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Modulation of human neutrophil function by fibronectin degradation products isolated from cryoglobulins

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Abstract

The proteolytic fragments of native fibronectin (cryopeptides) complexed to pathological immunoglobulins in cryoglobulins were isolated from the serum of six different patients. Two peptides of 117,000 daltons and 70,000 daltons were purified and characterized byN-termmal amino acid sequencing. The priming effect of the mixture of these two peptides, referred to as cryopeptides, on neutrophil functions, namely the respiratory burst, exocytosis, and Ca2+ release, was investigated. Cryopeptides and cryoglobulins assayed separately did not increase neutrophil respiration or cytosol free calcium concentration; however, both of them induced granule enzyme secretion. Sequential exposure of neutrophils to either cryopeptides or the respective cryoglobulins, and then toN-formyl-methionyl-leucyl-phenylalanine or serum opsonized zymosan, resulted in a synergistic stimulation of O2 uptake compared to the effect ofN-formyl-peptides or opsonized zymosan tested separately; Ca2+ release was significantly enhanced by the pretreatment of neutrophils with cryopeptides. These data suggest that cryopeptides and cryoglobulins may play a role in host defense against bacterial infections through neutrophil activation.

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Author notes

  1. D. Anthony

    Present address: Department of Biochemistry, University of London King's College, Strand, WC2R 2LS, London, UK

Authors and Affiliations

  1. Laboratoire d'Enzymologie, France

    F. Morel, L. Cohen Tanugi Cholley & D. Anthony

  2. Laboratoire de Biochimie A, France

    J. C. Renversez & C. Revol

  3. Laboratoire de Biochimie, CEN, 85 X, 38041, Grenoble Cédex, France

    A. C. Dianoux, F. Boulay & P. V. Vignais

  4. Laboratoire de Biologie structurale Départment de Biologie moléculaire et structurale, CEN, 85 X, 38041, Grenoble Cédex, France

    J. Gagnon

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  1. F. Morel
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Morel, F., Cohen Tanugi Cholley, L., Dianoux, A.C. et al. Modulation of human neutrophil function by fibronectin degradation products isolated from cryoglobulins. Inflammation 16, 325–341 (1992). https://doi.org/10.1007/BF00917625

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