scholarly journals Epigenetic Alterations of Heat Shock Proteins (HSPs) in Cancer

2019 ◽  
Vol 20 (19) ◽  
pp. 4758 ◽  
Author(s):  
Hyun Ban ◽  
Tae-Su Han ◽  
Keun Hur ◽  
Hyun-Soo Cho
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Cytotoxic Agents ◽  
Epigenetic Alterations ◽  
Regulatory Processes ◽  
Physiological Processes ◽  
Epigenetic Modifiers ◽  
Epigenetic Machinery ◽  
Shock Proteins

Heat shock proteins (HSPs) are associated with various physiological processes (protein refolding and degradation) involved in the responses to cellular stress, such as cytotoxic agents, high temperature, and hypoxia. HSPs are overexpressed in cancer cells and play roles in their apoptosis, invasion, proliferation, angiogenesis, and metastasis. The regulation or translational modification of HSPs is recognized as a therapeutic target for the development of anticancer drugs. Among the regulatory processes associated with HSP expression, the epigenetic machinery (miRNAs, histone modification, and DNA methylation) has key functions in cancer. Moreover, various epigenetic modifiers of HSP expression have also been reported as therapeutic targets and diagnostic markers of cancer. Thus, in this review, we describe the epigenetic alterations of HSP expression in cancer cells and suggest that HSPs be clinically applied as diagnostic and therapeutic markers in cancer therapy via controlled epigenetic modifiers.

scholarly journals Hsps responsible for apoptosis induction failure in cervical cancer cells upon osthole and tamoxifen treatment

2019 ◽  
Vol 73 ◽  
pp. 563-571
Author(s):  
Joanna Jakubowicz-Gil ◽  
Roman Paduch ◽  
Krystyna Skalicka-Woźniak ◽  
Joanna Sumorek-Wiadro ◽  
Adrian Zając ◽  
...  
Keyword(s):  
Cervical Cancer ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Cell Lines ◽  
Tamoxifen Treatment ◽  
Hpv 16 ◽  
Cervical Cancer Cells ◽  
Shock Proteins ◽  
Human Cervical Cancer

Aim: The aim of the present study was to investigate the efficacy of osthole (7-metoxy-8-isopenthenocoumarin) alone and combined with tamoxifen (TAM) in the elimination of human cervical cancer cells via programmed death. The involvement of heat shock proteins, i.e. well-known molecular chaperones, will be investigated. Material/Methods: Three human cervical cancer cell lines, infected with human papilloma virus (HPV), i.e. HeLa (HPV 18), SiHa (HPV 16), and CaSki (HPV 16 and 18), were used in the experiments. After osthole and TAM treatment, cells stained with fluorochromes were analyzed microscopically according to apoptotic, autophagic, and necrotic morphology. Hsp27, Hsp72, and Hsp90 levels were analyzed by immunoblotting. Transfection with specific siRNA was used for blocking of Hsp expression. Results: In the HeLa, CaSki, and SiHa cell lines, osthole and TAM applied alone had no significant effect on cell death induction. This was correlated with an overexpression of heat shock proteins 27, 72, and 90. In the case of a combination of both drugs, the level of apoptosis was elevated only in SiHa cells. Preincubation with osthole followed by TAM addition as well as simultaneous incubation with both drugs was the most effective. This was correlated with the inhibition of Hsp27, Hsp72, and Hsp90 expression. Blocking of Hsp expression with specific siRNA increased the sensitivity of the studied cell lines to the induction of apoptosis, but not to autophagy or necrosis. Conclusions: Our results indicated that the elimination of heat shock proteins from cervical cancer cells sensitized them to initiation of apoptosis after osthole and tamoxifen treatment.

Heat Shock Proteins and Cardiovascular Pathophysiology

2001 ◽  
Vol 81 (4) ◽  
pp. 1461-1497 ◽  
Author(s):  
Luc H. E. H. Snoeckx ◽  
Richard N. Cornelussen ◽  
Frans A. Van Nieuwenhoven ◽  
Robert S. Reneman ◽  
Ger J. Van der Vusse
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cardiovascular System ◽  
Defense Mechanism ◽  
Physiological Role ◽  
Eukaryotic Cell ◽  
Cellular Protein ◽  
Cell Organelles ◽  
Physiological Processes ◽  
Shock Proteins

In the eukaryotic cell an intrinsic mechanism is present providing the ability to defend itself against external stressors from various sources. This defense mechanism probably evolved from the presence of a group of chaperones, playing a crucial role in governing proper protein assembly, folding, and transport. Upregulation of the synthesis of a number of these proteins upon environmental stress establishes a unique defense system to maintain cellular protein homeostasis and to ensure survival of the cell. In the cardiovascular system this enhanced protein synthesis leads to a transient but powerful increase in tolerance to such endangering situations as ischemia, hypoxia, oxidative injury, and endotoxemia. These so-called heat shock proteins interfere with several physiological processes within several cell organelles and, for proper functioning, are translocated to different compartments following stress-induced synthesis. In this review we describe the physiological role of heat shock proteins and discuss their protective potential against various stress agents in the cardiovascular system.

scholarly journals Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes

2019 ◽  
Vol 24 (6) ◽  
pp. 1027-1044 ◽  
Author(s):  
Dorota Scieglinska ◽  
Zdzisław Krawczyk ◽  
Damian Robert Sojka ◽  
Agnieszka Gogler-Pigłowska
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Current Knowledge ◽  
Skin Layer ◽  
Keratinocyte Differentiation ◽  
Epidermal Keratinocytes ◽  
Physiological Processes ◽  
Open Questions ◽  
Stratified Squamous Epithelium ◽  
Shock Proteins

AbstractHeat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes.

