Publication

Barcoding heat shock proteins to human diseases: looking beyond the heat shock response

Kakkar, V., Meister-Broekema, M., Minoia, M., Carra, S. & Kampinga, H. H., Apr-2014, In : Disease models & mechanisms. 7, 4, p. 421-434 14 p.

Research output: Contribution to journalReview articleAcademicpeer-review

APA

Kakkar, V., Meister-Broekema, M., Minoia, M., Carra, S., & Kampinga, H. H. (2014). Barcoding heat shock proteins to human diseases: looking beyond the heat shock response. Disease models & mechanisms, 7(4), 421-434. https://doi.org/10.1242/dmm.014563

Author

Kakkar, Vaishali ; Meister-Broekema, Melanie ; Minoia, Melania ; Carra, Serena ; Kampinga, Harm H. / Barcoding heat shock proteins to human diseases : looking beyond the heat shock response. In: Disease models & mechanisms. 2014 ; Vol. 7, No. 4. pp. 421-434.

Harvard

Kakkar, V, Meister-Broekema, M, Minoia, M, Carra, S & Kampinga, HH 2014, 'Barcoding heat shock proteins to human diseases: looking beyond the heat shock response', Disease models & mechanisms, vol. 7, no. 4, pp. 421-434. https://doi.org/10.1242/dmm.014563

Standard

Barcoding heat shock proteins to human diseases : looking beyond the heat shock response. / Kakkar, Vaishali; Meister-Broekema, Melanie; Minoia, Melania; Carra, Serena; Kampinga, Harm H.

In: Disease models & mechanisms, Vol. 7, No. 4, 04.2014, p. 421-434.

Research output: Contribution to journalReview articleAcademicpeer-review

Vancouver

Kakkar V, Meister-Broekema M, Minoia M, Carra S, Kampinga HH. Barcoding heat shock proteins to human diseases: looking beyond the heat shock response. Disease models & mechanisms. 2014 Apr;7(4):421-434. https://doi.org/10.1242/dmm.014563


BibTeX

@article{9b19bce1153c4e0298d3fdbae34c142a,
title = "Barcoding heat shock proteins to human diseases: looking beyond the heat shock response",
abstract = "There are numerous human diseases that are associated with protein misfolding and the formation of toxic protein aggregates. Activating the heat shock response (HSR) - and thus generally restoring the disturbed protein homeostasis associated with such diseases - has often been suggested as a therapeutic strategy. However, most data on activating the HSR or its downstream targets in mouse models of diseases associated with aggregate formation have been rather disappointing. The human chaperonome consists of many more heat shock proteins (HSPs) that are not regulated by the HSR, however, and researchers are now focusing on these as potential therapeutic targets. In this Review, we summarize the existing literature on a set of aggregation diseases and propose that each of them can be characterized or `barcoded' by a different set of HSPs that can rescue specific types of aggregation. Some of these 'non-canonical' HSPs have demonstrated effectiveness in vivo, in mouse models of protein-aggregation disease. Interestingly, several of these HSPs also cause diseases when mutated - so-called chaperonopathies - which are also discussed in this Review.",
keywords = "Chaperonopathies, Heat shock protein, Protein-aggregation diseases, AMYOTROPHIC-LATERAL-SCLEROSIS, ALPHA-B-CRYSTALLIN, UBIQUITIN-PROTEASOME SYSTEM, RECESSIVE SPASTIC ATAXIA, TRANSGENIC MOUSE MODEL, BARDET-BIEDL-SYNDROME, POLYGLUTAMINE-INDUCED NEURODEGENERATION, SYNUCLEIN-INDUCED TOXICITY, AGGREGATION IN-VITRO, MOLECULAR CHAPERONES",
author = "Vaishali Kakkar and Melanie Meister-Broekema and Melania Minoia and Serena Carra and Kampinga, {Harm H.}",
year = "2014",
month = apr,
doi = "10.1242/dmm.014563",
language = "English",
volume = "7",
pages = "421--434",
journal = "Disease models & mechanisms",
issn = "1754-8403",
publisher = "COMPANY OF BIOLOGISTS LTD",
number = "4",

}

RIS

TY - JOUR

T1 - Barcoding heat shock proteins to human diseases

T2 - looking beyond the heat shock response

AU - Kakkar, Vaishali

AU - Meister-Broekema, Melanie

AU - Minoia, Melania

AU - Carra, Serena

AU - Kampinga, Harm H.

PY - 2014/4

Y1 - 2014/4

N2 - There are numerous human diseases that are associated with protein misfolding and the formation of toxic protein aggregates. Activating the heat shock response (HSR) - and thus generally restoring the disturbed protein homeostasis associated with such diseases - has often been suggested as a therapeutic strategy. However, most data on activating the HSR or its downstream targets in mouse models of diseases associated with aggregate formation have been rather disappointing. The human chaperonome consists of many more heat shock proteins (HSPs) that are not regulated by the HSR, however, and researchers are now focusing on these as potential therapeutic targets. In this Review, we summarize the existing literature on a set of aggregation diseases and propose that each of them can be characterized or `barcoded' by a different set of HSPs that can rescue specific types of aggregation. Some of these 'non-canonical' HSPs have demonstrated effectiveness in vivo, in mouse models of protein-aggregation disease. Interestingly, several of these HSPs also cause diseases when mutated - so-called chaperonopathies - which are also discussed in this Review.

AB - There are numerous human diseases that are associated with protein misfolding and the formation of toxic protein aggregates. Activating the heat shock response (HSR) - and thus generally restoring the disturbed protein homeostasis associated with such diseases - has often been suggested as a therapeutic strategy. However, most data on activating the HSR or its downstream targets in mouse models of diseases associated with aggregate formation have been rather disappointing. The human chaperonome consists of many more heat shock proteins (HSPs) that are not regulated by the HSR, however, and researchers are now focusing on these as potential therapeutic targets. In this Review, we summarize the existing literature on a set of aggregation diseases and propose that each of them can be characterized or `barcoded' by a different set of HSPs that can rescue specific types of aggregation. Some of these 'non-canonical' HSPs have demonstrated effectiveness in vivo, in mouse models of protein-aggregation disease. Interestingly, several of these HSPs also cause diseases when mutated - so-called chaperonopathies - which are also discussed in this Review.

KW - Chaperonopathies

KW - Heat shock protein

KW - Protein-aggregation diseases

KW - AMYOTROPHIC-LATERAL-SCLEROSIS

KW - ALPHA-B-CRYSTALLIN

KW - UBIQUITIN-PROTEASOME SYSTEM

KW - RECESSIVE SPASTIC ATAXIA

KW - TRANSGENIC MOUSE MODEL

KW - BARDET-BIEDL-SYNDROME

KW - POLYGLUTAMINE-INDUCED NEURODEGENERATION

KW - SYNUCLEIN-INDUCED TOXICITY

KW - AGGREGATION IN-VITRO

KW - MOLECULAR CHAPERONES

U2 - 10.1242/dmm.014563

DO - 10.1242/dmm.014563

M3 - Review article

C2 - 24719117

VL - 7

SP - 421

EP - 434

JO - Disease models & mechanisms

JF - Disease models & mechanisms

SN - 1754-8403

IS - 4

ER -

ID: 14138845