Citation: NING Zhang-yong, ZHAO De-ming, YANG Jian-min, ZHOU Xian-mei, YU Bo, KONG Xiao-ming, YIN Xiao-min. The Impact of PrP106-126 on Prion Gene Expression of Cultured Neurons .VIROLOGICA SINICA, 2006, 21(6) : 609-613.

The Impact of PrP106-126 on Prion Gene Expression of Cultured Neurons

  • Corresponding author: ZHAO De-ming, 
  • Available online: 20 November 2006
  • The polypeptide fragment PrP106-126 of the cellular prion protein was utilized to construct the model of cultured cortical neurons and cerebellar granule cells. The model was used to study the viability of neurons and PrP gene expression. The results showed that the viability of cortical neurons and its PrP gene expression decreased significantly after incubation with PrP106-126, compared with that of the SCR-treated group and the control group. Similar results were obtained for treated cerebellar granule cells but with different extent and time phases. These findings provided relevant base-line data for understanding the function of the prion protein in diseases and for further studies of molecular pathogenesis of TSE.

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    The Impact of PrP106-126 on Prion Gene Expression of Cultured Neurons

      Corresponding author: ZHAO De-ming,
    • 1. 1. College of veterinary medicine, South China Agricultural University, Guangzhou 510642,China
    • 2. National Animal Transmissible Spongiform Encephalopathies Laboratory, China Agricultural University, Beijing 100094, China

    Abstract: The polypeptide fragment PrP106-126 of the cellular prion protein was utilized to construct the model of cultured cortical neurons and cerebellar granule cells. The model was used to study the viability of neurons and PrP gene expression. The results showed that the viability of cortical neurons and its PrP gene expression decreased significantly after incubation with PrP106-126, compared with that of the SCR-treated group and the control group. Similar results were obtained for treated cerebellar granule cells but with different extent and time phases. These findings provided relevant base-line data for understanding the function of the prion protein in diseases and for further studies of molecular pathogenesis of TSE.

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