onr:"swepub:oai:lup.lub.lu.se:53eb3a0d-a2ef-4e12-b48b-51f468800383"
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- Bergenfeldt, M.Lund University,Lunds universitet,Kirurgi, Lund,Sektion V,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Surgery (Lund),Section V,Department of Clinical Sciences, Lund,Faculty of Medicine,Skåne University Hospital (author)
Release of neutrophil proteinase 4(3) and leukocyte elastase during phagocytosis and their interaction with proteinase inhibitors
- Article/chapterEnglish1992
Publisher, publication year, extent ...
- 2009-07-08
- Informa UK Limited,1992
- 7 s.
Numbers
- LIBRIS-ID:oai:lup.lub.lu.se:53eb3a0d-a2ef-4e12-b48b-51f468800383
- https://lup.lub.lu.se/record/53eb3a0d-a2ef-4e12-b48b-51f468800383URI
- https://doi.org/10.3109/00365519209088387DOI
Supplementary language notes
- Language:English
- Summary in:English
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- SwePubSwePub
Classification
Notes
- Neutrophil proteinase 4 (NP4) is a major neutral proteinase of the human polymorphonuclear (PMN) leukocyte, which is present in amounts similar to leukocyte elastase. NP4(3) is a potent, non-specific proteinase, which may degrade structural and soluble proteins in the tissues and body fluids, and it has been implicated as an important pathogenetic factor in lung emphysema. We have studied the release of elastase and NP4(3) in an in vitro model of phagocytosis, α1-pproteinase inhibitor (α1-PI) is the major plasma inhibitor of both leukocyte elastase and NP4(3), but α1-PI bound leukocyte elastase more readily than NP4(3). The basic conditions were designed so that some proteolytic activity was present in the medium. Addition of increasing amounts of Secretory leukocyte protease inhibitor (SLPI) to the incubation mixtures resulted in binding of leukocyte elastase to this inhibitor and extinction of free proteolytic activity against both natural and synthetic substrates. The progressive binding of leukocyte elastase to SLPI instead of α1-PI was paralleled by an increasing binding of NP4(3) to α1-PI. SLPI is a potent inhibitor of leukocyte elastase and cathepsin G, and although it lacks inhibitory effect on NP4(3), it may obviously indirectly aid in the binding and inhibition of NP4(3) to α1-PI, by taking care of at least part of the leukocyte elastase. As a specific NP4(3)-inhibitor is not readily available for therapeutic use, this effect may prove useful under in vivo conditions and enhance the protective effect of administered recombinant human SLPI.
Subject headings and genre
- MEDICIN OCH HÄLSOVETENSKAP Medicinska och farmaceutiska grundvetenskaper Läkemedelskemi hsv//swe
- MEDICAL AND HEALTH SCIENCES Basic Medicine Medicinal Chemistry hsv//eng
- Leukocyte elastase
- Neutrophil proteinase 4
- Phagocytosis
- Proteinase-3
- Secretory leukocyte protease inhibitor
Added entries (persons, corporate bodies, meetings, titles ...)
- Axelsson, L.Lund University,Lunds universitet,Experimentell patologi, Malmö,Forskargrupper vid Lunds universitet,Experimental Pathology, Malmö,Lund University Research Groups,Skåne University Hospital(Swepub:lu)expp-lax (author)
- Ohlsson, K. (author)
- Kirurgi, LundSektion V (creator_code:org_t)
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- In:Scandinavian Journal of Clinical and Laboratory Investigation: Informa UK Limited52:8, s. 823-8290036-55131502-7686
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