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Journal articles on the topic 'Geldanamycin'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 April 2022

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1

Martín, Juan F., Angelina Ramos, and Paloma Liras. "Regulation of Geldanamycin Biosynthesis by Cluster-Situated Transcription Factors and the Master Regulator PhoP." Antibiotics 8, no. 3 (June 30, 2019): 87. http://dx.doi.org/10.3390/antibiotics8030087.

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Geldanamycin and the closely related herbimycins A, B, and C are benzoquinone-type ansamycins with antitumoral activity. They are produced by Streptomyces hygroscopicus var. geldanus, Streptomyces lydicus and Streptomyces autolyticus among other Streptomyces strains. Geldanamycins interact with the Hsp-90 chaperone, a protein that has a key role in tumorigenesis of human cells. Geldanamycin is a polyketide antibiotic and the polyketide synthase contain seven modules organized in three geldanamycin synthases genes named gdmAI, gdmAII, and gdmAIII. The loading domain of GdmI activates AHBA, and also related hydroxybenzoic acid derivatives, forming geldanamycin analogues. Three regulatory genes, gdmRI, gdmRII, and gdmRIII were found associated with the geldanamycin gene cluster in S. hygroscopicus strains. GdmRI and GdmRII are LAL-type (large ATP binding regulators of the LuxR family) transcriptional regulators, while GdmRIII belongs to the TetR-family. All three are positive regulators of geldanamycin biosynthesis and are strictly required for expression of the geldanamycin polyketide synthases. In S. autolyticus the gdmRIII regulates geldanamycin biosynthesis and also expression of genes in the elaiophylin gene cluster, an unrelated macrodiolide antibiotic. The biosynthesis of geldanamycin is very sensitive to the inorganic phosphate concentration in the medium. This regulation is exerted through the two components system PhoR-PhoP. The phoRP genes of S. hygroscopicus are linked to phoU encoding a transcriptional modulator. The phoP gene was deleted in S. hygroscopicus var geldanus and the mutant was unable to grow in SPG medium unless supplemented with 5 mM phosphate. Also, the S. hygroscopicus pstS gene involved in the high affinity phosphate transport was cloned, and PhoP binding sequences (PHO boxes), were found upstream of phoU, phoRP, and pstS; the phoRP-phoU sequences were confirmed by EMSA and nuclease footprinting protection assays. The PhoP binding sequence consists of 11 nucleotide direct repeat units that are similar to those found in S. coelicolor Streptomyces avermitilis and other Streptomyces species. The available genetic information provides interesting tools for modification of the biosynthetic and regulatory mechanisms in order to increase geldanamycin production and to obtain new geldanamycin analogues with better antitumor properties.

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2

Clevenger, Randell C., Joseph M. Raibel, Angela M. Peck, and Brian S. J. Blagg. "Biotinylated Geldanamycin." Journal of Organic Chemistry 69, no. 13 (June 2004): 4375–80. http://dx.doi.org/10.1021/jo049848m.

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3

SAUSVILLE, E. A. "Geldanamycin Analogs." Journal of Chemotherapy 16, sup4 (November 2004): 68–69. http://dx.doi.org/10.1179/joc.2004.16.supplement-1.68.

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4

Dhayapulay, Akhila, and Mathumai Kanapathipillai. "Exosomes Based Geldanamycin Delivery to Cancer Cells with Increased Therapeutic Efficacy." Journal of Biomedical Nanotechnology 15, no. 11 (November 1, 2019): 2202–8. http://dx.doi.org/10.1166/jbn.2019.2844.

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HSP90 has been shown to promote oncogenic functions and cell proliferation during tumor progression. Geldanamycin is a potent inhibitor of HSP90, however therapeutic effects are often hampered due to its extreme hydrophobicity and systemic toxicity. Hence targeted delivery strategies are needed to overcome these limitations and to improve the efficacy of the drug. Here we utilize a novel geldanamycin delivery approach by utilizing exosomes. For the study, exosomes were extracted from cancer cells, loaded with geldanamycin, and the therapeutic effects were tested in cancer cells. Results show that cancer cells derived exosomes exhibit specificity to cancer cells. Further exosomes loaded geldanamycin show several fold increase in efficacy compared to free geldanamycin. Findings indicate exosomal formulations could be used for extremely hydrophobic HSP90 inhibitor geldanamycin delivery for inhibiting cancer cell proliferation.

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5

Kiang, Juliann G., Phillip D. Bowman, Xinyue Lu, Yansong Li, Brian W. Wu, Horace H. Loh, K. T. Tsen, and George C. Tsokos. "Geldanamycin inhibits hemorrhage-induced increases in caspase-3 activity: role of inducible nitric oxide synthase." Journal of Applied Physiology 103, no. 3 (September 2007): 1045–55. http://dx.doi.org/10.1152/japplphysiol.00100.2007.

