Identification and characterization of equine granzyme B.
Abstract: In the present study we describe the isolation and characterization of putative equine granzyme B for which we propose the designation 'eqGrzmB'. Sequence analysis revealed characteristic features of a GrzmB protease such as the presence of a signal (leader-) peptide and an activation di-peptide. The isolated eqGrzmB is functionally active when expressed in human or in insect cells. Furthermore, exchange of any of three putative active site amino acids, which are highly conserved along granzyme B enzymes, led to a complete loss of enzymatic activity in the newly identified eqGrzmB. Phylogenetic analysis places eqGrzmB in the chymase-locus within the large family of granzymes in close proximity to putative equine mast cell protease and to granzyme B from mouse, rat, and human. eqGrzmB proteolytic activity has been kinetically characterized and can be specifically inhibited by granzyme B inhibitors. Taken together, we conclude that we have isolated a new member of the granzyme B family, the first granzyme identified in Equidae. The description of equine granzyme B might facilitate the development of immunological assays for the activity of equine lymphocytes.
Publication Date: 2007-06-03 PubMed ID: 17604123DOI: 10.1016/j.vetimm.2007.05.002Google Scholar: Lookup
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- Journal Article
Summary
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This research describes the identification and characterization of an enzyme (equine granzyme B) in horses. The research shows that this enzyme, which shares similar features to related enzymes in other species, plays a role in immune response and could be a key to developing new diagnostics or treatments for immune-related conditions in horses.
Study Objective and Methodology
- The primary objective of this study was to identify and describe the characteristics of an enzyme called equine granzyme B (eqGrzmB) in horses.
- The researchers used sequence analysis to highlight key features of this enzyme. This includes the presence of a signal (leader-) peptide and an activation di-peptide.
- The enzyme was tested for activity by expressing it in human and insect cells. To evaluate the importance of the enzyme’s active site amino acids, the researchers altered these and observed any changes in enzymatic activity.
Key Findings
- The isolated eqGrzmB was found to be functionally active when expressed in human or insect cells.
- However, when any of three active site amino acids were exchanged, it led to a complete loss of the enzyme’s activity. This confirms the significance of these amino acids in eqGrzmB function.
- A phylogenetic analysis positioned eqGrzmB within the large family of granzymes, close to the equine mast cell protease and granzyme B from mouse, rat, and human. This suggests a shared evolutionary history and similar function.
- The eqGrzmB enzyme’s proteolytic activity was kinetically characterized, and it was found that it could be specifically inhibited by granzyme B inhibitors.
Implications and Conclusion
- The identification and characterization of eqGrzmB represent the first granzyme discovered in the Equidae family (which includes horses, donkeys, and zebras).
- This could have potential implications for the development of immunological assays for equine lymphocyte activity, which could help in diagnosing and treating immune-related conditions in horses.
- Overall, the researchers concluded that they had isolated a new member of the granzyme B family (eqGrzmB), which opens up further avenues for research in equine immunology.
Cite This Article
APA
Piuko K, Bravo IG, Müller M.
(2007).
Identification and characterization of equine granzyme B.
Vet Immunol Immunopathol, 118(3-4), 239-251.
https://doi.org/10.1016/j.vetimm.2007.05.002 Publication
Researcher Affiliations
- Deutsches Krebsforschungszentrum, Forschungsschwerpunkt Angewandte Tumorvirologie, F035, Im Neuenheimer Feld 242, 69120 Heidelberg, Germany.
MeSH Terms
- Amino Acid Sequence
- Animals
- Cell Line
- Cloning, Molecular
- DNA, Complementary / genetics
- Gene Expression Regulation, Enzymologic
- Granzymes / antagonists & inhibitors
- Granzymes / chemistry
- Granzymes / genetics
- Granzymes / metabolism
- Horses / genetics
- Humans
- Molecular Sequence Data
- Mutation
- Phylogeny
- Substrate Specificity
Citations
This article has been cited 2 times.- Yang J, Pemberton A, Morrison WI, Connelley T. Granzyme B Is an Essential Mediator in CD8(+) T Cell Killing of Theileria parva-Infected Cells. Infect Immun 2019 Jan;87(1).
- Tachibana Y, Nakano Y, Nagaoka K, Kikuchi M, Nambo Y, Haneda S, Matsui M, Miyake Y, Imakawa K. Expression of endometrial immune-related genes possibly functioning during early pregnancy in the mare. J Reprod Dev 2013;59(1):85-91.
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