R, Kohler L, Grünig G, Pellegrini A.
(1985).
Comparison of neutrophil elastases and of neutrophil protease inhibitors in the horse and man.
Am J Vet Res, 46(12), 2480-2484.
Publication
Researcher Affiliations
MeSH Terms
- Animals
- Cytosol / metabolism
- Horses
- Humans
- Neutrophils / metabolism
- Pancreatic Elastase / blood
- Protease Inhibitors / blood
- Protease Inhibitors / isolation & purification
- Species Specificity
Citations
This article has been cited 6 times.- Cao JX, Dai JQ, Dai ZM, Yin GL, Yang WJ. A male reproduction-related Kazal-type peptidase inhibitor gene in the prawn, Macrobrachium rosenbergii: molecular characterization and expression patterns. Mar Biotechnol (NY) 2007 Jan-Feb;9(1):45-55.
- Skerlavaj B, Scocchi M, Gennaro R, Risso A, Zanetti M. Structural and functional analysis of horse cathelicidin peptides. Antimicrob Agents Chemother 2001 Mar;45(3):715-22.
- Gardi C, Cavarra E, Calzoni P, Marcolongo P, de Santi M, Martorana PA, Lungarella G. Neutrophil lysosomal dysfunctions in mutant C57 Bl/6J mice: interstrain variations in content of lysosomal elastase, cathepsin G and their inhibitors. Biochem J 1994 Apr 1;299 ( Pt 1)(Pt 1):237-45.
- Kordula T, Dubin A, Schooltink H, Koj A, Heinrich PC, Rose-John S. Molecular cloning and expression of an intracellular serpin: an elastase inhibitor from horse leucocytes. Biochem J 1993 Jul 1;293 ( Pt 1)(Pt 1):187-93.
- Dubin A, Potempa J, Travis J. Structural and functional characterization of elastases from horse neutrophils. Biochem J 1994 Jun 1;300 ( Pt 2)(Pt 2):401-6.
- Potempa J, Wunderlich JK, Travis J. Comparative properties of three functionally different but structurally related serpin variants from horse plasma. Biochem J 1991 Mar 1;274 ( Pt 2)(Pt 2):465-71.
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