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Hemorrhage has been shown to increase inducible nitric oxide synthase (iNOS) and deplete ATP levels in tissues and geldanamycin limits both processes. Moreover, it is evident that inhibition of iNOS reduces caspase-3 and increases survival. Thus we sought to identify the molecular events responsible for the beneficial effect of geldanamycin. Hemorrhage in mice significantly increased caspase-3 activity and protein while treatment with geldanamycin significantly limited these increases. Similarly, geldanamycin inhibited increases in proteins forming the apoptosome (a complex of caspase-9, cytochrome c, and Apaf-1). Modulation of the expression of iNOS by iNOS gene transfection or siRNA treatment demonstrated that the level of iNOS correlates with caspase-3 activity. Our data indicate that geldanamycin limits caspase-3 expression and protects from organ injury by suppressing iNOS expression and apoptosome formation. Geldanamycin, therefore, may prove useful as an adjuvant in fluids used to treat patients suffering blood loss.

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6

Mandler, Raya, Hisataka Kobayashi, Ella R. Hinson, Martin W. Brechbiel, and Thomas A. Waldmann. "Herceptin-Geldanamycin Immunoconjugates." Cancer Research 64, no. 4 (February 15, 2004): 1460–67. http://dx.doi.org/10.1158/0008-5472.can-03-2485.

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7

Othman, A. A., and Z. S. Shoheib. "Detrimental effects of geldanamycin on adults and larvae of Trichinella spiralis." Helminthologia 53, no. 2 (June 1, 2016): 126–32. http://dx.doi.org/10.1515/helmin-2016-0003.

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SummaryTrichinellosis is a zoonotic disease affecting mainly the temperate regions. The treatment is a challenge for the physician, and the available therapy is far from ideal. Therefore, this work aimed to evaluate the effect of heat shock protein 90 inhibitor, geldanamycin, on the adult worms and larvae of Trichinella spiralis. This research comprised an in vivo study in which T. spiralis-infected mice were treated by two different doses of geldanamycin, thereafter larval count and pathological changes were determined in the muscles. Meanwhile, the in vitro study investigated the effect of two different concentrations of geldanamycin on adult worms and larvae of T. spiralis via transmission electron microscopy. The in vivo study showed significant reduction of muscle larval counts under the effect of geldanamycin. Moreover, characteristic changes were noted as regards the parasite and the inflammatory response. The in vitro study revealed degenerative changes in the body wall of larvae and adults of T. spiralis under the influence of geldanamycin. In conclusion, heat shock protein 90 inhibitor, geldanamycin, seems to have detrimental effects on the adults and larvae of T. spiralis. It, or one of its derivatives, could be an adjuvant to anthelmintic therapy of trichinellosis, but more studies are warranted to establish its usefulness.

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8

Zhang, Zhi, Yunfeng Li, Rentao Zhang, and Xiaoming Yu. "Total Synthesis of Geldanamycin." Journal of Organic Chemistry 86, no. 21 (October 16, 2021): 15063–75. http://dx.doi.org/10.1021/acs.joc.1c01582.

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9

Vivas-Reyes, Ricardo, Alejando Morales-Bayuelo, Carlos Gueto, Juan C. Drosos, Johana Márquez Lázaro, Rosa Baldiris, Maicol Ahumedo, Catalina Vivas-Gomez, and Dilia Aparicio. "Study of interaction energies between residues of the active site of Hsp90 and geldanamycin analogues using quantum mechanics/molecular mechanics methods." F1000Research 8 (December 2, 2019): 2040. http://dx.doi.org/10.12688/f1000research.20844.1.

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Background: Heat shock protein (Hsp90KDa) is a molecular chaperone involved in the process of cellular oncogenesis, hence its importance as a therapeutic target in clinical trials. Geldanamycin is an inhibitor of Hsp90 chaperone activity, which binds to the ATP binding site in the N-terminal domain of Hsp90. However, geldanamycin has shown hepatotoxic damage in clinical trials; for this reason, its use is not recommended. Taking advantage that geldanamycin binds successfully to Hsp90, many efforts have focused on the search for similar analogues, which have the same or better biological response and reduce the side effects of its predecessor; 17-AAG and 17-DMAG are examples of these analogues. Methods: In order to know the chemical factors influencing the growth or decay of the biological activity of geldanamycin analogues, different computational techniques such as docking, 3DQSAR and quantum similarity were used. Moreover, the study quantified the interaction energy between amino acids residues of active side and geldanamycin analogues, through hybrid methodologies and density functional theory (DFT) indexes. Results: The evaluation of interaction energies showed that the interaction with Lys58 residue is essential for the union of the analogues to the active site of Hsp90, and improves its biological activity. This union is formed through a substituent on C-11 of the geldanamycin macrocycle. A small and attractor group was found as the main steric and electrostatic characteristic that substituents on C11 need in order to interact with Lys 58; behavior was observed with hydroxy and methoxy series of geldanamycin analogues, under study. Conclusion: These outcomes were supported with quantum similarity and reactivity indices calculations using DFT in order to understand the non-covalent stabilization in the active site of these compounds.

