Guidelines for the nomenclature of the human heat shock proteins

Kampinga, Harm H.; Hageman, Jurre; Vos, Michel J.; Kubota, Hiroshi; Tanguay, Robert M.; Bruford, Elspeth A.; Cheetham, Michael E.; Chen, Bin; Hightower, Lawrence E.

doi:10.1007/s12192-008-0068-7

Cited by 1,150 publications

(956 citation statements)

References 14 publications

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“…29 HSPs have been classified into several families according to their molecular weight, such as small HSPs (including HSP27), HSP40, HSP60, HSP70, HSP90 and HSP110. 35 Until recently, the expression status of HSPs and their prognostic and therapeutic implications for cancer have mainly focused on HSP27, HSP60, HSP70 and HSP90. 29,33 However, there have been insufficient investigations into the expression of HSP110, the mutations of HSPs and their clinical implications in cancer.…”

Section: Discussionmentioning

confidence: 99%

Expression status of wild-type HSP110 correlates with HSP110 T17 deletion size and patient prognosis in microsatellite-unstable colorectal cancer

Kim

Rhee

et al. 2014

Modern Pathology

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It has been recently suggested that the expression levels of mutant HSP110 could be a prognostic marker in colorectal cancer with a high level of microsatellite instability (MSI-H). The aim of our study was to validate the prognostic significance of HSP110 mutation using immunohistochemistry and DNA testing in MSI-H colorectal cancer. Wild-type HSP110 (HSP110wt)-specific immunohistochemistry was performed in 168 MSI-H colorectal cancer tissues, and their expression levels were evaluated using a four-tier scoring system (0/1 þ /2 þ /3 þ ). Of these tissues, 167 cases were analyzed for HSP110 T 17 deletion. Associations with clinicopathological, molecular and survival parameters were statistically analyzed. The low-level expression of HSP110wt (0/1 þ ) was observed in 40 MSI-H colorectal cancers (24%) and was significantly related to large HSP110 T 17 deletions (Z 4 bp, Po0.001). In survival analysis, patients with low HSP110wt expression (0/1 þ ) showed better diseasefree survival compared with those with high expression (2 þ /3 þ ; P ¼ 0.005). This significance in survival difference was maintained in patients with 5-fluorouracil-based chemotherapy-treated tumors (P ¼ 0.024) and in those with stage III/IV tumors (P ¼ 0.032). Multivariate analysis confirmed the role of HSP110wt expression as an independent prognostic factor (P ¼ 0.016, hazard ratio ¼ 4.32). In MSI-H colorectal cancer, a low expression of HSP110wt is associated with large HSP110 T 17 deletions and better clinical outcome. Immunohistochemistry of HSP110wt can be a simple and valuable tool for the prognostic and therapeutic stratification of patients with MSI-H colorectal cancer.

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Section: Discussionmentioning

confidence: 99%

Expression status of wild-type HSP110 correlates with HSP110 T17 deletion size and patient prognosis in microsatellite-unstable colorectal cancer

Kim

Rhee

et al. 2014

Modern Pathology

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“…HSPs are classified in six sub groups: HSPA (HSP70), HSPB (small HSPs), HSPC (HSP90), HSPD and HSPE (chaperonin families HSP60 and HSP10, respectively), HSPH (HSP110), and DNAJ (HSP40) 29 . Each subgroup comprises several family members and cofactors with distinct and/or overlapping functions, which are localized in various cellular com partments 30,31 .…”

Section: The Proteostasis Network Componentsmentioning

confidence: 99%

“…Diverse reports have described a caus ative relationship between mutations in small HSPs and develop ment of cardiac disease. The human family of small HSPs consists of ten members (HSPB1 to HSPB10) 29 , which share a highly conserved C terminal α crystallin domain 80 . Knowledge about the different functionalities of these ten members of the HSPB fam ily is only beginning to emerge, but data indicate their importance in human pathology as a cause of disease when mutated 30,81 .…”

Section: Derailment Owing To Genetic Mutationsmentioning

confidence: 99%

Proteostasis in cardiac health and disease

Henning

Brundel²

2017

Nat Rev Cardiol

137

126

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The worldwide increase in life expectancy gives rise to an increasing prevalence of cardiac diseases, which remain the leading cause of disability and death in the developed world [1][2][3] . Currently, the mechanisms under lying how ageing contributes to the initiation or acceler ation of cardiac diseases are essentially unresolved. Prevailing theories of ageing centre on gradual derail ment of cellular protein homeostasis -proteostasis -either by design (genetically) or by 'wear and tear' (environmentally) 3 . Central to the role of proteostasis derailment as a major factor in ageing is the observation that protein function declines over time.Proteins are the most versatile and complex macro molecules and are involved in the proper functioning of every biological process 4 . After synthesis as a poly peptide chain from the genetic code, proper function of a protein relies heavily on its correct folding into a 3D native state and on various post translational modifi cations, mostly involving the addition of chem ical groups (including phosphate, acetate, and carbo hydrate). Protein maturation, transport, and ultimately breakdown is monitored and supported by various classes of proteins, collectively called 'protein quality control' (PQC) [3][4][5] . Balanced proteostasis, therefore, depends on proper PQC and is crucial for cellular and organismal health 6 . The intricate network making up the PQC involves numerous proteins, of which the main players are the chaperones and their regula tors 4,7-9 (assisting in folding and refolding of proteins) and the pathways that clear irreversibly misfolded and aggregation prone proteins (the ubiquitin-proteasome system [UPS] and autophagy systems) 9-11 . With ageing, the gradual accumulation of misfolded or damaged pro teins, together with concomitant failure of PQC, results in proteotoxic stress and compromised defence against reactive oxygen species (ROS) 10 , a process that is likely to be accelerated in various age related diseases includ ing neurodegenerative diseases 12,13 , type 2 diabetes mel litus 14 , cancer 15 , and cardiac diseases [16][17][18][19][20] . In addition to the accumulation of misfolded proteins, ageing is accompanied by an imbalance in the proteome, as indi cated by lowered expression of chaperone, proteaso mal, ribosomal, and mitochondrial proteins, whereas proteins related to oxidative stress are upregulated 21,22 . Although mild impairment of proteostasis extends lifespan in Caenorhabditis elegans, referred to as hormesis, sustained impairment is accompanied by loss of PQC to neutralize this effect 3,5 . Importantly, evidence indicates that the amount of soluble, aggregate prone protein oligomers, rather than the abundance of pro tein aggregates, correlates with disease severity 23,24 . Therefore, protein aggregates, which contain both misfolded proteins and elevated levels of chaper ones, constitute an adequate PQC response, aimed at sequestering potentially harmful protein oligomers, rather than embodying the ultimate cellular threat 25 . This ...

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“…Hsp10 typically functions as chaperone in mitochondria together with Hsp60 (Jia et al, 2011). In general, Hsp proteins function as molecular chaperones by supporting the folding of newly synthesized polypeptides and the assembly of multi-protein complexes (Beckmann et al, 1990;Kampinga et al, 2009;Jakob et al, 1993). SIRT1 has been shown to maintain the DNA-binding state of HSF1 for Hsp70 induction (Liu et al, 2014) whereas Hsp10 has proven to be a functional SIRT3 substrate (Lu et al, 2015).…”

Section: Introductionmentioning

confidence: 99%