Variations in binding characteristics of glycosylated human C-reactive proteins in different pathological conditions
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
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Title |
Variations in binding characteristics of glycosylated
human C-reactive proteins in different pathological
conditions
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Creator |
Das, Tanusree
Mandal, Chhabinath Mandal, Chitra |
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Subject |
Drug Development/Diagnostics & Biotechnology
Infectious Diseases and Immunology |
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Description |
C-reactive protein (CRP) is a clinically important classic acute phase pentameric protein. It is thought to play an important
role in immunomodulation. Earlier reports convincingly demonstrated that human CRP is differentially glycosylated in
different pathological conditions. Although CRP is considered to be a clinically important molecule, changes in binding
characteristics with appropriate ligands with respect to glycosylation remain unexplored. In an effort to demonstrate that
these glycosylated molecular variants are capable of modulating their binding activity with different ligands, CRPs were
affinity purified from six different clinical samples. Variable amounts of linkage-specific sialic acid derivatives were found
in these CRPs with varying tryptophan contents. Differential binding patterns with antibodies against human CRP, human
IgG, and other ligands like fibronectin, fetuin, and asialofetuin indicated that the purified CRPs differed significantly in their
lectin-like interactions. Thus, we have convincingly demonstrated that differentially induced CRPs exhibited variable binding
characteristics. These results may have far reaching practical applications for understanding acute phase responses.
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Date |
2004
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Identifier |
http://www.eprints.iicb.res.in/566/1/GLYCOCONJUGATE_JOURNAL%2C_20_(_9)%2C__537%2D543[93].pdf
Das, Tanusree and Mandal, Chhabinath and Mandal, Chitra (2004) Variations in binding characteristics of glycosylated human C-reactive proteins in different pathological conditions. Glycoconjugate Journal , 20 (9). pp. 537-543. |
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Relation |
http://dx.doi.org/10.1023/B:GLYC.0000043290.90182.e6
http://www.eprints.iicb.res.in/566/ |
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