Effect of geldanamycin on the expression of the matrix molecules and angiogenetic factors in a gastric cancer cell line

Gürpınar, Tuğba; Kosova, Funda; Kurt, Feyzan Özdal; Cambaz, S U; Yücel, A T; Umur, Nurcan; Tuğlu, Mehmet İbrahim

doi:10.1080/10520295.2020.1772507

Cited by 3 publications

(1 citation statement)

References 38 publications

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“…Studies have also found that TSP1 can inhibit MMP-9, thereby controlling tumor angiogenesis (18). Gürpınar et al (19) demonstrated that TSP2 gene expression in colorectal cancer cells can reduce the expression of MMP-9 and MMP-2. Huang et al (20) analyzed the correlation between TSP, hematoma, and peripheral edema in patients with cerebral hemorrhage.…”

Section: Discussionmentioning

confidence: 99%

Correlation analysis between TSP2, MMP-9 and perihematoma edema, as well as the short-term prognosis of patients with hypertensive intracerebral hemorrhage

Cao¹,

Fa-jian²,

Liu³

et al. 2021

Ann Palliat Med

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Section: Discussionmentioning

confidence: 99%

Correlation analysis between TSP2, MMP-9 and perihematoma edema, as well as the short-term prognosis of patients with hypertensive intracerebral hemorrhage

Cao¹,

Fa-jian²,

Liu³

et al. 2021

Ann Palliat Med

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Macrolactam Synthesis via Ring-Closing Alkene–Alkene Cross-Coupling Reactions

2020

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Reported herein is a practical method for macrolactam synthesis via a Rh(III)-catalyzed ring closing alkene–alkene cross-coupling reaction. The reaction proceeded via a Rh-catalyzed alkenyl sp2 C–H activation process, which allows access to macrocyclic molecules of different ring sizes. Macrolactams containing a conjugated diene framework could be easily prepared in high chemoselectivities and Z,E stereoselectivities.

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Targeting HSP90 as a Novel Therapy for Cancer: Mechanistic Insights and Translational Relevance

Zhang

Liu

et al. 2022

Cells

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Heat shock protein (HSP90), a highly conserved molecular chaperon, is indispensable for the maturation of newly synthesized poly-peptides and provides a shelter for the turnover of misfolded or denatured proteins. In cancers, the client proteins of HSP90 extend to the entire process of oncogenesis that are associated with all hallmarks of cancer. Accumulating evidence has demonstrated that the client proteins are guided for proteasomal degradation when their complexes with HSP90 are disrupted. Accordingly, HSP90 and its co-chaperones have emerged as viable targets for the development of cancer therapeutics. Consequently, a number of natural products and their analogs targeting HSP90 have been identified. They have shown a strong inhibitory effect on various cancer types through different mechanisms. The inhibitors act by directly binding to either HSP90 or its co-chaperones/client proteins. Several HSP90 inhibitors—such as geldanamycin and its derivatives, gamitrinib and shepherdin—are under clinical evaluation with promising results. Here, we review the subcellular localization of HSP90, its corresponding mechanism of action in the malignant phenotypes, and the recent progress on the development of HSP90 inhibitors. Hopefully, this comprehensive review will shed light on the translational potential of HSP90 inhibitors as novel cancer therapeutics.

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Effect of geldanamycin on the expression of the matrix molecules and angiogenetic factors in a gastric cancer cell line

Cited by 3 publications

References 38 publications

Correlation analysis between TSP2, MMP-9 and perihematoma edema, as well as the short-term prognosis of patients with hypertensive intracerebral hemorrhage

Correlation analysis between TSP2, MMP-9 and perihematoma edema, as well as the short-term prognosis of patients with hypertensive intracerebral hemorrhage

Macrolactam Synthesis via Ring-Closing Alkene–Alkene Cross-Coupling Reactions

Targeting HSP90 as a Novel Therapy for Cancer: Mechanistic Insights and Translational Relevance

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