Fibronectin degradation products containing the cytoadhesive tetrapeptide stimulate human neutrophil degranulation

Détails

ID Serval
serval:BIB_911B9860DFC9
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Fibronectin degradation products containing the cytoadhesive tetrapeptide stimulate human neutrophil degranulation
Périodique
Journal of Clinical Investigation
Auteur(s)
Wachtfogel  Y. T., Abrams  W., Kucich  U., Weinbaum  G., Schapira  M., Colman  R. W.
ISSN
0021-9738 (Print)
Statut éditorial
Publié
Date de publication
05/1988
Volume
81
Numéro
5
Pages
1310-6
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: May
Résumé
We investigated whether adhesive glycoproteins, such as fibronectin or fibrinogen, could function to provide a nidus for neutrophil degranulation. Elastase release in recalcified plasma was normal in afibrinogenemic plasma, but 73% less in plasma depleted of fibronectin. Proteolytic digests of fibronectin, but not intact fibronectin (50-1,000 micrograms/ml), induced a concentration-dependent release of neutrophil elastase and lactoferrin. MAbs N293, which recognized the mid-molecule of fibronectin, N294, which was directed toward the 11-kD cell adhesive fragment, and N295, generated against the amino terminal of the 11-kD fragment, inhibited the release of elastase by 7, 24, and 60%, respectively. The cytoadhesive tetrapeptide portion of fibronectin, Arg-Gly-Asp-Ser (250-1,000 micrograms/ml), released 1.94 +/- 0.10 micrograms/ml of elastase from 10(7) neutrophils, in contrast to the lack of release by the control hexapeptide, Arg-Gly-Tyr-Ser-Leu-Gly. Plasmin appeared to be the enzyme responsible for fibronectin cleavage, since neutrophil elastase release in plasma that had been depleted of plasminogen was decreased and reconstitution of plasminogen-deficient plasma with purified plasminogen corrected the abnormal release. Plasmin cleaved fibronectin to multiple degradation products, each less than 200 kD. This fibronectin digest released 1.05 microgram/ml of elastase from 10(7) neutrophils. We suggest that the activation of plasminogen leads to the formation of fibronectin degradation products capable of functioning as agonists for neutrophils.
Mots-clé
Antibodies, Monoclonal Cytoplasmic Granules/metabolism Fibronectins/*metabolism/pharmacology Humans Neutrophils/*metabolism/ultrastructure Oligopeptides/*pharmacology Pancreatic Elastase/metabolism Peptide Fragments/*metabolism Plasmin/metabolism
Pubmed
Web of science
Création de la notice
25/01/2008 16:27
Dernière modification de la notice
03/03/2018 19:27
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