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Glycobiology Advance Access published online on April 27, 2005
Glycobiology, 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
Received January 21, 2005
Revised April 19, 2005
Accepted April 20, 2005

Article

Increased Sialylation and Defucosylation of Plasma Proteins are Early Events in the Acute Phase Response

Manasi M. Chavan 1*, Poonam D. Kawle 2, and Narendra G. Mehta 2

1 Biochemistry and Cell Biology, ACTREC, Navi Mumbai 410 208, India; Present address: Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794
2 Biochemistry and Cell Biology, ACTREC, Navi Mumbai 410 208, India

* To whom correspondence should be addressed.
Manasi M. Chavan, E-mail: mchavan{at}notes.cc.sunysb.edu


  Abstract

Within hours of turpentine injection to stimulate the acute phase (AP) response in rats, the N-acetylneuraminic acid (NeuAc) content of plasma proteins (PP) increases and that of fucose (Fuc) decreases, each by about 60%. The two changes are inversely related (r = -0.97). The NeuAc/galactose (Gal) ratio increases from the normal 0.75 to 1.0 on day 2 AP. While 50% of the isolated oligosaccharides of normal plasma (NP) 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-terminating chains. {alpha}1-Acid glycoprotein (a positive-AP protein), {alpha}1-macroglobulin (a non-AP protein) and {alpha}1-inhibitor3 (a negative-AP protein) also show similar alterations in NeuAc/Gal ratio and decrease in Fuc. {alpha}2-Macroglobulin, which arises only during the AP, does not contain significant amounts of fucose (data not shown). Sambucus nigra agglutinin ({alpha}2,6-linked NeuAc-specific) binds majority of PP, which is increased during the AP. Maackia amurensis lectin ({alpha}2,3-linked NeuAc-specific) binds only 3 proteins in NP, and three additional proteins in AP. The fucose-specific Aleuria aurantia agglutinin and Lens culinaris agglutinin each detects five proteins in NP. The binding decreases during the AP. These results show that (i) sialylation and defucosylation of preexisting PP occur rapidly in the AP; (ii) sialylation caps the pre-existing Gal-terminating oligosaccharides; and (iii) the oligosaccharides of even the non- and negative-AP proteins are modified. These changes are distinct from the elevation in the levels of protein-bound monosaccharides and the altered Con A-binding profile the oligosaccharides of AP proteins acquire in diseases.

Keywords: acute phase, glycosylation, plasma proteins.
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