scholarly journals The Role of Non-Canonical Hsp70s (Hsp110/Grp170) in Cancer

2020 ◽  
Author(s):  
Graham Chakafana ◽  
Addmore Shonhai
Keyword(s):  
Heat Shock ◽  
Drug Targets ◽  
Structural Features ◽  
Cancer Development ◽  
Fair Share ◽  
E Coli ◽  
Binding Domains ◽  
Current Review ◽  
Shock Proteins

Although cancers account for over 16% of all global deaths annually, at present, no reliable therapies exist for most types of the disease. As protein folding facilitators, heat shock proteins (Hsps) play an important role in cancer development. Not surprisingly, Hsps are among leading anticancer drug targets. Generally, Hsp70s are divided into two main subtypes: canonical Hsp70 (E. coli Hsp70/DnaK homologues) and the non-canonical (Hsp110 and Grp170) members. These two main Hsp70 groups are delineated from each other by distinct structural and functional specifications. Non-canonical Hsp70s are considered as holdase chaperones, while canonical Hsp70s are refoldases. This distinct characteristic feature is mirrored by the distinct structural features of these two groups of chaperones. Hsp110/Grp170 members are larger as they possess an extended acidic insertion in their substrate binding domains. While the role of canonical Hsp70s in cancer has received a fair share of attention, the roles of non-canonical Hsp70s in cancer development has received less attention in comparison. In the current review, we discuss the structure-function features of non-canonical Hsp70s members and how these features impact on their role in cancer development. We further mapped out their interactome and discussed the prospects of targeting these proteins in cancer therapy.

scholarly journals The Role of Non-Canonical Hsp70s (Hsp110/Grp170) in Cancer

Cells ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 254
Author(s):  
Graham Chakafana ◽  
Addmore Shonhai
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Drug Targets ◽  
Structural Features ◽  
Cancer Development ◽  
Fair Share ◽  
Binding Domains ◽  
Current Review ◽  
Shock Proteins

Although cancers account for over 16% of all global deaths annually, at present, no reliable therapies exist for most types of the disease. As protein folding facilitators, heat shock proteins (Hsps) play an important role in cancer development. Not surprisingly, Hsps are among leading anticancer drug targets. Generally, Hsp70s are divided into two main subtypes: canonical Hsp70 (Escherichia coli Hsp70/DnaK homologues) and the non-canonical (Hsp110 and Grp170) members. These two main Hsp70 groups are delineated from each other by distinct structural and functional specifications. Non-canonical Hsp70s are considered as holdase chaperones, while canonical Hsp70s are refoldases. This unique characteristic feature is mirrored by the distinct structural features of these two groups of chaperones. Hsp110/Grp170 members are larger as they possess an extended acidic insertion in their substrate binding domains. While the role of canonical Hsp70s in cancer has received a fair share of attention, the roles of non-canonical Hsp70s in cancer development has received less attention in comparison. In the current review, we discuss the structure-function features of non-canonical Hsp70s members and how these features impact their role in cancer development. We further mapped out their interactome and discussed the prospects of targeting these proteins in cancer therapy.

The Biological Role of the Universally Conserved E. coli Heat Shock Proteins

Heat Shock ◽  
1991 ◽  
pp. 45-53 ◽  
Author(s):  
D. Ang ◽  
T. Ziegelhoffer ◽  
A. Maddock ◽  
J. Zeilstra-Ryalls ◽  
C. Georgopoulos ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Biological Role ◽  
E Coli ◽  
Shock Proteins

scholarly journals Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi

2015 ◽  
Vol 2015 ◽  
pp. 1-11 ◽  
Author(s):  
Shraddha Tiwari ◽  
Raman Thakur ◽  
Jata Shankar
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Posttranslational Modifications ◽  
Biological Processes ◽  
Current Review ◽  
Hsp60 Expression ◽  
Response To Stress ◽  
Aggregation And Disaggregation ◽  
Shock Proteins

