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Activated human PMN synthesize and release a strongly fucosylated glycoform of α 1 ‐acid glycoprotein, which is transiently deposited in human myocardial infarction
Author(s) -
Poland Dennis C. W.,
Vallejo JuanJesús García,
Niessen Hans W. M.,
Nijmeyer Remco,
Calafat Jero,
Hack C. Erik,
Van het Hof Bert,
Van Dijk Willem
Publication year - 2005
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.1004566
Subject(s) - glycoprotein , complement system , in vivo , biochemistry , inflammation , in vitro , secretion , flow cytometry , glycan , granulocyte , chemistry , biology , microbiology and biotechnology , immunology , antibody
α 1 ‐Acid glycoprotein (AGP) is a major acute‐phase protein present in human plasma as well as in polymorphonuclear leukocytes (PMN). In this report, we show that PMN synthesize a specific glycoform of AGP, which is stored in the specific and azurophilic granules. Activation of PMN results in the rapid release of soluble AGP. PMN AGP exhibits a substantially higher apparent molecular weight than plasma AGP (50–60 kD vs. 40–43 kD), owing to the presence of strongly fucosylated and sialylated polylactosamine units on its five N‐linked glycans. PMN AGP is also released in vivo from activated PMN, as appeared from studies using well‐characterized myocard slices of patients that had died within 2 weeks after an acute myocardial infarction. AGP was found deposited transiently on damaged cardiomyocytes in areas with infiltrating PMN only. It is interesting that this was inversely related to the deposition of activated complement C3. Strongly fucosylated and sialylated AGP glycoforms have the ability to bind to E‐selectin and to inhibit complement activation. We suggest that AGP glycoforms in PMN provide an endogenous feedback‐inhibitory response to excessive inflammation.