In-vitro effects of α1-Acid Glycoprotein on Collagen Fibril Formation in Rheumatoid Arthritis

α1‐Acid glycoprotein (AGP) is an acute phase protein, the concentration of which increases during an inflammatory response. The glycosylation pattern of AGP alters during inflammatory disease and microheterogeneity studies of rheumatoid AGP have shown the molecule to be hyperfucosylated. AGP also in...

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Bibliographic Details
Published in:Pharmacy and Pharmacology Communications 1999-08, Vol.5 (8), p.507-510
Main Authors: YULE, F. S. B., WATSON, J., SMITH, K. D.
Format: Article
Language:English
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Summary:α1‐Acid glycoprotein (AGP) is an acute phase protein, the concentration of which increases during an inflammatory response. The glycosylation pattern of AGP alters during inflammatory disease and microheterogeneity studies of rheumatoid AGP have shown the molecule to be hyperfucosylated. AGP also influences collagen fibril formation. We studied the effect of rheumatoid and normal plasma AGP on type I collagen fibrillogenesis. The interaction between AGP and collagen was observed using electron microscopy and circular dichroism spectroscopy, the monosaccharide composition of AGP was determined by high pH anion‐exchange chromatography. Fibrils formed in the presence of AGP were either similar to normal collagen or contained longer spacings. For normal plasma AGP the effect was concentration‐dependent. Rheumatoid AGP completely inhibited fibril formation. The glycosylation of AGP appears to determine the type and extent of collagen fibril formation, and thus exacerbates the pathogenesis of the disease.
ISSN:1460-8081
2042-7158
DOI:10.1211/146080899128735252