Article
Microbiology
Antonio Luis de O. A. Petersen, Benjamin Cull, Beatriz R. S. Dias, Luana C. Palma, Yasmin da S. Luz, Juliana P. B. de Menezes, Jeremy C. Mottram, Patricia S. T. Veras
Summary: The Hsp90 inhibitor 17-AAG was shown to cause abnormal activation of the autophagic pathway, leading to the formation of immature autophagosomes and subsequent parasite death. This study provides evidence of the role of autophagy in 17-AAG-induced cell death, supporting the potential of Hsp90 as a drug target for parasitic diseases.
Article
Microbiology
Yujia Zhao, Dai Xiao, Luwen Zhang, Daili Song, Rui Chen, Shiqian Li, Yijie Liao, Yimin Wen, Weizhe Liu, Enbo Yu, Yiping Wen, Rui Wu, Qin Zhao, Senyan Du, Xintian Wen, Sanjie Cao, Xiaobo Huang
Summary: This study evaluated three HSP90 inhibitors for their effects on Porcine deltacoronavirus (PDCoV) infection and found that 17-AAG and VER-82576 showed inhibitory effects on PDCoV replication, possibly by targeting the host cell factor HSP90AB1.
VETERINARY MICROBIOLOGY
(2022)
Review
Biochemistry & Molecular Biology
Giusi Alberti, Giuseppe Vergilio, Letizia Paladino, Rosario Barone, Francesco Cappello, Everly Conway de Macario, Alberto J. L. Macario, Fabio Bucchieri, Francesca Rappa
Summary: Breast cancer is a major public health problem, and the role of the chaperone system in its development and treatment is still poorly understood. This article discusses the pro-carcinogenic roles of four chaperones, Hsp27, Hsp60, Hsp70, and Hsp90, in breast cancer and their potential for anti-cancer therapies. The article also briefly explores the potential of extracellular vesicles in breast cancer diagnosis and management. Overall, understanding the chaperone system can provide new insights into the mechanisms of breast cancer and the development of targeted treatments.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Oncology
Reine Hanna, Jad Abdallah, Tamara Abou-Antoun
Summary: The study demonstrated that HSP90 inhibition can effectively suppress cellular proliferation, viability, and migration/invasion, while promoting apoptosis in neuroblastoma cells. The treatment also attenuated the stem-cell self-renewal potential in MYCN-amplified cells, showing a novel therapeutic mechanism to enhance therapeutic sensitivity.
FRONTIERS IN ONCOLOGY
(2021)
Review
Biochemistry & Molecular Biology
Bereket Birbo, Elechi E. Madu, Chikezie O. Madu, Aayush Jain, Yi Lu
Summary: HSP90 is a crucial chaperone protein with different isoforms present in various cell compartments. Elevated levels of HSP90 have been linked to cancer, making it a target for cancer drugs. Differences in conformation between normal HSP90 and tumor phenotype HSP90 have led to the development of HSP90 inhibitors as a potential cancer treatment.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Microbiology
Luyao Liu, Xueying Zhang, Shruti Kayastha, Lihua Tan, Heng Zhang, Jingwen Tan, Linyun Li, Jinghua Mao, Yi Sun
Summary: Invasive candidiasis is a leading cause of mortality in medical environments, and the resistance of Candida species to antifungal drugs is increasing. This study demonstrates that Hsp90 inhibitors have the potential to improve fungal resistance to antifungal drugs. The results provide new insights into the development of drugs against drug-resistant Candida species.
FRONTIERS IN MICROBIOLOGY
(2022)
Article
Cell Biology
Mieun Lee-Theilen, Julia R. Hadhoud, Giulietta Volante, Delaine D. Fadini, Julia Eichhorn, Udo Rolle, Henning C. Fiegel
Summary: This study successfully identified CSCs of hepatoblastoma using CD34, CD90, OV-6, and csVimentin as markers. These CSCs exhibit characteristics of drug resistance and tumor relapse promotion.
