Hostname: page-component-745bb68f8f-grxwn Total loading time: 0 Render date: 2025-02-06T07:47:09.910Z Has data issue: false hasContentIssue false
  • English
  • Français

Equine neutrophil elastase 2A concentrations in tracheal wash preparations and synovial fluid as a potential objective marker for inflammatory airway and joint diseases in horses

Published online by Cambridge University Press:  27 February 2018

M P Dagleish
M P Dagleish*
Affiliation:
Moredun Research Institute, Pentlands Science Park, Bush Loan, Penicuik, Near Edinburgh EH26 0PZ, UK, Email: [email protected]
Get access

Extract

Neutrophil elastase (NE), a powerful proteolytic enzyme found within the primary cytoplasmic granules of polymorphonuclear leukocytes (PMN), is capable of degrading almost any component of the extracellular pulmonary matrix and forms part of the cells’ armoury against invading microbes (Crystal, 1996; Haslett, Savill and Meagher, 1989). It is essential during inflammation for diapedesis and migration to extravascular compartments (Henson and Johnson, 1987), oxygen independent bactericidal activity and the remodelling of damaged tissues (Ganz, Metcalf, Gallin and Lehrer, 1987) and is crucial for health as an absence results in increased susceptibility to pyogenic infections which, if untreated, are eventually fatal. Mature PMN contain a finite amount of NE (Campbell, Silverman and Campbell, 1989) which can only be synthesized during development within the bone marrow, especially the pro–myelocyte stage (Fouret, duBois, Bernaudin, Takahashi, Ferrans and Crystal, 1989).

PMN are often the first white blood cells to be attracted to an inflamed and/or infected area within the body and can persist there due to their role in remodelling damaged tissue.

Type
Research Article
Information
BSAP Occasional Publication , Volume 32: Emerging Equine Science , 2004 , pp. 79 - 82
Copyright
Copyright © British Society of Animal Production 2004

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Campbell, E.J., Silverman, E.K. and Campbell, M.A. (1989). Elastase and cathepsin–g of human–monocytes – quantification of cellular content, release in response to stimuli, and heterogeneity in elastase–mediated proteolytic activity. Journal of Immunology 143: 2961–2968.CrossRefGoogle ScholarPubMed
Crystal, R.G. (1996). Alpha 1–Antitrypsin Deficiency, Marcel Dekker, Inc. New York, Basel, Hong Kong.Google Scholar
Dagleish, M. P., Pemberton, A. D., Brazil, T. J., MCAleese, S. M., Miller, H. R. P. and Scudamore, C. L. (1999). Kinetics of Equine Neutrophil Elastase Release and Superoxide Anion Generation Following Secretagogue Activation: A Potential Mechanism for Antiproteinase Inactivation. Veterinary Immunology and Immunopathology 72: 257–275.Google Scholar
Dixon, P.M., Railton, D.I. and Mcgorum, B.C. (1995). Equine pulmonary disease: a case controlled study of 300 referred cases. Part 3: Ancillary diagnostic findings. Equine Veterinary Journal 27: 428–435.Google Scholar
Fouret, P., duBois, R.M., Bernaudin, J.F., Takahashi, H., Ferrans, V.J. and Crystal, R.G. (1989). Expression of the neutrophil elastase gene during human–bone marrow cell–differentiation. Journal of Experimental Medicine 169: 833–845.Google Scholar
Ganz, T., Metcalf, J.A., Gallin, J.I. and Lehrer, R.I. (1987). 2 geneticdisorders that affect human–neutrophils (pmn) are associated with deficiencies of microbicidal and cyto–toxic granule proteins. Clinical Research 35: A 424.Google Scholar
Haslett, C., Savill, J.S. and Meagher, L. (1989). The neutrophil. Current Opinion In Immunology 2: 10–18.Google Scholar
Henson, P.M. and Johnston, R.B. (1987). Tissue–injury in inflammation – oxidants, proteinases, and cationic proteins. Journal of Clinical Investigation 79: 669–674.Google Scholar
Tremaine, H. (2000). Infection of equine joints and tendon sheaths. In Practice 22: 262–273.CrossRefGoogle Scholar