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Glycobiology Advance Access originally published online on April 27, 2005
Glycobiology 2005 15(9):838-848; doi:10.1093/glycob/cwi067
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response

Manasi M. Chavan1,2, Poonam D. Kawle and Narendra G. Mehta

Biochemistry and Cell Biology, ACTREC, Navi Mumbai 410 208, India

1 To whom correspondence should be addressed; e-mail: mchavan{at}notes.cc.sunysb.edu

2 Present address: Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794

Received on January 21, 2005; revised on April 19, 2005; accepted on April 20, 2005

Within hours of turpentine injection to stimulate the acute phase (AP) response in rats, the N-acetylneuraminic acid content of plasma proteins increases and that of fucose decreases, each by about 60%. The two changes are inversely related (r 5 20.97). The NeuAc/Gal ratio increases from the normal 0.75 to 1.0 on day 2 of the AP. Whereas 50% of the isolated oligosaccharides of normal plasma proteins are retarded on immobilized Ricinus communis agglutinin, those from day 2 AP plasma fail to do so. This indicates that NeuAc caps the normally Gal-terminated chains. a1-Acid glycoprotein (a positive AP protein), a1-macroglobulin (a non-AP protein), and a1-inhibitor3 (a negative AP protein) also show similar alterations in NeuAc/Gal ratio and decreases in Fuc. a2-Macroglobulin, which arises only during the AP, does not contain significant amounts of Fuc. Sambucus nigra agglutinin (a2,6-linked NeuAc-specific) binds a majority of plasma proteins, and binding is increased during the AP response. Maackia amurensis lectin (a2,3-linked NeuAc-specific) binds only three proteins in normal plasma and three additional proteins in AP plasma. The Fuc-specific Aleuria aurantia agglutinin and Lens culinaris agglutinin each detect five proteins in normal plasma. Their binding decreases during the AP response. These results show that: (1) sialylation and defucosylation of preexisting plasma proteins occur rapidly in the AP response; (2) sialylation caps the preexisting Gal-terminating oligosaccharides; and (3) the oligosaccharides of even the non-AP and negative AP proteins are modified. These changes are distinct from the elevation in the levels of protein-bound monosaccharides and the altered concanavalin A-binding profile the oligosaccharides of AP proteins acquire in diseases.

Key words: acute phase / glycosylation / plasma proteins


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