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Published online before print January 12, 2005

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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.1004566

Received for publication October 6, 2004.

Accepted for publication December 9, 2004.

Article

Activated human PMN synthesize and release a strongly fucosylated glycoform of ₁-acid glycoprotein, which is transiently deposited in human myocardial infarction

Dennis C. W. Poland ^*, Juan-Jesús García Vallejo ^*, Hans W. M. Niessen , Remco Nijmeyer , Jero Calafat ^¶, C. Erik Hack ^||, Bert Van het Hof ^*, and Willem Van Dijk ^*@

Departments of *Molecular Cell Biology & Immunology, Glycoimmunology Group, Pathology, and Clinical Chemistry, and Institute for Cardiovascular Research, VU University Medical Centre, Amsterdam, the Netherlands; ^¶Division of Cell Biology, the Netherlands Cancer Institute, Amsterdam; and ^||Department of Immunopathology, Sanquin Research at CLB and Laboratory for Experimental and Clinical Immunology, Academic Medical Center, University of Amsterdam, the Netherlands

^@ To whom correspondence should be addressed. E-mail: w.vandijk{at}vumc.nl.

	Abstract

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.

Key Words: activated complement C3 • molecular weight • orosomucoid • subcellular localization • secretion • specific granules • azurophilic granules

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