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10

Vivas-Reyes, Ricardo, Alejando Morales-Bayuelo, Carlos Gueto, Juan C. Drosos, Johana Márquez Lázaro, Rosa Baldiris, Maicol Ahumedo, Catalina Vivas-Gomez, and Dilia Aparicio. "Study of interaction energies between residues of the active site of Hsp90 and geldanamycin analogues using quantum mechanics/molecular mechanics methods." F1000Research 8 (April 16, 2020): 2040. http://dx.doi.org/10.12688/f1000research.20844.2.

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Background: Heat shock protein (Hsp90KDa) is a molecular chaperone involved in the process of cellular oncogenesis, hence its importance as a therapeutic target. Geldanamycin is an inhibitor of Hsp90 chaperone activity, which binds to the ATP binding site in the N-terminal domain of Hsp90. However, geldanamycin has shown hepatotoxic damage in clinical trials; for this reason, its use is not recommended. Taking advantage that geldanamycin binds successfully to Hsp90, many efforts have focused on the search for similar analogues, which have the same or better biological response and reduce the side effects of its predecessor; 17-AAG and 17-DMAG are examples of these analogues. Methods: In order to know the chemical factors influencing the growth or decay of the biological activity of geldanamycin analogues, different computational techniques such as docking, 3DQSAR and quantum similarity were used. Moreover, the study quantified the interaction energy between amino acids residues of active side and geldanamycin analogues, through hybrid methodology (Autodock-PM6) and DFT indexes. Results: The evaluation of interaction energies showed that the interaction with Lys58 residue is essential for the union of the analogues to the active site of Hsp90, and improves its biological activity. This union is formed through a substituent on C-11 of the geldanamycin macrocycle. A small and attractor group was found as the main steric and electrostatic characteristic that substituents on C11 need in order to interact with Lys 58; behavior was observed with hydroxy and methoxy series of geldanamycin analogues, under study. Conclusion: This study contributes with new hybrid methodology (Autodock-PM6) for the generation of 3DQSAR models, which to consider the interactions between compounds and amino acids residues of Hsp90´s active site in the alignment generation. Additionally, quantum similarity and reactivity indices calculations using DFT were performed to know the non-covalent stabilization in the active site of these compounds.

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11

Mlejnek, Petr, and Petr Dolezel. "N-acetylcysteine prevents the geldanamycin cytotoxicity by forming geldanamycin–N-acetylcysteine adduct." Chemico-Biological Interactions 220 (September 2014): 248–54. http://dx.doi.org/10.1016/j.cbi.2014.06.025.

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12

Marcu, Monica G., Melissa Doyle, Anne Bertolotti, David Ron, Linda Hendershot, and Len Neckers. "Heat Shock Protein 90 Modulates the Unfolded Protein Response by Stabilizing IRE1α." Molecular and Cellular Biology 22, no. 24 (December 15, 2002): 8506–13. http://dx.doi.org/10.1128/mcb.22.24.8506-8513.2002.

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ABSTRACT The molecular chaperone HSP90 regulates stability and function of multiple protein kinases. The HSP90-binding drug geldanamycin interferes with this activity and promotes proteasome-dependent degradation of most HSP90 client proteins. Geldanamycin also binds to GRP94, the HSP90 paralog located in the endoplasmic reticulum (ER). Because two of three ER stress sensors are transmembrane kinases, namely IRE1α and PERK, we investigated whether HSP90 is necessary for the stability and function of these proteins. We found that HSP90 associates with the cytoplasmic domains of both kinases. Both geldanamycin and the HSP90-specific inhibitor, 514, led to the dissociation of HSP90 from the kinases and a concomitant turnover of newly synthesized and existing pools of these proteins, demonstrating that the continued association of HSP90 with the kinases was required to maintain their stability. Further, the previously reported ability of geldanamycin to stimulate ER stress-dependent transcription apparently depends on its interaction with GRP94, not HSP90, since geldanamycin but not 514 led to up-regulation of BiP. However, this effect is eventually superseded by HSP90-dependent destabilization of unfolded protein response signaling. These data establish a role for HSP90 in the cellular transcriptional response to ER stress and demonstrate that chaperone systems on both sides of the ER membrane serve to integrate this signal transduction cascade.

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13

Kang, Shin-Ae, Hyun-Soo Cho, Jong Bok Yoon, In Kwon Chung, and Seung-Taek Lee. "Hsp90 rescues PTK6 from proteasomal degradation in breast cancer cells." Biochemical Journal 447, no. 2 (September 26, 2012): 313–20. http://dx.doi.org/10.1042/bj20120803.

