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p(MGI:Sqstm1)

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Entity

Name
Sqstm1
Namespace
mgi
Namespace Version
20181021
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/f2f993e599694ab5ce989cc39d789a499f75db99/external/mgi-names.belns

Appears in Networks 1

Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 5

a(CHEBI:heme) increases p(MGI:Sqstm1) View Subject | View Object

Beyond this common protein expression signature, the toxic heme response of Hmox1 (− /−) MEF cells was uniquely characterized by a cluster of strongly upregulated proteins. Within this cluster we identified ubiquitin, the ubiquitin adaptor protein sequestosome/p-62 (Sqstm1), a number of heat shock proteins, as well as antioxidant defense proteins (i.e., peroxiredoxins, glutathione-S-transferase, and thioredoxin reductase). PubMed:25301065

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a(CHEBI:heme) increases p(MGI:Sqstm1) View Subject | View Object

We confirmed by selected reaction monitoring (SRM) mode mass spectrometry (Figure 3a) and western blot (Figures 3c and d), respectively, that heme increased Sqstm1, ubiquitin, and Hsp70, with a much stronger response in Hmox1 (−/− ) compared with Hmox1 (+/+) MEF cells. PubMed:25301065

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a(CHEBI:heme) increases p(MGI:Sqstm1) View Subject | View Object

At higher extracellular heme concentrations, heme exposure dose dependently caused accumulation of myc-tagged Sqstm1 (Figure 3g). PubMed:25301065

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a(CHEBI:heme) negativeCorrelation deg(p(MGI:Sqstm1)) View Subject | View Object

This result strongly supports that high cellular heme concentration impairs degradation of Sqstm1 by the homeostatic protein degradation pathways. PubMed:25301065

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p(MGI:Hmox1) decreases p(MGI:Sqstm1) View Subject | View Object

We confirmed by selected reaction monitoring (SRM) mode mass spectrometry (Figure 3a) and western blot (Figures 3c and d), respectively, that heme increased Sqstm1, ubiquitin, and Hsp70, with a much stronger response in Hmox1 (−/− ) compared with Hmox1 (+/+) MEF cells. PubMed:25301065

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Out-Edges 1

deg(p(MGI:Sqstm1)) negativeCorrelation a(CHEBI:heme) View Subject | View Object

This result strongly supports that high cellular heme concentration impairs degradation of Sqstm1 by the homeostatic protein degradation pathways. PubMed:25301065

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About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.