Small heat shock proteins in cancer therapy and prognosis

Small heat shock proteins (sHSPs) are ubiquitous ATP-independent chaperones that play essential roles in response to cellular stresses and protein homeostasis. Investigations of sHSPs reveal that sHSPs are ubiquitously expressed in numerous types of tumors, and their expression is closely associated with cancer progression. sHSPs have been suggested to control a diverse range of cancer functions, including tumorigenesis, cell growth, apoptosis, metastasis, and chemoresistance, as well as regulation of cancer stem cell properties. Recent advances in the field indicate that some sHSPs have been validated as a powerful target in cancer therapy. In this review, we present and highlight current understanding, recent progress, and future challenges of sHSPs in cancer development and therapy.

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Faculty Opinions recommendation of Selective Cu2+ binding, redox silencing, and cytoprotective effects of the small heat shock proteins alphaA- and alphaB-crystallin.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1122926.580027 ◽

2008 ◽

Author(s):

George Perry

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Small Heat Shock Proteins ◽

Shock Proteins

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

Protein and Peptide Letters ◽

10.2174/0929866521666131224094408 ◽

2014 ◽

Vol 21 (6) ◽

pp. 564-571 ◽

Cited By ~ 4

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

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

Current Chemical Biology ◽

10.2174/2212796809666151022202506 ◽

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

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Small Heat Shock Proteins and Protection Against Ischemic Injury in Cardiac Myocytes

Circulation ◽

10.1161/01.cir.96.12.4343 ◽

1997 ◽

Vol 96 (12) ◽

pp. 4343-4348 ◽

Cited By ~ 237

Author(s):

Jody L. Martin ◽

Ruben Mestril ◽

Randa Hilal-Dandan ◽

Laurence L. Brunton ◽

Wolfgang H. Dillmann

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Cardiac Myocytes ◽

Ischemic Injury ◽

Small Heat Shock Proteins ◽

Shock Proteins

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Translation of Some Maize Small Heat Shock Proteins Is Initiated From Internal In-Frame AUGs

Genetics ◽

10.1093/genetics/148.1.471 ◽

1998 ◽

Vol 148 (1) ◽

pp. 471-477

Author(s):

J Roger H Frappier ◽

David B Walden ◽

Burr G Atkinson

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Single Gene ◽

Small Heat Shock Proteins ◽

Shock Proteins

Abstract Etiolated maize radicles (inbred Oh43) subjected to a brief heat shock synthesize a family of small heat shock proteins (≃18 kD) that is composed of at least 12 members. We previously described the cDNA-derived sequence of three maize shsp mRNAs (cMHSP18-1, cMHSP18-3, and cMHSP18-9). In this report, we demonstrate that the mRNA transcribed in vitro from one of these cDNAs (cMHSP 18-9) is responsible for the synthesis of three members of the shsp family, and we suggest that cMHSP18-3 may be responsible for the synthesis of three additional members and cMHSP18-1 for the synthesis of two other members of this family. The fact that these genes do not contain introns, coupled with the observations reported herein, suggest that maize may have established another method of using a single gene to produce a number of different proteins.

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