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PTK6 [protein tyrosine kinase 6; also known as Brk (breast tumour kinase)] is a non-receptor tyrosine kinase, closely related to Src, but evolutionarily distinct, that is up-regulated in various cancers, including breast cancer. Hsp90 (heat-shock protein 90) was identified as a PTK6-interacting protein in HEK (human embryonic kidney)-293 cells overexpressing PTK6. Hsp90 interacted with the PTK6 tyrosine kinase catalytic domain, but catalytic activity was not required for the interaction. Geldanamycin, an Hsp90 inhibitor, significantly decreased the PTK6 protein level through proteasome-dependent degradation, but did not affect the level of Src. Geldanamycin treatment also decreased phosphorylation of PTK6 substrates due to reduced amounts of PTK6. Moreover, overexpression of CHIP [C-terminus of Hsc70 (heat-shock cognate 70)-interacting protein], a chaperone-dependent E3 ligase, enhanced proteosomal degradation of PTK6. Geldanamycin increased the interaction of PTK6 with CHIP, but decreased the interaction of PTK6 with Hsp90. We also found that endogenous PTK6 associated with Hsp90 and geldanamycin decreased expression of endogenous PTK6 in breast carcinoma cells. Finally, we report that silencing endogenous CHIP expression in breast carcinoma cells inhibited geldanamycin-induced PTK6 reduction. These results demonstrate that Hsp90 plays an essential role in regulating PTK6 stability and suggest that Hsp90 inhibitors may be useful as therapeutic drugs for PTK6-positive cancers, including breast cancer.

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14

Fike, Candice D., Sandra L. Pfister, James C. Slaughter, Mark R. Kaplowitz, Yongmei Zhang, Heng Zeng, Naila Rashida Frye, and Judy L. Aschner. "Protein complex formation with heat shock protein 90 in chronic hypoxia-induced pulmonary hypertension in newborn piglets." American Journal of Physiology-Heart and Circulatory Physiology 299, no. 4 (October 2010): H1190—H1204. http://dx.doi.org/10.1152/ajpheart.01207.2009.

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Aberrant interactions between heat shock protein (Hsp)90 and its client proteins could contribute to pulmonary hypertension. We tested the hypotheses that 1) the interaction between Hsp90 and its known client protein, endothelial nitric oxide synthase (eNOS), is impaired in pulmonary resistance arteries (PRAs) from piglets with pulmonary hypertension caused by exposure to 3 or 10 days of hypoxia and 2) Hsp90 interacts with the prostanoid pathway proteins prostacyclin synthase (PGIS) and/or thromboxane synthase (TXAS). We also determined whether Hsp90 antagonism with geldanamycin alters the agonist-induced synthesis of prostacyclin and thromboxane or alters PRA responses to these prostaglandin metabolites. Compared with normoxic piglets, less eNOS coimmunoprecipitated with Hsp90 in PRAs from hypoxic piglets. Despite reduced Hsp90-eNOS interactions, dilation to ACh was enhanced in geldanamycin-treated PRAs from hypoxic, but not normoxic, piglets. In PRAs from all groups of piglets, PGIS and TXAS coimmunoprecipitated with Hsp90. Geldanamycin reduced the ACh-induced synthesis of prostacyclin and thromboxane and altered responses to the thromboxane mimetic U-46619 in PRAs from all groups. Although geldanamycin enhanced responses to prostacyclin in PRAs from both groups of hypoxic piglets, geldanamycin had no effect on prostacyclin responses in PRAs from either group of normoxic piglets. Our findings indicate that Hsp90 influences both prostanoid and eNOS signaling in the pulmonary circulation of newborn piglets and that the impact of pharmacological inhibition of Hsp90 on these signaling pathways is altered during exposure to chronic hypoxia.

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15

HE, W., J. LEI, Y. LIU, and Y. WANG. "Regulatory Genes of Geldanamycin Biosynthesis." Chinese Journal of Biotechnology 24, no. 5 (May 2008): 717–22. http://dx.doi.org/10.1016/s1872-2075(08)60036-9.

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16

Kitson, Russell R. A., and Christopher J. Moody. "Synthesis of novel geldanamycin derivatives." Tetrahedron 82 (February 2021): 131927. http://dx.doi.org/10.1016/j.tet.2021.131927.

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17

Peng, Yong, Xiaoqiang Liu, and Daniel R. Schoenberg. "The 90-kDa Heat Shock Protein Stabilizes the Polysomal Ribonuclease 1 mRNA Endonuclease to Degradation by the 26S Proteasome." Molecular Biology of the Cell 19, no. 2 (February 2008): 546–52. http://dx.doi.org/10.1091/mbc.e07-08-0774.

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The polysomal ribonuclease 1 (PMR1) mRNA endonuclease forms a selective complex with its translating substrate mRNAs where it is activated to initiate mRNA decay. Previous work showed tyrosine phosphorylation is required for PMR1 targeting to this polysome-bound complex, and it identified c-Src as the responsible kinase. c-Src phosphorylation occurs in a distinct complex, and the current study shows that 90-kDa heat shock protein (Hsp90) is also recovered with PMR1 and c-Src. Hsp90 binding to PMR1 is inhibited by geldanamycin, and geldanamycin stabilizes substrate mRNA to PMR1-mediated decay. PMR1 is inherently unstable and geldanamycin causes PMR1 to rapidly disappear in a process that is catalyzed by the 26S proteasome. We present a model where Hsp90 interacts transiently to stabilize PMR1 in a manner similar to its interaction with c-Src, thus facilitating the tyrosine phosphorylation and targeting of PMR1 to polysomes.

