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American Journal of Respiratory Cell and Molecular Biology. Vol. 28, pp. 485-498, 2003
© 2003 American Thoracic Society
DOI: 10.1165/rcmb.4913

Secretory Component Is Cleaved by Neutrophil Serine Proteinases but its Epithelial Production Is Increased by Neutrophils through NF-{kappa}B– and p38 Mitogen-Activated Protein Kinase–Dependent Mechanisms

Charles Pilette, Youssef Ouadrhiri, Françoise Dimanche, Jean-Pierre Vaerman and Yves Sibille

Experimental Medicine Unit, Christian de Duve Institute of Cellular Pathology, University of Louvain, Brussels, Belgium

Address correspondence to: Yves Sibille, M.D., PhD., Unité de Médecine Expérimentale, Avenue Hippocrate, 74 BP 7430, B-1200 Bruxelles, Belgique. E-mail: sibille{at}mexp.ucl.ac.be

We previously showed that expression of polymeric immunoglobulin receptor (pIgR)/secretory component (SC), the epithelial receptor assuming transport of polymeric IgA in mucosal secretions, is strongly decreased in severe chronic obstructive pulmonary disease. Here, we evaluated in vitro the effects of polymorphonuclear neutrophil (PMN) mediators on pIgR/SC. On polyacrylamide gel electrophoresis analysis, soluble SC was rapidly cleaved by supernatants from phorbol-myristate-acetate-activated PMN, through a serine proteinase activity. Moreover, purified PMN serine proteinases also cleaved SC. Similarly, polymeric IgA was rapidly cleaved in monomers by neutrophil elastase, whereas secretory immunoglobulin A was relatively resistant to neutrophil elastase. Surface pIgR on human bronchial epithelial cells was also cleaved by serine proteinases, as shown by immunofluorescence. In contrast, pIgR/SC production by cultured epithelial cells (quantified by enzyme-linked immunosorbent assay) was significantly increased by supernatants from interleukin-8/formylmethionylleucylphenylalanine-activated PMN (122.6 ± 17.3 versus 70.9 ± 9 ng/mg protein, P < 0.01). Upregulation of pIgR/SC production by bronchial epithelial cells was abolished by nuclear factor {kappa}B- and p38 mitogen-activated protein kinase (MAPK) inhibitors. Moreover, supernatants from interleukin-8/formylmethionylleucylphenylalanine-activated PMN induced the phosphorylation of I{kappa}B-{alpha} and p38 MAPK in epithelial cells, independently of serine proteinases. Thus, PMN serine proteinases cleave pIgR/SC, whereas activated PMN induce an increased pIgR/SC expression through epithelial activation of nuclear factor {kappa}B and p38 MAPK pathways.

Abbreviations: N-methoxysuccinyl-ala-ala-pro-val-chlormethylketone, APV-CMK • bovine serum albumin, BSA • cathepsin G, CathG • complete MEM, cMEM • chronic obstructive pulmonary disease, COPD • enhanced chemiluminescence, ECL • enzyme-linked immunosorbent assay, ELISA • extracellular signal-regulated kinase, ERK • fetal bovine serum, FBS • fluorescein isothiocyanate, FITC • formylmethionylleucylphenylalanine, fMLP • primary human bronchial epithelial cells, HBEC • Hanks' balanced salt solution, HBSS • N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid, HEPES • leucozyme, LZ • mitogen-activated protein kinase, MAPK • modified Eagle's medium, MEM • neutrophil elastase, NE • nuclear factor {kappa}B, NF-{kappa}B • phosphate-buffered saline, PBS • Tween 20 PBS, PBST • polymeric immunoglobulin receptor, pIgR • phorbol-myristate-acetate, PMA • polymorphonuclear neutrophil, PMN • phenyl-methyl-sulfonyl-fluoride, PMSF • proteinase 3, PR3 • secretory component, SC • secretory leukocyte proteinase inhibitor, SLPI • Soybean trypsin inhibitor, STI • tumor necrosis factor, TNF




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