Stresgenin B, an Inhibitor of Heat-induced Heat Shock Protein Gene Expression, Produced by Streptomyces sp. A-9.

Akagawa, Hisayoshi; Takano, Yukie; Ishii, Ayako; Mizuno, Satoshi; Izui, Reiko; Sameshima, Tomohiro; Kawamura, Naoto; Dobashi, Kazuyuki; Yoshioka, Takeo

doi:10.7164/antibiotics.52.960

Cited by 26 publications

(21 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The natural product Stresgenin B has also been reported to inhibit induction of HSPs, but its mode of action is still unknown [114]. Quercetin increases the sensitivity of drug-resistant cancer cells to anti-cancer agents [115], and sensitizes cancer cells to hyperthermia, cisplatin [116] and tiazofurin [117].…”

Section: The Inhibition Of Hsfs In Cancer Therapymentioning

confidence: 99%

Implication of Heat Shock Factors in Tumorigenesis: Therapeutical Potential

Thonel

Mezger

Garrido

2011

Cancers

View full text Add to dashboard Cite

Heat Shock Factors (HSF) form a family of transcription factors (four in mammals) which were named according to the discovery of their activation by a heat shock. HSFs trigger the expression of genes encoding Heat Shock Proteins (HSPs) that function as molecular chaperones, contributing to establish a cytoprotective state to various proteotoxic stresses and in pathological conditions. Increasing evidence indicates that this ancient transcriptional protective program acts genome-widely and performs unexpected functions in the absence of experimentally defined stress. Indeed, HSFs are able to re-shape cellular pathways controlling longevity, growth, metabolism and development. The most well studied HSF, HSF1, has been found at elevated levels in tumors with high metastatic potential and is associated with poor prognosis. This is partly explained by the above-mentioned cytoprotective (HSP-dependent) function that may enable cancer cells to adapt to the initial oncogenic stress and to support malignant transformation. Nevertheless, HSF1 operates as major multifaceted enhancers of tumorigenesis through, not only the induction of classical heat shock genes, but also of “non-classical” targets. Indeed, in cancer cells, HSF1 regulates genes involved in core cellular functions including proliferation, survival, migration, protein synthesis, signal transduction, and glucose metabolism, making HSF1 a very attractive target in cancer therapy. In this review, we describe the different physiological roles of HSFs as well as the recent discoveries in term of non-cogenic potential of these HSFs, more specifically associated to the activation of “non-classical” HSF target genes. We also present an update on the compounds with potent HSF1-modulating activity of potential interest as anti-cancer therapeutic agents.

show abstract

Section: The Inhibition Of Hsfs In Cancer Therapymentioning

confidence: 99%

Implication of Heat Shock Factors in Tumorigenesis: Therapeutical Potential

Thonel

Mezger

Garrido

2011

Cancers

View full text Add to dashboard Cite

show abstract

“…The first report was that Streptomyces spp. produce stressgenin, which inhibits stress protein transcription in both bacteria and mammalian cells (1). More recently, Streptococcus hawaiiensis has been found to produce acyldepsipeptides, which have activity against streptococci and staphylococci both in vitro and in vivo.…”

Section: Bacterial Molecular Chaperones As Antibacterial Targetsmentioning

confidence: 99%

Stress Wars: the Direct Role of Host and Bacterial Molecular Chaperones in Bacterial Infection

2006

View full text Add to dashboard Cite

“…AS-9 [97]. It is almost 5 times as potent as the flavonoid quercetin in the suppression of heat shock protein synthesis from a gene under the control of the Hsp70B promoter.…”

Section: Stresgenin Bmentioning

confidence: 99%

Heat-Shock Protein 90: Potential Involvement in the Pathogenesis of Malignancy and Pharmacological Intervention

Ochel

Gademann

2002

Oncol Res Treat

View full text Add to dashboard Cite

Heat-shock protein 90 (Hsp90) is an essential, cytosolic protein. Its overexpression in a wide variety of malignant tumors makes it a candidate target for pharmacological intervention. The association with Hsp90 stabilizes key regulatory proteins like Fak, Bcr-Abl, ErbB2, mutant p53 and Raf-1. The disruption of these heterocomplexes by Hsp90 inhibitors causes the rapid degradation of Hsp90-client proteins by the proteasome. Benzoquinone ansamycins were the first group of compounds for which interference with Hsp90 function was shown to be the major mechanism of action. They are in the early phase of clinical development. Radicicol and its derivatives are functional analogues of benzoquinone ansamycins without structural similarity. Flavonoids and stresgenin B share the ability to suppress heat-shock protein synthesis. Recently, it became apparent that coumarin antibiotics, cisplatin and paclitaxel also bind to Hsp90. The clinical value of the newly characterized agents with activity towards Hsp90 remains to be determined.

show abstract

Stresgenin B, an Inhibitor of Heat-induced Heat Shock Protein Gene Expression, Produced by Streptomyces sp. A-9.

Cited by 26 publications

References 22 publications

Implication of Heat Shock Factors in Tumorigenesis: Therapeutical Potential

Implication of Heat Shock Factors in Tumorigenesis: Therapeutical Potential

Stress Wars: the Direct Role of Host and Bacterial Molecular Chaperones in Bacterial Infection

Heat-Shock Protein 90: Potential Involvement in the Pathogenesis of Malignancy and Pharmacological Intervention

Contact Info

Product

Resources

About