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18

Vetcher, Leandro, Zong-Qiang Tian, Robert McDaniel, Andreas Rascher, W. Peter Revill, C. Richard Hutchinson, and Zhihao Hu. "Rapid Engineering of the Geldanamycin Biosynthesis Pathway by Red/ET Recombination and Gene Complementation." Applied and Environmental Microbiology 71, no. 4 (April 2005): 1829–35. http://dx.doi.org/10.1128/aem.71.4.1829-1835.2005.

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ABSTRACT Genetic manipulation of antibiotic producers, such as Streptomyces species, is a rational approach to improve the properties of biologically active molecules. However, this can be a slow and sometimes problematic process. Red/ET recombination in an Escherichia coli host has permitted rapid and more versatile engineering of geldanamycin biosynthetic genes in a complementation plasmid, which can then be readily transferred into the Streptomyces host from which the corresponding wild type gene(s) has been removed. With this rapid Red/ET recombination and gene complementation approach, efficient gene disruptions and gene replacements in the geldanamycin biosynthetic gene cluster have been successfully achieved. As an example, we describe here the creation of a ketoreductase 6 null mutation in an E. coli high-copy-number plasmid carrying gdmA2A3 from Streptomyces hygroscopicus NRRL3602 and the subsequent complementation of a gdmA2A3 deletion host with this plasmid to generate a novel geldanamycin analog.

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19

Conde, Renaud, Zachery R. Belak, Manoj Nair, Ruth F. O’Carroll, and Nick Ovsenek. "Modulation of Hsf1 activity by novobiocin and geldanamycin." Biochemistry and Cell Biology 87, no. 6 (December 2009): 845–51. http://dx.doi.org/10.1139/o09-049.

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Since Hsp90 is a known modulator of HSF1 activity, we examined the effects of two pharmacological inhibitors of Hsp90, novobiocin and geldanamycin, on HSF1 DNA-binding activity in the Xenopus oocyte model system. Novobiocin exhibits antiproliferative activity in culture cells and interacts with a C-terminal ATP-binding pocket on Hsp90, inhibiting Hsp90 autophosphorylation. Treatment of oocytes with novobiocin followed by heat shock results in a dose-dependent decrease in HSF1 DNA-binding and transcriptional activity. Immunoprecipitation experiments demonstrate novobiocin does not alter HSF1 activity through dissociation of Hsp90 from either monomeric or trimerized HSF1, suggesting that the effect of novobiocin on HSF1 is mediated through alterations in Hsp90 autophosphorylation. Geldanamycin binds the N-terminal ATPase site of Hsp90 and inhibits chaperone activity. Geldanamycin treatment of oocytes resulted in a dose-dependant increase in stability of active HSF1 trimers during submaximal heat shock and a delay in disassembly of trimers during recovery. The results suggest that Hsp90 chaperone activity is required for disassembly of HSF1 trimers. The data obtained with novobiocin suggests the C-terminal ATP-binding activity of Hsp90 is required for the initial steps of HSF1 trimerization, whereas the effects of geldanamycin suggest N-terminal ATPase and chaperone activities are required for disassembly of activated trimers. These data provide important insight into the molecular mechanisms by which pharmacological inhibitors of Hsp90 affect the heat shock response.

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20

Rascher, Andreas, Zhihao Hu, Greg O. Buchanan, Ralph Reid, and C. Richard Hutchinson. "Insights into the Biosynthesis of the Benzoquinone Ansamycins Geldanamycin and Herbimycin, Obtained by Gene Sequencing and Disruption." Applied and Environmental Microbiology 71, no. 8 (August 2005): 4862–71. http://dx.doi.org/10.1128/aem.71.8.4862-4871.2005.

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ABSTRACT Geldanamycin and the closely related herbimycins A, B, and C were the first benzoquinone ansamycins to be extensively studied for their antitumor properties as small-molecule inhibitors of the Hsp90 protein chaperone complex. These compounds are produced by two different Streptomyces hygroscopicus strains and have the same modular polyketide synthase (PKS)-derived carbon skeleton but different substitution patterns at C-11, C-15, and C-17. To set the stage for structural modification by genetic engineering, we previously identified the gene cluster responsible for geldanamycin biosynthesis. We have now cloned and sequenced a 115-kb segment of the herbimycin biosynthetic gene cluster from S. hygroscopicus AM 3672, including the genes for the PKS and most of the post-PKS tailoring enzymes. The similarities and differences between the gene clusters and biosynthetic pathways for these closely related ansamycins are interpreted with support from the results of gene inactivation experiments. In addition, the organization and functions of genes involved in the biosynthesis of the 3-amino-5-hydroxybenzoic acid (AHBA) starter unit and the post-PKS modifications of progeldanamycin were assessed by inactivating the subclusters of AHBA biosynthetic genes and two oxygenase genes (gdmM and gdmL) that were proposed to be involved in formation of the geldanamycin benzoquinoid system. A resulting novel geldanamycin analog, KOS-1806, was isolated and characterized.