Article
Biochemistry & Molecular Biology
Iga Dalidowska, Olga Gazi, Dorota Sulejczak, Maciej Przybylski, Pawel Bieganowski
Summary: The research showed that the Hsp90 inhibitor 17-AAG effectively reduces the replication rate of human adenovirus 5 and inhibits its transcription of early and late genes, viral DNA replication, and protein expression. Additionally, 17-AAG decreases the level of newly synthesized E1A protein, potentially explaining its anti-adenoviral activity by reducing E1A levels.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Cell Biology
Xiude Ren, Tao Li, Wei Zhang, Xuejun Yang
Summary: Heat-shock protein 90 (HSP90) is an important molecule chaperone associated with tumorigenesis and malignancy. It plays a role in the malignant behaviors of cancer cells, but currently there are no effective single-agent treatments. Combining HSP90 inhibitors with other anticancer therapies may be a better strategy.
Article
Chemistry, Medicinal
Sanket J. Mishra, Weiya Liu, Kristin Beebe, Monimoy Banerjee, Caitlin N. Kent, Vitumbiko Munthali, John Koren, John A. Taylor, Leonard M. Neckers, Jeffrey Holzbeierlein, Brian S. J. Blagg
Summary: Hsp90 proteins play a crucial role in cancer progression, and inhibiting their activity may be beneficial for cancer treatment. Current Hsp90 inhibitors target all isoforms, potentially leading to adverse effects. Utilizing Hsp90 beta-selective inhibitors as a new approach for cancer therapy holds promise in reducing side effects.
JOURNAL OF MEDICINAL CHEMISTRY
(2021)
Review
Oncology
Christian Tibor Josef Magyar, Yogesh K. Vashist, Deborah Stroka, Corina Kim-Fuchs, Martin D. Berger, Vanessa M. Banz
Summary: HSP90 inhibitors may have potential efficacy in the treatment of gastrointestinal cancers, but more research is needed to determine which patient subgroups and at what time point these inhibitors may be beneficial.
JOURNAL OF CANCER RESEARCH AND CLINICAL ONCOLOGY
(2023)
Article
Pharmacology & Pharmacy
Tetsuro Marunouchi, Takumi Ito, Sumika Onda, Lina Kyo, Kirara Takahashi, Manami Uchida, Emi Yano, Kouichi Tanonaka
Summary: The study shows that the Hsp90 inhibitor 17-AAG can improve cardiac function and reduce cardiac hypertrophy and fibrosis after myocardial infarction. Activation of the RIP1/RIP3/MLKL pathway is a common event in the development of chronic heart failure.
JOURNAL OF PHARMACOLOGICAL SCIENCES
(2021)
Review
Pharmacology & Pharmacy
Zahra Alimardan, Maryam Abbasi, Farshid Hasanzadeh, Mahmud Aghaei, Ghadamali Khodarahmi, Khosrow Kashfi
Summary: Heat shock proteins (Hsps), including Hsp70, Hsp90, and small Hsps, and the transcription factor FoxM1, have important roles in carcinogenesis. Hsp70 functions in cancer initiation and protein folding, and is overexpressed in human cancers. It also interacts with cochaperones and regulates the FoxM1 signaling pathway. FoxM1 is overexpressed in most human cancers and is involved in various cancer-related processes. This review covers the structure, function, and inhibitors of Hsp70, Hsp90, and FoxM1.
BIOCHEMICAL PHARMACOLOGY
(2023)
Review
Cell Biology
Kruthika Iyer, Kailash Chand, Alapani Mitra, Jay Trivedi, Debashis Mitra
Summary: Heat shock proteins (HSPs) are cellular proteins induced during stress conditions, acting as chaperones that regulate protein folding and determine the fate of mis-folded/unfolded proteins. In viral infections, certain HSP isoforms play significant roles with varying pro-viral or anti-viral activities.
CELL STRESS & CHAPERONES
(2021)
Article
Biochemistry & Molecular Biology
Xin Tang, Cheng Chang, Daniel Mosallaei, David T. Woodley, Axel H. Schonthal, Mei Chen, Wei Li
Summary: The expression of Hsp90 varies dramatically among different types of noncancer cells and organs, which affects the sensitivity and resistance to Hsp90 ATP-binding inhibitors. Even in the presence of full Hsp90 alpha, a minimum amount of Hsp90 beta is still required for cell growth and survival. These findings could complicate biomarker selection, toxicity readout, and clinical efficacy of Hsp90-ATP-binding inhibitors in cancer clinical trials.
MOLECULAR AND CELLULAR BIOLOGY
(2022)