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Blood, 15 June 2001, Vol. 97, No. 12, pp. 3951-3959
PHAGOCYTES
Human cathelicidin, hCAP-18, is processed to the antimicrobial
peptide LL-37 by extracellular cleavage with
proteinase 3
Ole E. Sørensen,
Per Follin,
Anders H. Johnsen,
Jero Calafat,
G. Sandra Tjabringa,
Pieter S. Hiemstra, and
Niels Borregaard
From the Granulocyte Research Laboratory, Departments
of Hematology and Clinical Biochemistry, Copenhagen University
Hospital, Denmark; the Department of Infectious Diseases,
Linköping University, Sweden; the Division of Cell Biology,
Netherlands Cancer Institute, Amsterdam, The Netherlands; and the
Department of Pulmonology, Leiden University Medical Center, Leiden,
The Netherlands.
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.

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M. G. Scott, D. J. Davidson, M. R. Gold, D. Bowdish, and R. E. W. Hancock
The Human Antimicrobial Peptide LL-37 Is a Multifunctional Modulator of Innate Immune Responses
J. Immunol.,
October 1, 2002;
169(7):
3883 - 3891.
[Abstract]
[Full Text]
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L. Udby, J. Calafat, O. E. Sorensen, N. Borregaard, and L. Kjeldsen
Identification of human cysteine-rich secretory protein 3 (CRISP-3) as a matrix protein in a subset of peroxidase-negative granules of neutrophils and in the granules of eosinophils
J. Leukoc. Biol.,
September 1, 2002;
72(3):
462 - 469.
[Abstract]
[Full Text]
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S. H. Hall, K. G. Hamil, and F. S. French
Host Defense Proteins of the Male Reproductive Tract
J Androl,
September 1, 2002;
23(5):
585 - 597.
[Full Text]
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E. Bulow, N. Bengtsson, J. Calafat, U. Gullberg, and I. Olsson
Sorting of neutrophil-specific granule protein human cathelicidin, hCAP-18, when constitutively expressed in myeloid cells
J. Leukoc. Biol.,
July 1, 2002;
72(1):
147 - 153.
[Abstract]
[Full Text]
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K. Lollike, M. Lindau, J. Calafat, and N. Borregaard
Compound exocytosis of granules in human neutrophils
J. Leukoc. Biol.,
June 1, 2002;
71(6):
973 - 980.
[Abstract]
[Full Text]
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M. V. Sawai, A. J. Waring, W. R. Kearney, P. B. McCray Jr, W. R. Forsyth, R. I. Lehrer, and B. F. Tack
Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides
Protein Eng. Des. Sel.,
March 1, 2002;
15(3):
225 - 232.
[Abstract]
[Full Text]
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N. Degousee, F. Ghomashchi, E. Stefanski, A. Singer, B. P. Smart, N. Borregaard, R. Reithmeier, T. F. Lindsay, C. Lichtenberger, W. Reinisch, et al.
Groups IV, V, and X Phospholipases A2s in Human Neutrophils. ROLE IN EICOSANOID PRODUCTION AND GRAM-NEGATIVE BACTERIAL PHOSPHOLIPID HYDROLYSIS
J. Biol. Chem.,
February 8, 2002;
277(7):
5061 - 5073.
[Abstract]
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K. Hase, L. Eckmann, J. D. Leopard, N. Varki, and M. F. Kagnoff
Cell Differentiation Is a Key Determinant of Cathelicidin LL-37/Human Cationic Antimicrobial Protein 18 Expression by Human Colon Epithelium
Infect. Immun.,
February 1, 2002;
70(2):
953 - 063.
[Abstract]
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