| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Published online before print August 17, 2004
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
,1
* Division of Infectious Diseases and
Department of Pediatrics, University of California San Diego; and
Research Unit Med Klinik B, Department of Medicine,University of Zürich, Switzerland
1 Correspondence: Medizinische Klinik B, Universitätsspital AW 9, Rämistrasse 100, CH-8091 Zürich, Switzerland. E-mail.klinsar{at}usz.unizh.ch
The antimicrobial activity of a number of chemokines has recently come into focus of research about innate immunity. We have previously shown that platelet basic protein (PBP), which gives rise to several antimicrobial peptides of platelets, is also expressed in human monocytes. In the present studies, we show that exposure of human monocytes to bacteria or microbial components (lipopolysaccharide and zymosan) induces a several-fold greater expression of derivates of PBP. Also, activation of proteinase-activated receptors (PARs) by thrombin or the synthetic peptide ligand SFLLRN of PAR-1 significantly increased PBP expression, presumably on the transcriptional level, as evidenced by higher mRNA levels. Derivates of PBP appeared to reach phago-lysosomes, as higher concentration was found in latex phagosomes isolated by a flotation method. By the gel-overlay technique, two bactericidal derivatives of PBP could be visualized, which were immunoreactive with anti-PBP antibody in Western blots. By matrix-assisted laser desorption/ionization time of flight and surface-enhanced laser desorption and ionization techniques, it was confirmed that the bands corresponded to PBP derivates. After immunofixation with a monoclonal antibody to PBP, the major peptide in zymosan-stimulated monocytes was identified to correspond by molecular weight to connective tissue-activating peptide III, which has been reported to be a major antimicrobial PBP derivate also in platelets. Our observations indicate that PBP and its derivates are constituents of the antimicrobial arsenal of human monocytes. Their increased expression after exposure to microorganisms allows a rapid host response to pathogens.
Key Words: macrophages • antimicrobial cationic peptides • ß-thromboglobulin • chemokines • receptors • proteinase-activated
This article has been cited by other articles:
|
|
 |
|
  N. Lippuner, B. Morell, A. Schaffner, and D. J. Schaer Proteinase-activated receptors induce nonoxidative, antimicrobial peptides and increased antimicrobial activity in human mononuclear phagocytes J. Leukoc. Biol., February 1, 2007; 81(2): 465 - 473. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. M. Pillai, M. Iwata, N. Awaya, L. Graf, and B. Torok-Storb Monocyte-derived CXCL7 peptides in the marrow microenvironment Blood, May 1, 2006; 107(9): 3520 - 3526. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. J. Schaer, C. A. Schaer, P. W. Buehler, R. A. Boykins, G. Schoedon, A. I. Alayash, and A. Schaffner CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin Blood, January 1, 2006; 107(1): 373 - 380. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Schaffner, P. Rhyn, G. Schoedon, and D. J. Schaer Regulated expression of platelet factor 4 in human monocytes--role of PARs as a quantitatively important monocyte activation pathway J. Leukoc. Biol., July 1, 2005; 78(1): 202 - 209. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
