Induction of glycosylation in human C-reactive protein under different pathological conditions
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
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| Title |
Induction of glycosylation in human C-reactive protein under different
pathological conditions
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| Creator |
Das, Tanusree
Sen, Asish Kempf, Tore Pramanik , Sumit R Mandal, Chhabinath Mandal, Chitra |
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| Subject |
Infectious Diseases and Immunology
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| Description |
As an acute-phase protein, human C-reactive protein (CRP) is
clinically important. CRPs were purified from several samples in
six different pathological conditions, where their levels ranged
from 22 to 342 µg/ml. Small, but significant, variations in
electrophoretic mobilities on native PAGE suggested differences
in molecular mass, charge and/or shape. Following separation by
SDS/PAGE, they showed single subunits with some differences
in their molecular masses ranging between 27 and 30.5 kDa, but
for a particular disease, the mobility was the same for CRPs
purified from multiple individuals or pooled sera. Isoelectric
focusing (IEF) also indicated that the purified CRPs differed
from each other. Glycosylation was demonstrated in these
purified CRPs by Digoxigenin kits, neuraminidase treatment and
binding with lectins. The presence of N-linked sugar moiety was
confirmed by N-glycosidase F digestion. The presence of sialic
acid, glucose, galactose and mannose has been demonstrated by
gas liquid chromatography, mass spectroscopic and fluorimetric
analysis. Matrix-assisted laser-desorption ionization analysis of
the tryptic digests of three CRPs showed systematic absence
of two peptide fragments, one at the N-terminus and the other
near the C-terminus. Model-building suggested that the loss of
these fragments exposed two potential glycosylation sites on a
cleft floor keeping the protein–protein interactions in pentraxins
and calcium-dependent phosphorylcholine-binding qualitatively
unaffected. Thus we have convincingly demonstrated that human
CRP is glycosylated in some pathological conditions.
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| Date |
2003
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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/557/1/BIOCHEMICAL_JOURNAL%2C373%2C345%2D355[44].pdf
Das, Tanusree and Sen, Asish and Kempf, Tore and Pramanik , Sumit R and Mandal, Chhabinath and Mandal, Chitra (2003) Induction of glycosylation in human C-reactive protein under different pathological conditions. Biochem Journal , 373. pp. 345-355. |
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| Relation |
http://dx.doi.org/10.1042/BJ20021701
http://www.eprints.iicb.res.in/557/ |
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