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21

Wu, Cheng-Zhu. "New Geldanamycin Analogs from Streptomyces hygroscopicus." Journal of Microbiology and Biotechnology 22, no. 11 (November 28, 2012): 1478–81. http://dx.doi.org/10.4014/jmb.1206.06026.

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22

Hargreaves, Robert, Cynthia L. David, Luke Whitesell, and Edward B. Skibo. "Design of quinolinedione-Based geldanamycin analogues." Bioorganic & Medicinal Chemistry Letters 13, no. 18 (September 2003): 3075–78. http://dx.doi.org/10.1016/s0960-894x(03)00650-4.

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23

Su, Chih-Hao, Keng-Hsin Lan, Chung-Pin Li, Yee Chao, Han-Chieh Lin, Shou-Dong Lee, and Wei-Ping Lee. "Phosphorylation accelerates geldanamycin-induced Akt degradation." Archives of Biochemistry and Biophysics 536, no. 1 (August 2013): 6–11. http://dx.doi.org/10.1016/j.abb.2013.04.015.

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24

Fukuyo, Yayoi, Clayton R. Hunt, and Nobuo Horikoshi. "Geldanamycin and its anti-cancer activities." Cancer Letters 290, no. 1 (April 2010): 24–35. http://dx.doi.org/10.1016/j.canlet.2009.07.010.

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25

Matsuoka, Erina, Naoki Kato, and Masakazu Hara. "Induction of the heat shock response in Arabidopsis by heat shock protein 70 inhibitor VER-155008." Functional Plant Biology 46, no. 10 (2019): 925. http://dx.doi.org/10.1071/fp18259.

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The heat shock protein 90 (HSP90) inhibitor, geldanamycin, is a chemical inducer of the heat shock response (HSR) in Arabidopsis. Geldanamycin is thought to activate the heat shock signal by dissociating the HSP90-heat shock factor (HSF) complex. Recent studies have indicated that plant HSP70 is also associated with HSF, suggesting that inhibition of HSP70 may induce the HSR. However, no studies have been conducted to test this hypothesis. Here, we found that a specific HSP70 inhibitor VER-155008 activated the promoter of a small HSP gene (At1 g53540, HSP17.6C-CI) of Arabidopsis, which was shown to be activated by geldanamycin and other HSP90 inhibitors. The production of HSP17.6C-CI, HSP70 and HSP90.1 proteins in Arabidopsis was enhanced by the addition of VER-155008. The reduction of chlorophyll contents by heat shock was ameliorated by VER-155008. Chaperone analyses indicated that VER-155008 inhibited the chaperone activities of wheat germ extract and human HSP70/HSP40, respectively. These results suggest that the inhibition of HSP70 by VER-155008 enhanced the heat tolerance of Arabidopsis by inducing the HSR in the plant.

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26

Khurana, Vini G., Kristian Feterik, Margaret J. Springett, Daihiko Eguchi, Vijay Shah, and Zvonimir S. Katusic. "Functional Interdependence and Colocalization of Endothelial Nitric Oxide Synthase and Heat Shock Protein 90 in Cerebral Arteries." Journal of Cerebral Blood Flow & Metabolism 20, no. 11 (November 2000): 1563–70. http://dx.doi.org/10.1097/00004647-200011000-00006.

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Heat shock protein 90 (HSP90), an essential component of several signal transduction systems, participates in the activation of endothelial nitric oxide synthase (eNOS) in cells. The objective of the current study was to determine if HSP90 and eNOS were functionally interdependent and colocalized in the cerebral circulation. The authors used isometric force recording, cyclic 3′5′-guanosine monophosphate (cGMP) radioimmunoassay (RIA), and immunogold electron microscopy (EM) to study canine basilar artery. They found that geldanamycin (0.1 to 10 μg/mL), a selective HSP90 inhibitor, caused concentration-dependent contractions in arterial rings (n = 6 dogs). Contractions to geldanamycin were unaffected by a cyclooxygenase inhibitor, indomethacin (10 μmol/L; P < 0.05, n = 6). Functional evidence for interaction between HSP90 and nitric oxide (NO)-mediated signaling included observations that the contractile effect of geldanamycin was the following: (1) endothelium-dependent, (2) abolished by Ng-nitro-l-arginine methylester (L-NAME; 0.3 mmol/L), and (3) nonadditive with the contractile effect of this NOS inhibitor ( P < 0.01, n = 6 for each). Furthermore, RIA showed significant reduction in cGMP levels in arteries treated with geldanamycin (3 μg/mL; P < 0.02, n = 8), whereas immunogold EM demonstrated areas of colocalization of HSP90 and eNOS selectively in the cytoplasm of endothelial cells. The current findings suggest that in cerebral arteries, endothelial HSP90 plays an important role in modulation of basal NO-mediated signaling. This interaction may be particularly important in stress-induced up-regulation of HSP90 with subsequent alteration of vasomotor function.