Calcium Phosphate Powder for Cancer Vaccination

2007 ◽  
Vol 361-363 ◽  
pp. 1207-1210 ◽  
Author(s):  
Patrick Frayssinet ◽  
Daniel Ciocca ◽  
Nicole Rouquet
Keyword(s):  
T Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Cancer Tissue ◽  
Phosphate Powder ◽  
Cancer Vaccination ◽  
Shock Proteins ◽  
Antigen Presenting ◽  
Proteins And Peptides

Cancer cells synthesize abnormal proteins and peptides which are associated to heat shock proteins being overproduced by these cells due to the stress induced by the particular biology of cancer tissue. We have purified on hydroxylapatite powder heat shock proteins using the HAparticles as purification bed, vectors for the proteins and vaccination adjuvant. The powder make possible that the purified HSPs and their associated peptides are transfected to the antigen presenting cells and presented to the T cells for the destruction of the cancer cells bearing the antigens.

scholarly journals Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates

2021 ◽  
Vol 8 ◽  
Author(s):  
Bruno Fauvet ◽  
Andrija Finka ◽  
Marie-Pierre Castanié-Cornet ◽  
Anne-Marie Cirinesi ◽  
Pierre Genevaux ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Wild Type ◽  
Triple Mutant ◽  
Respiratory Enzymes ◽  
Physiological Processes ◽  
Knockout Mutants ◽  
Shock Proteins ◽  
Control Protein

In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration with Hsp70 (DnaK) remains poorly characterized. To uncover physiological processes that depend on HtpG and DnaK, we performed comparative quantitative proteomic analyses of insoluble and total protein fractions from unstressed wild-type (WT) Escherichia coli and from knockout mutants ΔdnaKdnaJ (ΔKJ), ΔhtpG (ΔG), and ΔdnaKdnaJΔhtpG (ΔKJG). Whereas the ΔG mutant showed no detectable proteomic differences with wild-type, ΔKJ expressed more chaperones, proteases and ribosomes and expressed dramatically less metabolic and respiratory enzymes. Unexpectedly, we found that the triple mutant ΔKJG showed higher levels of metabolic and respiratory enzymes than ΔKJ, suggesting that bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70–Hsp40 substrates. Further in vivo experiments suggest that such Hsp90-mediated degradation possibly occurs through the HslUV protease.

Targeting Heat Shock Proteins on Cancer Cells:  Selection, Characterization, and Cell-Penetrating Properties of a Peptidic GRP78 Ligand†

Biochemistry ◽  
2006 ◽  
Vol 45 (31) ◽  
pp. 9434-9444 ◽  
Author(s):  
Youngsoo Kim ◽  
Antonietta M. Lillo ◽  
Sebastian C. J. Steiniger ◽  
Ying Liu ◽  
Carlo Ballatore ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Cell Penetrating ◽  
Shock Proteins

The Role of Heat Shock Proteins in Cisplatin Resistance

2019 ◽  
Vol 18 (15) ◽  
pp. 2093-2109 ◽  
Author(s):  
Zdzisław Krawczyk ◽  
Agnieszka Gogler-Pigłowska ◽  
Damian R. Sojka ◽  
Dorota Scieglinska
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Relevant Information ◽  
Multiple Observations ◽  
Wide Range ◽  
Cellular Context ◽  
Universal Relationship ◽  
Shock Proteins

Background: Cisplatin (CDDP), a small molecule platinum-based compound, is an effective anticancer drug used against a wide range of human neoplasms. Long-term clinical use of CDDP is however limited due to the development of drug resistance and the possible incidence of serious side effects including nephrotoxicity and ototoxicity. The mechanisms underlying resistance of cells to CDDP are complex, and among them, the cytoprotective involvement of proteins referred to as Heat Shock Proteins (HSP) seems potentially important. Methods: We searched various electronic databases including PubMed and selected the reports concerning the contribution of HSPs to CDDP resistance of cancer cells and to minimize the CDDP-induced nephrotoxicity and ototoxicity. Results: This critical review of data collected so far summarizes the results on the major HSPs: HSP27/HSPB1, HSP70/HSPA1, HSP90/HSPC and GRP78/HSPA5, because only these have been the subject of the most intense research in the matter discussed here. We also provide relevant information concerning some other HSPs, namely HSPA9/mortalin, HSPA2, HSP110 and DNAJ. A possible role of HSPs in counteracting CDDP-induced neprho- and ototoxicity is mentioned. Conclusions: This review shows that no universal relationship between the levels of expression of HSPs and sensitivity of cancer cells to CDDP can be confirmed. Multiple observations indicate however that such correlation can rather manifest as a molecular or cellular context-dependent phenomenon. Thus, HSPs can be viewed as an important component of the multifactorial, complex response of cancer cells to CDDP. However, to strengthen such a conviction, more extensive studies are needed.

Sign in / Sign up

Export Citation Format

Share Document