By the same authors

Endoplasmic reticulum (ER) stress in amyotrophic lateral sclerosis (ALS)

Research output: Chapter in Book/Report/Conference proceedingChapter

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Endoplasmic reticulum (ER) stress in amyotrophic lateral sclerosis (ALS). / Chen, Han Jou; De Belleroche, Jackie.

Endoplasmic Reticulum Stress in Health and Disease. Vol. 9789400743519 Springer Netherlands, 2012. p. 323-337.

Research output: Chapter in Book/Report/Conference proceedingChapter

Harvard

Chen, HJ & De Belleroche, J 2012, Endoplasmic reticulum (ER) stress in amyotrophic lateral sclerosis (ALS). in Endoplasmic Reticulum Stress in Health and Disease. vol. 9789400743519, Springer Netherlands, pp. 323-337. https://doi.org/10.1007/978-94-007-4351-9_14

APA

Chen, H. J., & De Belleroche, J. (2012). Endoplasmic reticulum (ER) stress in amyotrophic lateral sclerosis (ALS). In Endoplasmic Reticulum Stress in Health and Disease (Vol. 9789400743519, pp. 323-337). Springer Netherlands. https://doi.org/10.1007/978-94-007-4351-9_14

Vancouver

Chen HJ, De Belleroche J. Endoplasmic reticulum (ER) stress in amyotrophic lateral sclerosis (ALS). In Endoplasmic Reticulum Stress in Health and Disease. Vol. 9789400743519. Springer Netherlands. 2012. p. 323-337 https://doi.org/10.1007/978-94-007-4351-9_14

Author

Chen, Han Jou ; De Belleroche, Jackie. / Endoplasmic reticulum (ER) stress in amyotrophic lateral sclerosis (ALS). Endoplasmic Reticulum Stress in Health and Disease. Vol. 9789400743519 Springer Netherlands, 2012. pp. 323-337

Bibtex - Download

@inbook{ff4de187039e47f798cc8c2c85917362,
title = "Endoplasmic reticulum (ER) stress in amyotrophic lateral sclerosis (ALS)",
abstract = "There have been considerable advances in understanding amyotrophic lateral sclerosis/motor neuron disease (ALS), particularly within the last 5 years with the identification of mutations in 4 key genes, TARDBP, FUS, VCP and VAPB that cause familial ALS. The strong association of TDP-43 with ubiquitinated protein aggregates in motor neurons, a hallmark of ALS in sporadic cases of ALS, clearly demonstrates the importance of these findings for understanding the pathology of sporadic cases. All of these genes are known to be involved in multiple cellular pathways but the key features that underpin ALS remain to be elucidated. What is known is that these causal genes result in a severe perturbation in the removal of mis-folded proteins with the accumulation of aggregated proteins. This may in part be due to protein degradation and mislocation and in some instances, it may be due to a direct effect on endogenous components of cellular protein control, the unfolded protein response (UPR) which operates within the endoplasmic reticulum (ER) and protein degradation pathways such as the ubiquitin proteasomal system (UPS) and early and late autophagy. Mutations in Vesicle associated protein-associated protein B (VAPB) and Valosin containing protein (VCP) cause familial Amyotrophic Lateral Sclerosis (FALS), which strongly indicates the importance of the prosurvival properties of these proteins in endoplasmic reticulum (ER) stress responses. The main components of ER stress and associated pathways include the unfolded protein response (UPR), ER-associated degradation (ERAD), the ubiquitin-proteasome system (UPS) and autophagy, all of which are known to be activated in ALS.",
keywords = "Amyotrophic lateral sclerosis, Apoptosis, Autophagy, Cell culture, Experimental models, Familial amyotrophic lateral sclerosis, Frontotemporal dementia, Frontotemporal lobar degeneration, Fusion in sarcoma gene, Keywords:: Endoplasmic reticulum stress, Motor neuron disease, Protein aggregates, TARDBP: TAR DNA-binding protein gene, TDP-43: TAR DNA-binding protein 43, Ubiquitin proteasomal system, Unfolded prortein response, Valosin containing protein, Vesicle associated protein-associated protein B",
author = "Chen, {Han Jou} and {De Belleroche}, Jackie",
year = "2012",
month = "3",
day = "1",
doi = "10.1007/978-94-007-4351-9_14",
language = "English",
isbn = "9400743505",
volume = "9789400743519",
pages = "323--337",
booktitle = "Endoplasmic Reticulum Stress in Health and Disease",
publisher = "Springer Netherlands",
address = "Netherlands",