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27

Lees, Michael J., and Murray L. Whitelaw. "Multiple Roles of Ligand in Transforming the Dioxin Receptor to an Active Basic Helix-Loop-Helix/PAS Transcription Factor Complex with the Nuclear Protein Arnt." Molecular and Cellular Biology 19, no. 8 (August 1, 1999): 5811–22. http://dx.doi.org/10.1128/mcb.19.8.5811.

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ABSTRACT The dioxin receptor is a ligand-activated transcription factor belonging to an emerging class of basic helix-loop-helix/PAS proteins which show interaction with the molecular chaperone hsp90 in their latent states and require heterodimerization with a general cofactor, Arnt, to form active DNA binding complexes. Upon binding of polycyclic aromatic hydrocarbons typified by dioxin, the dioxin receptor translocates from the cytoplasm to the nucleus to allow interaction with Arnt. Here we have bypassed the nuclear translocation step by creating a cell line which expresses a constitutively nuclear dioxin receptor, which we find remains in a latent form, demonstrating that ligand has functional roles beyond initiating nuclear import of the receptor. Treatment of the nuclear receptor with dioxin induces dimerization with Arnt to form an active transcription factor complex, while in stark contrast, treatment with the hsp90 ligand geldanamycin results in rapid degradation of the receptor. Inhibition of degradation by a proteasome inhibitor allowed geldanamycin to transform the nuclear dioxin receptor to a heterodimer with Arnt (DR-Arnt). Our results indicate that unchaperoned dioxin receptor is extremely labile and is consistent with a concerted nuclear mechanism for receptor activation whereby hsp90 is released from the ligand-bound dioxin receptor concomitant with Arnt dimerization. Strikingly, artificial transformation of the receptor by geldanamycin provided a DR-Arnt complex capable of binding DNA but incapable of stimulating transcription. Limited proteolysis of DR-Arnt heterodimers indicated different conformations for dioxin versus geldanamycin-transformed receptors. Our studies of intracellular dioxin receptor transformation indicate that ligand plays multiple mechanistic roles during receptor activation, being important for nuclear translocation, transformation to an Arnt heterodimer, and maintenance of a structural integrity key for transcriptional activation.

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Zhang, Hao, Guang-Zhi Sun, Xiang Li, Hong-Yu Pan, and Yan-Sheng Zhang. "A New Geldanamycin Analogue from Streptomyces hygroscopicus." Molecules 15, no. 3 (March 3, 2010): 1161–67. http://dx.doi.org/10.3390/molecules15031161.

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Kuduk, Scott D., Christina R. Harris, Fuzhong F. Zheng, Laura Sepp-Lorenzino, Quathek Ouerfelli, Neal Rosen, and Samuel J. Danishefsky. "Synthesis and evaluation of geldanamycin–testosterone hybrids." Bioorganic & Medicinal Chemistry Letters 10, no. 11 (June 2000): 1303–6. http://dx.doi.org/10.1016/s0960-894x(00)00208-0.

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30

Hilton, Margaret J., Christopher M. Brackett, Brandon Q. Mercado, Brian S. J. Blagg, and Scott J. Miller. "Catalysis-Enabled Access to Cryptic Geldanamycin Oxides." ACS Central Science 6, no. 3 (February 24, 2020): 426–35. http://dx.doi.org/10.1021/acscentsci.0c00024.

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31

Kuduk, Scott D., Fuzhong F. Zheng, Laura Sepp-Lorenzino, Neal Rosen, and Samuel J. Danishefsky. "Synthesis and evaluation of geldanamycin-estradiol hybrids." Bioorganic & Medicinal Chemistry Letters 9, no. 9 (May 1999): 1233–38. http://dx.doi.org/10.1016/s0960-894x(99)00185-7.

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Tian, Zong-Qiang, Zhan Wang, Karen S. MacMillan, Yiqing Zhou, Christopher W. Carreras, Thomas Mueller, David C. Myles, and Yaoquan Liu. "Potent Cytotoxic C-11 Modified Geldanamycin Analogues." Journal of Medicinal Chemistry 52, no. 10 (May 28, 2009): 3265–73. http://dx.doi.org/10.1021/jm900098v.

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Mendelsohn, J. "Use of an Antibody to Target Geldanamycin." Journal of the National Cancer Institute 92, no. 19 (October 4, 2000): 1549–51. http://dx.doi.org/10.1093/jnci/92.19.1549.

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34

Gorska, Magdalena. "Geldanamycin and its derivatives as Hsp90 inhibitors." Frontiers in Bioscience 17, no. 7 (2012): 2269. http://dx.doi.org/10.2741/4050.

