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Journal of Molecular Neuroscience

, Volume 51, Issue 3, pp 734–748 | Cite as

Abnormally Upregulated αB-crystallin Was Highly Coincidental with the Astrogliosis in the Brains of Scrapie-Infected Hamsters and Human Patients with Prion Diseases

  • Ke Wang
  • Jin Zhang
  • Yin Xu
  • Ke Ren
  • Wu-Ling Xie
  • Yu-E Yan
  • Bao-Yun Zhang
  • Qi Shi
  • Yong LiuEmail author
  • Xiao-Ping DongEmail author
Article

Abstract

αB-crystallin is a member of the small heat shock protein family constitutively presenting in brains at a relatively low level. To address the alteration of αB-crystallin in prion disease, the αB-crystallin levels in the brains of scrapie agent 263 K-infected hamsters were analyzed. The levels of αB-crystallin were remarkably increased in the brains of 263 K-infected hamsters, showing a time-dependent manner along with incubation time. Immunohistochemical (IHC) and immunofluorescent (IFA) assays illustrated more αB-crystallin-positive signals in the regions of the cortex and thalamus containing severe astrogliosis. Double-stained IFA verified that the αB-crystallin signals colocalized with the enlarged glial fibrillary acidic protein-positive astrocytes, but not with neuronal nuclei-positive cells. IHC and IFA of the serial brain sections of infected hamsters showed no colocalization and correlation between PrPSc deposits and αB-crystallin increase. Moreover, increased αB-crystallin deposits were observed in the brain sections of parietal lobe of a sporadic Creutzfeldt–Jakob disease (sCJD) case, parietal lobe and thalamus of a G114V genetic CJD case, and thalamus of a fatal family insomnia (FFI) case, but not in a parietal lobe of FFI where only very mild astrogliosis was addressed. Additionally, the molecular interaction between αB-crystallin and PrP was only observed in the reactions of recombinant proteins purified from Escherichia coli, but not either in that of brain homogenates or in that of the cultured cell lysates expressing human PrP and αB-crystallin. Our data indicate that brain αB-crystallin is abnormally upregulated in various prion diseases, which is coincidental with astrogliosis. Direct interaction between αB-crystallin and PrP seems not to be essential during the pathogenesis of prion infection.

Keywords

αB-crystallin PrP GFAP Astrogliosis Prion disease 

Notes

Acknowledgments

This work was supported by the Chinese National Natural Science Foundation Grant (81100980, 81101302, and 31100117), the China Mega-Project for Infectious Disease (2011ZX10004-101 and 2012ZX10004215), and the SKLID Development Grant (2012SKLID102, 2011SKLID302, 2011SKLID204, and 2011SKLID211).

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Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  • Ke Wang
    • 1
    • 2
  • Jin Zhang
    • 2
    • 3
  • Yin Xu
    • 2
  • Ke Ren
    • 2
  • Wu-Ling Xie
    • 1
    • 2
  • Yu-E Yan
    • 2
  • Bao-Yun Zhang
    • 2
  • Qi Shi
    • 2
  • Yong Liu
    • 1
    Email author
  • Xiao-Ping Dong
    • 2
    • 4
    Email author
  1. 1.School of MedicineXi’an Jiaotong UniversityXi’anPeople’s Republic of China
  2. 2.State Key Laboratory for Infectious Disease Prevention and Control, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases (Hangzhou)National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and PreventionBeijingPeople’s Republic of China
  3. 3.Shandong International Travel HealthCare CenterShandong Entry-Exit Inspection and Quarantine BureauQingdaoPeople’s Republic of China
  4. 4.Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology and Immunology, Institute of MicrobiologyChinese Academy of SciencesBeijingPeople’s Republic of China

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