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Entity

Name
huntingtin aggregates
Namespace
HBP
Namespace Version
20190206
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/3c85897632afa791ac78fb3aa2e392963ab155b1/export/hbp-names.belns

Appears in Networks 6

In-Edges 18

a(PUBCHEM:1560402) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

In addition, SMER-10, -18, and -28 were effective at suppressing mHTT aggregation and toxicity in COS-7 cells and flies (146). PubMed:25784053

Annotations
Cell Ontology (CL)
motor neuron

a(PUBCHEM:799645) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

In addition, SMER-10, -18, and -28 were effective at suppressing mHTT aggregation and toxicity in COS-7 cells and flies (146). PubMed:25784053

Annotations
Cell Ontology (CL)
motor neuron

p(FPLX:"CCT_complex") increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

p(HGNC:CCT5) causesNoChange a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

p(HGNC:CDC23) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

p(HGNC:CDC27) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

p(HGNC:DNAJA1) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

p(HGNC:DNAJA4) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

p(HGNC:HSPA14) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

p(HGNC:HSPA8) increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

a(CHEBI:"Congo Red") decreases a(HBP:"huntingtin aggregates") View Subject | View Object

If oligomerization of mutant Huntingtin is inhibited by administration of Congo red starting at this age, no aggregates can be detected in the brain 5weeks later (Sanchez et al., 2003). PubMed:14556719

p(HGNC:HTT, var("?")) increases a(HBP:"huntingtin aggregates") View Subject | View Object

However, a contribution to the pathogenesis by loss of function of Huntingtin encoded from the wild-type allele has not been excluded in HD (Cattaneo et al., 2001), since the mutant protein not only aggregates itself but can also promote aggregation of the wild-type protein (Busch et al.,2003). PubMed:14556719

a(PUBCHEM:877863) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

In addition, SMER-10, -18, and -28 were effective at suppressing mHTT aggregation and toxicity in COS-7 cells and flies (146). PubMed:25784053

Annotations
Cell Ontology (CL)
motor neuron

p(FPLX:"CCT_complex") decreases a(HBP:"huntingtin aggregates") View Subject | View Object

TRiC also interacts with N-terminal fragments of mutant huntingtin that contain an expanded polyglutamine repeat sequence (165–168). Binding to TRiC modulates the aggregation properties of this protein and reduces its cytotoxicity. PubMed:23746257

p(FPLX:HSPA) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

This approach is based on multiple lines of evidence demonstrating that overexpression of chaperones such as Hsp70 and Hsp40 prevents the aggregation and toxicity of huntingtin and α-synuclein (38, 231–234). PubMed:23746257

composite(p(FPLX:"CCT_complex"), p(FPLX:HSPA)) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

The Hsp70 system acts synergistically with the cytosolic chaperonin TRiC to prevent aggregation of proteins with expanded polyglutamine tracts (165–168). PubMed:23746257

p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") decreases a(HBP:"huntingtin aggregates") View Subject | View Object

This approach is based on multiple lines of evidence demonstrating that overexpression of chaperones such as Hsp70 and Hsp40 prevents the aggregation and toxicity of huntingtin and α-synuclein (38, 231–234). PubMed:23746257

Out-Edges 2

a(HBP:"huntingtin aggregates") decreases bp(GO:"clathrin-dependent endocytosis") View Subject | View Object

CME inhibition was also observed in cells containing aggregated forms of polyQ- expanded Htt exon 1 (Htt Q53); these cells exhibited 50 ± 15% reduced levels of internalized transferrin compared with cells with soluble Htt Q23 or Htt Q53 protein (Fig. S2 A–C ). PubMed:24706768

a(HBP:"huntingtin aggregates") decreases bp(GO:"clathrin-dependent endocytosis") View Subject | View Object

In contrast, there was a marked reduction in CME in neurons containing mutant Htt exon 1 Q73-CFP aggregates compared with nonexpressing cells (Fig. 5 B , Center ; quantification in Fig. 5 D ); PubMed:24706768

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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.