Document Detail


Evidence for the tight binding of human mucus proteinase inhibitor to highly glycosylated macromolecules in sputum.
MedLine Citation:
PMID:  2775494     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Two extraction procedures of non-purulent sputum for the isolation of human mucus proteinase inhibitor (MPI) in its free and bound forms have been assayed. The dissociating procedure involved sputum homogenization in 1M NaCl and 4% (w/v) trichloroacetic treatment. When the soluble material was applied to a CM-Trisacryl column, a non-negligible, MPI-related inhibitory activity was recovered with the highly glycosylated constituents not retained on the column; the amount of MPI released in a free form was retained and eluted from the column according to the basic character of this inhibitor. The non-dissociating procedure consisted in a high water dilution (1:12) of sputum, known to bring into solution the macromolecular, fibrillar constituents, which was followed by ultrafiltration on selected Mr cut-off membranes. All the inhibitory activity was recovered with the high Mr (greater than 100,000) fraction which was shown on SDS-PAGE to be essentially composed of strongly glycosylated material; on electrophoretic analysis under non-reducing conditions, the MPI activity was visualized as three bands which corresponded to the inhibitor released from this high Mr fraction in the presence of SDS. As mucin-type molecules are the major, highly glycosylated constituents of bronchial secretions, it is suggested that they are responsible for the entrapping of MPI within their macromolecular network; it would appear that, as well as for lysozyme, electrostatic interactions occur between the acid charges of mucins and the basic charges of MPI. The possible in vivo consequences of these interactions on MPI activity are discussed.
Authors:
I Van-Seuningen; M Davril; A Hayem
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biological chemistry Hoppe-Seyler     Volume:  370     ISSN:  0177-3593     ISO Abbreviation:  Biol. Chem. Hoppe-Seyler     Publication Date:  1989 Jul 
Date Detail:
Created Date:  1989-10-23     Completed Date:  1989-10-23     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8503054     Medline TA:  Biol Chem Hoppe Seyler     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  749-55     Citation Subset:  IM    
Affiliation:
Unité INSERM No. 16, Lille, France.
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MeSH Terms
Descriptor/Qualifier:
Bronchi / secretion
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Glycoproteins / metabolism*
Humans
Molecular Weight
Mucus / analysis*
Protease Inhibitors / metabolism*
Protein Binding
Sputum / metabolism*
Ultrafiltration
Chemical
Reg. No./Substance:
0/Glycoproteins; 0/Protease Inhibitors

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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