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166 GLYCOSYLATED C-REACTIVE PROTEIN STIMULATES PROINFLAMMATORY MEDIATOR EXPRESSION IN RAT AORTIC SMOOTH MUSCLE CELLS.
  1. W. Feng,
  2. D. Xing,
  3. S. Oparil,
  4. Y. F. Chen,
  5. A. J. Szalai
  1. University of Alabama at Birmingham, Birmingham, AL; Chitra Mandal, Indian Institute of Chemical Biology, Kolkata, India

Abstract

Background It has been reported that human C-reactive protein (CRP) can be glycosylated in different pathological conditions (eg, lupus, leukemia, tuberculosis) and thereby exhibit variable binding characteristics. This study tested the hypothesis that nonglycosylated CRP (non-g-CRP) and glycosylated CRP (g-CRP) differ in their ability to induce proinflammatory mediator expression by rat aortic smooth muscle cells (RASMCs).

Methods Quiescent RASMCs were treated for 6 hrs with non-g-CRP versus g-CRP (0.5 to 5 μg/mL) separately purified to apparent homogeneity from 6 different patients, and then harvested for RNA extraction. Real time RT-PCR was performed to assess mRNA expression of chemokines (cytokine-induced neutrophil chemoattractant [CINC]-2 and monocyte chemoattractant protein [MCP]-1), interleukin (IL)-6 and adhesion molecules (intercellular adhesion molecule [ICAM]-1 and vascular cell adhesion molecule [VCAM]-1). Data (mRNA to 18S RNA ratios) were normalized to the mean mRNA levels of vehicle-treated RASMCs.

Results g-CRP dose dependently stimulated expression of CINC-2, MCP-1, IL-6, ICAM-1, and VCAM-1 in RASMCs (Table). Surprisingly, non-g-CRP had no effect on expression of the same proinflammatory mediators.

Conclusion g-CRP elicits more robust proinflammatory molecule mRNA production from RASMCs than non-g-CRP, in a pattern consistent with modulation of the vascular injury response. This finding may help further define the clinical utility of CRP in the context of heart and blood vessel disease.

Table

Glycosylated CRP Stimulates Proinflammatory Mediator mRNA Expression in RASMCs

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