}

RIS (suitable for import to EndNote) - Download

TY - CHAP

T1 - Endoplasmic reticulum (ER) stress in amyotrophic lateral sclerosis (ALS)

AU - Chen, Han Jou

AU - De Belleroche, Jackie

PY - 2012/3/1

Y1 - 2012/3/1

N2 - There have been considerable advances in understanding amyotrophic lateral sclerosis/motor neuron disease (ALS), particularly within the last 5 years with the identification of mutations in 4 key genes, TARDBP, FUS, VCP and VAPB that cause familial ALS. The strong association of TDP-43 with ubiquitinated protein aggregates in motor neurons, a hallmark of ALS in sporadic cases of ALS, clearly demonstrates the importance of these findings for understanding the pathology of sporadic cases. All of these genes are known to be involved in multiple cellular pathways but the key features that underpin ALS remain to be elucidated. What is known is that these causal genes result in a severe perturbation in the removal of mis-folded proteins with the accumulation of aggregated proteins. This may in part be due to protein degradation and mislocation and in some instances, it may be due to a direct effect on endogenous components of cellular protein control, the unfolded protein response (UPR) which operates within the endoplasmic reticulum (ER) and protein degradation pathways such as the ubiquitin proteasomal system (UPS) and early and late autophagy. Mutations in Vesicle associated protein-associated protein B (VAPB) and Valosin containing protein (VCP) cause familial Amyotrophic Lateral Sclerosis (FALS), which strongly indicates the importance of the prosurvival properties of these proteins in endoplasmic reticulum (ER) stress responses. The main components of ER stress and associated pathways include the unfolded protein response (UPR), ER-associated degradation (ERAD), the ubiquitin-proteasome system (UPS) and autophagy, all of which are known to be activated in ALS.

AB - There have been considerable advances in understanding amyotrophic lateral sclerosis/motor neuron disease (ALS), particularly within the last 5 years with the identification of mutations in 4 key genes, TARDBP, FUS, VCP and VAPB that cause familial ALS. The strong association of TDP-43 with ubiquitinated protein aggregates in motor neurons, a hallmark of ALS in sporadic cases of ALS, clearly demonstrates the importance of these findings for understanding the pathology of sporadic cases. All of these genes are known to be involved in multiple cellular pathways but the key features that underpin ALS remain to be elucidated. What is known is that these causal genes result in a severe perturbation in the removal of mis-folded proteins with the accumulation of aggregated proteins. This may in part be due to protein degradation and mislocation and in some instances, it may be due to a direct effect on endogenous components of cellular protein control, the unfolded protein response (UPR) which operates within the endoplasmic reticulum (ER) and protein degradation pathways such as the ubiquitin proteasomal system (UPS) and early and late autophagy. Mutations in Vesicle associated protein-associated protein B (VAPB) and Valosin containing protein (VCP) cause familial Amyotrophic Lateral Sclerosis (FALS), which strongly indicates the importance of the prosurvival properties of these proteins in endoplasmic reticulum (ER) stress responses. The main components of ER stress and associated pathways include the unfolded protein response (UPR), ER-associated degradation (ERAD), the ubiquitin-proteasome system (UPS) and autophagy, all of which are known to be activated in ALS.

KW - Amyotrophic lateral sclerosis

KW - Apoptosis

KW - Autophagy

KW - Cell culture

KW - Experimental models

KW - Familial amyotrophic lateral sclerosis

KW - Frontotemporal dementia

KW - Frontotemporal lobar degeneration

KW - Fusion in sarcoma gene

KW - Keywords:: Endoplasmic reticulum stress

KW - Motor neuron disease

KW - Protein aggregates

KW - TARDBP: TAR DNA-binding protein gene

KW - TDP-43: TAR DNA-binding protein 43

KW - Ubiquitin proteasomal system

KW - Unfolded prortein response

KW - Valosin containing protein

KW - Vesicle associated protein-associated protein B

UR - http://www.scopus.com/inward/record.url?scp=84931407177&partnerID=8YFLogxK

U2 - 10.1007/978-94-007-4351-9_14

DO - 10.1007/978-94-007-4351-9_14

M3 - Chapter

AN - SCOPUS:84931407177

SN - 9400743505

SN - 9789400743502

VL - 9789400743519

SP - 323

EP - 337

BT - Endoplasmic Reticulum Stress in Health and Disease

PB - Springer Netherlands

ER -