Stress (biotic or abiotic) is an unfavourable condition for an organism including fungus. To overcome stress, organism expresses heat-shock proteins (Hsps) or chaperons to perform biological function. Hsps are involved in various routine biological processes such as transcription, translation and posttranslational modifications, protein folding, and aggregation and disaggregation of proteins. Thus, it is important to understand holistic role of Hsps in response to stress and other biological conditions in fungi. Hsp104, Hsp70, and Hsp40 are found predominant in replication and Hsp90 is found in transcriptional and posttranscriptional process. Hsp90 and Hsp70 in combination or alone play a major role in morphogenesis and dimorphism. Heat stress in fungi expresses Hsp60, Hsp90, Hsp104, Hsp30, and Hsp10 proteins, whereas expression of Hsp12 protein was observed in response to cold stress. Hsp30, Hsp70, and Hsp90 proteins showed expression in response to pH stress. Osmotic stress is controlled by small heat-shock proteins and Hsp60. Expression of Hsp104 is observed under high pressure conditions. Out of these heat-shock proteins, Hsp90 has been predicted as a potential antifungal target due to its role in morphogenesis. Thus, current review focuses on role of Hsps in fungi during morphogenesis and various stress conditions (temperature, pH, and osmotic pressure) and in antifungal drug tolerance.

In Vitro Holdase Activity of E. coli Small Heat-Shock Proteins IbpA, IbpB and IbpAB: A Biophysical Study with Some Unconventional Techniques

2014 ◽  
Vol 21 (6) ◽  
pp. 564-571 ◽  
Author(s):  
Sourav Roy ◽  
Monobesh Patra ◽  
Suman Nandy ◽  
Milon Banik ◽  
Rakhi Dasgupta ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Biophysical Study ◽  
Shock Proteins

Malaria Heat Shock Proteins: Drug Targets that Chaperone other Drug Targets

2010 ◽  
Vol 10 (3) ◽  
pp. 147-157 ◽  
Author(s):  
E.-R. Pesce ◽  
I.L. Cockburn ◽  
J.L. Goble ◽  
L.L. Stephens ◽  
G.L. Blatch
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Drug Targets ◽  
Shock Proteins

The Small Heat-shock Proteins IbpA and IbpB in E. coli: The Small Ones With a Big Role

2016 ◽  
Vol 9 (2) ◽  
pp. 84-96
Author(s):  
Sanchari Bhattacharjee ◽  
Rakhi Dasgupta ◽  
Angshuman Bagchi
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Shock Proteins

ATPase inhibition by omeprazole reveals role of heat shock proteins on testicular torsion

Andrologia ◽  
2020 ◽  
Author(s):  
Cengiz Güney ◽  
Kübra Açıkalın Coşkun ◽  
Yusuf Tutar
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Testicular Torsion ◽  
Shock Proteins ◽  
Atpase Inhibition

scholarly journals Oncogenic Functions and Clinical Significance of Circular RNAs in Colorectal Cancer

Cancers ◽  
2021 ◽  
Vol 13 (14) ◽  
pp. 3395
Author(s):  
Maria Radanova ◽  
Galya Mihaylova ◽  
Neshe Nazifova-Tasinova ◽  
Mariya Levkova ◽  
Oskan Tasinov ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Drug Targets ◽  
Clinicopathological Characteristics ◽  
Circular Rnas ◽  
Diagnostic Biomarkers ◽  
The Third ◽  
Current Review ◽  
Important Challenge ◽  
Prediction Of Metastasis

Colorectal cancer (CRC) is ranked as the second most commonly diagnosed disease in females and the third in males worldwide. Therefore, the finding of new more reliable biomarkers for early diagnosis, for prediction of metastasis, and resistance to conventional therapies is an important challenge in overcoming the disease. The current review presents circular RNAs (circRNAs) with their unique features as potential prognostic and diagnostic biomarkers in CRC. The review highlights the mechanism of action and the role of circRNAs with oncogenic functions in the CRC as well as the association between their expression and clinicopathological characteristics of CRC patients. The comprehension of the role of oncogenic circRNAs in CRC pathogenesis is growing rapidly and the next step is using them as suitable new drug targets in the personalized treatment of CRC patients.

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