Specific cleavage of the lung surfactant protein A by human cathepsin S may impair its antibacterial properties

Article ID	Journal	Published Year	Pages	File Type
8324069	The International Journal of Biochemistry & Cell Biology	2013	9 Pages	PDF

Abstract

- Lung SP-A that participates to innate host defense is degraded in sputum of CF patients.
- Cathepsin S cleaves specifically SP-A within its carbohydrate recognition domain.
- Hydrolysis of SP-A by cathepsin S may impair its antibacterial properties.

Keywords

HNE methylmethanethiosulfonate N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-l-proline CA-074 MMTS 3-Nitro-tyrosine DPPG E-64 ABZ phorbol 12-myristate 13-acetate 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride dl-dithiothreitol AEBSF CAT AmC DTT DPPC NSP PMSF BCA 1,2-dipalmitoyl-sn-glycero-3-phosphocholine 1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol 7-amino-4-methyl coumarin PMA ortho-aminobenzoic acid Fluorescence resonance energy transfer FRET Human neutrophil elastase BALF bicinchoninic acid phenylmethylsulfonyl fluoride Cystic fibrosis broncho-alveolar lavage fluid Cathepsin