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Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
Linköping University, Faculty of Health Sciences. Linköping University, Department of Molecular and Clinical Medicine, Infectious Diseases. Östergötlands Läns Landsting, Centre for Medicine, Department of Infectious Diseases in Östergötland.
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2001 (English)In: Blood, ISSN 0006-4971, Vol. 97, no 12, 3951-3959 p.Article in journal (Refereed) Published
Abstract [en]

Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. The known biologic functions reside in the C-terminus, which must be cleaved from the holoprotein to become active. Bovine and porcine cathelicidins are cleaved by elastase from the azurophil granules to yield the active antimicrobial peptides. The aim of this study was to identify the physiological setting for cleavage of the only human cathelicidin, hCAP-18, to liberate the antibacterial and cytotoxic peptide LL-37 and to identify the protease responsible for this cleavage. Immunoelectron microscopy demonstrated that both hCAP-18 and azurophil granule proteins were present in the phagolysosome. Immunoblotting revealed no detectable cleavage of hCAP-18 in cells after phagocytosis. In contrast, hCAP-18 was cleaved to generate LL-37 in exocytosed material. Of the 3 known serine proteases from azurophil granules, proteinase 3 was solely responsible for cleavage of hCAP-18 after exocytosis. This is the first detailed study describing the generation of a human antimicrobial peptide from a promicrobicidal protein, and it demonstrates that the generation of active antimicrobial peptides from common proproteins occurs differently in related species.

Place, publisher, year, edition, pages
2001. Vol. 97, no 12, 3951-3959 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-25908DOI: 10.1182/blood.V97.12.3951Local ID: 10350OAI: diva2:246456
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2011-01-13

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Follin, Per
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Faculty of Health SciencesInfectious DiseasesDepartment of Infectious Diseases in Östergötland
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