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. 2014 Oct 9;9(10):e109238.
doi: 10.1371/journal.pone.0109238. eCollection 2014.

Obesity associated molecular forms of C-reactive protein in human

Affiliations

Obesity associated molecular forms of C-reactive protein in human

Bela F Asztalos et al. PLoS One. .

Abstract

Objective: To describe novel C-reactive protein (CRP) molecular forms (mf) in human plasma.

Design and methods: Five novel CRP-mfs, disctinct from the previously described native (nCRP) and modified (mCRP) C-reactive proteins, were separated from human plasma by polyacrylamide gel electrophoresis and immunodetected by western blot in subjects with or without increased BMI, cardiovascular disease (CVD), and diabetes (n = 1800).

Results: Three of the five CRP-mfs were present in all samples. One, CRPmf-4, was present in a subgroup of subjects and its presence was associated with elevated body mass index (BMI). CRP-mf-5 was present in about 2% of the subjects and was not associated with any other parameters. The presence or distribution of the 5 CRP-mfs were not Ca2+-dependent. Crossed immuno-localization experiments indicated that none of the CRP-mfs were complexed with any of the lipoprotein classes or with signature proteins of the complement-factor. Moreover, the distribution of CRP-mfs were not significantly correlated with plasma CRP levels. CRP-mf-4 was significantly associated with increased BMI, but not with other parameters of the metabolic syndrome (HDL-C and triglyceride levels, and diabetes).

Conclusions: We have identified five new CRP-mfs out of which CRP-mf-4 was significantly associated with obesity. We have shown that oligomerization of CRP was not calcium dependent. We hypothesize that adipose tissue produces a factor which influences the formation of CRP mf-4. CRP-mfs might be used as an obesity-associated inflammatory marker.

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Conflict of interest statement

Competing Interests: The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. CRP-mfs were separated on 3–16% linear gradient PAG.
Electrophoreses were carried out under non-denaturing conditions. Gels were electrotransfered to nitrocellulose membrane followed by imuno-probing membranes with a polyclonal antibody specific to human CRP. Subjects' total plasma CRP values varied between less than 2 µg/mL (columns 4, 6, 7 in panel-a, and columns 4 and 7 in panel-b) and about 20 µg/mL (column 2 in panel-a, and column 1 panel-b). Column 1 in panel a shows the native or pentamer (nCRP) and the modified or monomer (mCRP) as well as the human serum albumin. It is worth noting that under non-denaturing conditions proteins are separated by their mass/charge ratio not by size.

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