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Inflammation Research

, Volume 65, Issue 10, pp 815–825 | Cite as

PGK1, a glucose metabolism enzyme, may play an important role in rheumatoid arthritis

  • Yan Zhao
  • Xinfeng Yan
  • Xia Li
  • Yabing Zheng
  • Shufeng Li
  • Xiaotian Chang
Original Research Paper

Abstract

Background

Some studies have indicated that glucose metabolism plays an important role in the pathogenesis of rheumatoid arthritis (RA). This study aimed to find the novel genes affecting glucose metabolism in RA.

Materials/methods

Synovial tissues of collagen-induced arthritis (CIA) were analyzed with Rat Glucose Metabolism RT2 Profiler™ PCR Array to screen those genes with special expressions in glucose metabolism. Real-time PCR, western blotting, and ELISA were used to confirm the result in synovial tissues and blood of human RA. Culture synovial fibroblast cells (RASF) was treated with siRNA to suppress expressions of the target genes. CCK-8 cell proliferation assay and two-compartment transwell system were performed to examine cell proliferation and cell migration of the treated RASF.

Results

Both PCR array and real-time PCR detected the up-regulation of ENO1, HK2, and PGK1 and the down-regulation of PCK1 and PDK4 in synovial tissues of CIA rats. Real-time PCR and western blotting detected the increased expression of ENO1 and PGK1 in RA synovial tissues. ELISA detected a high level of PGK1 in the blood of RA patients. Decreased cell proliferation and cell migration capabilities were significantly detected in RASF following treatment of anti-PGK1 siRNA. IL-1β and IFN-γ rather than TNF-α and IL-1α levels were significantly declined in supernatants of the treated RASF.

Conclusions

PGK1, a glycolytic enzyme catalyzing the conversion of 3-phosphoglycerate into 2-phosphoglycerate, has increased expression in synovial tissues and blood of RA, which may be involved in pro-inflammation and synovial hyperplasia of the disease.

Keywords

Rheumatoid arthritis (RA) Collagen II-induced arthritis (CIA) Glucose metabolism Enolase 1 (ENO1) Phosphoglycerate kinase 1 (PGK1) 

Notes

Acknowledgments

This study was supported by the National Natural Science Foundation of China (NTFC) (81171990 and 81373218), and the Shandong Science and Technology Promotion Program (2014GSF118135 and 2014XGA01011).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

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Copyright information

© Springer International Publishing 2016

Authors and Affiliations

  • Yan Zhao
    • 1
  • Xinfeng Yan
    • 1
  • Xia Li
    • 2
  • Yabing Zheng
    • 1
  • Shufeng Li
    • 1
  • Xiaotian Chang
    • 1
  1. 1.Medical Research Center of Shandong Provincial Qianfoshan HospitalShandong UniversityJinanPeople’s Republic of China
  2. 2.Department of PediatricsJinan Maternity and Child Care HospitalJinanPeople’s Republic of China

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