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Proteomics analyses for the global proteins in the brain tissues of different human prion diseases.

Shi Q, Chen LN, Zhang BY, Xiao K, Zhou W, Chen C, Zhang XM, Tian C, Gao C, Wang J, Han J, Dong XP - Mol. Cell Proteomics (2015)

Bottom Line: Global protein profiling, significant pathway, and functional categories were analyzed.Almost coincident biological functions were identified in the brain tissues of the three diseases.This is the first study to provide a reference proteome map for human prion diseases and will be helpful for future studies focused on potential biomarkers for the diagnosis and therapy of human prion diseases.

View Article: PubMed Central - PubMed

Affiliation: From the ‡State Key Laboratory for Infectious Disease Prevention and Control, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases (Zhejiang University, Hangzhou 310003), National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Chang-Bai Rd 155, Beijing 102206, People's Republic of China;

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The percentages of whole changed proteins in cortex and cerebellum regions of sCJD, FFI, and G114V sCJD based on their changing folds. The changed proteins are grouped as up-regulation (>2.4-fold, 1.8–2.4-fold, and 1.2–1.8-fold) and down-regulation (0.8–0.6-fold, 0.6–0.4-fold, and <0.4-fold) after normalized with those of normal control. The percentage of the changed proteins in each group was showed on the bottom.
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Figure 3: The percentages of whole changed proteins in cortex and cerebellum regions of sCJD, FFI, and G114V sCJD based on their changing folds. The changed proteins are grouped as up-regulation (>2.4-fold, 1.8–2.4-fold, and 1.2–1.8-fold) and down-regulation (0.8–0.6-fold, 0.6–0.4-fold, and <0.4-fold) after normalized with those of normal control. The percentage of the changed proteins in each group was showed on the bottom.

Mentions: To obtain the overviews of the brain protein alterations in various subtypes of human prion diseases, the changing values of individual 2287 identified proteins in every disease were displayed logarithmically after being normalized with the data of normal controls. As shown in supplemental Fig. S2A, in the assays of cortex regions, G114V gCJD and sCJD appeared to have more dots in the areas of higher or lower log values than FFI, whereas in the pictures of cerebellum, the dot distributions of three prion diseases were quite similar (supplemental Fig. S2B). Furthermore, the numbers of the changed proteins were counted and grouped based on their changing folds, including the up-regulation of [gt]2.4-fold, 1.8–2.4-fold, 1.2–1.8-fold, the down-regulation of 0.8–0.6-fold, 0.6–0.4-fold and <0.4-fold. The percentage of the changed proteins in each group was calculated in the context of whole changed proteins. As illustrated in Fig. 3, majorities of the changed proteins in cortex and cerebellum of three prion diseases were located in the mildly changed groups (1.2–1.8 fold up-regulation and 0.8–0.6 fold down-regulation). Compared with sCJD and G114V gCJD, FFI had lower percentages in the severely [gt]2.4-fold increased and <0.4-fold decreased) and moderately (1.8–2.4-fold increased and 0.6–0.4-fold decreased) changed groups in cortex, while they had lower percentages only in the severely changed groups in cerebellum. The portions of the proteins in severely and moderately changed groups of the cerebellum were higher than that of the cortex in all tested prion diseases. In addition, the ratios of down-regulated proteins in the severely and moderately changed groups were higher than that of up-regulated ones (Fig. 3).


Proteomics analyses for the global proteins in the brain tissues of different human prion diseases.

Shi Q, Chen LN, Zhang BY, Xiao K, Zhou W, Chen C, Zhang XM, Tian C, Gao C, Wang J, Han J, Dong XP - Mol. Cell Proteomics (2015)

The percentages of whole changed proteins in cortex and cerebellum regions of sCJD, FFI, and G114V sCJD based on their changing folds. The changed proteins are grouped as up-regulation (>2.4-fold, 1.8–2.4-fold, and 1.2–1.8-fold) and down-regulation (0.8–0.6-fold, 0.6–0.4-fold, and <0.4-fold) after normalized with those of normal control. The percentage of the changed proteins in each group was showed on the bottom.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4390265&req=5

Figure 3: The percentages of whole changed proteins in cortex and cerebellum regions of sCJD, FFI, and G114V sCJD based on their changing folds. The changed proteins are grouped as up-regulation (>2.4-fold, 1.8–2.4-fold, and 1.2–1.8-fold) and down-regulation (0.8–0.6-fold, 0.6–0.4-fold, and <0.4-fold) after normalized with those of normal control. The percentage of the changed proteins in each group was showed on the bottom.
Mentions: To obtain the overviews of the brain protein alterations in various subtypes of human prion diseases, the changing values of individual 2287 identified proteins in every disease were displayed logarithmically after being normalized with the data of normal controls. As shown in supplemental Fig. S2A, in the assays of cortex regions, G114V gCJD and sCJD appeared to have more dots in the areas of higher or lower log values than FFI, whereas in the pictures of cerebellum, the dot distributions of three prion diseases were quite similar (supplemental Fig. S2B). Furthermore, the numbers of the changed proteins were counted and grouped based on their changing folds, including the up-regulation of [gt]2.4-fold, 1.8–2.4-fold, 1.2–1.8-fold, the down-regulation of 0.8–0.6-fold, 0.6–0.4-fold and <0.4-fold. The percentage of the changed proteins in each group was calculated in the context of whole changed proteins. As illustrated in Fig. 3, majorities of the changed proteins in cortex and cerebellum of three prion diseases were located in the mildly changed groups (1.2–1.8 fold up-regulation and 0.8–0.6 fold down-regulation). Compared with sCJD and G114V gCJD, FFI had lower percentages in the severely [gt]2.4-fold increased and <0.4-fold decreased) and moderately (1.8–2.4-fold increased and 0.6–0.4-fold decreased) changed groups in cortex, while they had lower percentages only in the severely changed groups in cerebellum. The portions of the proteins in severely and moderately changed groups of the cerebellum were higher than that of the cortex in all tested prion diseases. In addition, the ratios of down-regulated proteins in the severely and moderately changed groups were higher than that of up-regulated ones (Fig. 3).

Bottom Line: Global protein profiling, significant pathway, and functional categories were analyzed.Almost coincident biological functions were identified in the brain tissues of the three diseases.This is the first study to provide a reference proteome map for human prion diseases and will be helpful for future studies focused on potential biomarkers for the diagnosis and therapy of human prion diseases.

View Article: PubMed Central - PubMed

Affiliation: From the ‡State Key Laboratory for Infectious Disease Prevention and Control, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases (Zhejiang University, Hangzhou 310003), National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Chang-Bai Rd 155, Beijing 102206, People's Republic of China;

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Related in: MedlinePlus