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DASGUPTA, G., and J. MOMAND. "Geldanamycin Prevents Nuclear Translocation of Mutant p53." Experimental Cell Research 237, no. 1 (November 25, 1997): 29–37. http://dx.doi.org/10.1006/excr.1997.3766.

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HU, ZHIHAO, YAOQUAN LIU, ZONG-QIANG TIAN, WEI MA, COURTNEY M. STARKS, RIKA REGENTIN, PETER LICARI, DAVID C. MYLES, and C. RICHARD HUTCHINSON. "Isolation and Characterization of Novel Geldanamycin Analogues." Journal of Antibiotics 57, no. 7 (2004): 421–28. http://dx.doi.org/10.7164/antibiotics.57.421.

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Qin, Hua-Li, and James S. Panek. "Total Synthesis of the Hsp90 Inhibitor Geldanamycin." Organic Letters 10, no. 12 (June 2008): 2477–79. http://dx.doi.org/10.1021/ol800749w.

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38

Barzilay, Eran, Nathalie Ben-Califa, Mika Shahar, Yoel Kashman, and Drorit Neumann. "Generation of a novel anti-geldanamycin antibody." Biochemical and Biophysical Research Communications 330, no. 2 (May 2005): 561–64. http://dx.doi.org/10.1016/j.bbrc.2005.03.014.

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Li, Shufen, Siyang Ni, Linzhuan Wu, Li Li, Bingya Jiang, Hongyuan Wang, Guizhi Sun, et al. "19-[(1′S,4′R)-4′-Hydroxy-1′-methoxy-2′-oxopentyl]geldanamycin, a Natural Geldanamycin Analogue fromStreptomyces hygroscopicus17997." Journal of Natural Products 76, no. 5 (May 8, 2013): 969–73. http://dx.doi.org/10.1021/np4000679.

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40

Castorena, Kathryn M., Spencer A. Weeks, Kenneth A. Stapleford, Amy M. Cadwallader, and David J. Miller. "A Functional Heat Shock Protein 90 Chaperone Is Essential for Efficient Flock House Virus RNA Polymerase Synthesis in Drosophila Cells." Journal of Virology 81, no. 16 (May 23, 2007): 8412–20. http://dx.doi.org/10.1128/jvi.00189-07.

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ABSTRACT The molecular chaperone heat shock protein 90 (Hsp90) is involved in multiple cellular processes including protein maturation, complex assembly and disassembly, and intracellular transport. We have recently shown that a disruption of Hsp90 activity in cultured Drosophila melanogaster cells suppresses Flock House virus (FHV) replication and the accumulation of protein A, the FHV RNA-dependent RNA polymerase. In the present study, we investigated whether the defect in FHV RNA polymerase accumulation induced by Hsp90 suppression was secondary to an effect on protein A synthesis, degradation, or intracellular membrane association. Treatment with the Hsp90-specific inhibitor geldanamycin selectively reduced FHV RNA polymerase synthesis by 80% in Drosophila S2 cells stably transfected with an inducible protein A expression plasmid. The suppressive effect of geldanamycin on protein A synthesis was not attenuated by proteasome inhibition, nor was it sensitive to changes in either the mRNA untranslated regions or protein A intracellular membrane localization. Furthermore, geldanamycin did not promote premature protein A degradation, nor did it alter the extremely rapid kinetics of protein A membrane association. These results identify a novel role for Hsp90 in facilitating viral RNA polymerase synthesis in Drosophila cells and suggest that FHV subverts normal cellular pathways to assemble functional replication complexes.

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Lerdrup, Mads, Silas Bruun, Michael V. Grandal, Kirstine Roepstorff, Malene M. Kristensen, Anette M. Hommelgaard, and Bo van Deurs. "Endocytic Down-Regulation of ErbB2 Is Stimulated by Cleavage of Its C-Terminus." Molecular Biology of the Cell 18, no. 9 (September 2007): 3656–66. http://dx.doi.org/10.1091/mbc.e07-01-0025.

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High ErbB2 levels are associated with cancer, and impaired endocytosis of ErbB2 could contribute to its overexpression. Therefore, knowledge about the mechanisms underlying endocytic down-regulation of ErbB2 is warranted. The C-terminus of ErbB2 can be cleaved after various stimuli, and after inhibition of HSP90 with geldanamycin this cleavage is accompanied by proteasome-dependent endocytosis of ErbB2. However, it is unknown whether C-terminal cleavage is linked to endocytosis. To study ErbB2 cleavage and endocytic trafficking, we fused yellow fluorescent protein (YFP) and cyan fluorescent protein (CFP) to the N- and C-terminus of ErbB2, respectively (YFP-ErbB2-CFP). After geldanamycin stimulation YFP-ErbB2-CFP became cleaved in nonapoptotic cells in a proteasome-dependent manner, and a markedly larger relative amount of cleaved YFP-ErbB2-CFP was observed in early endosomes than in the plasma membrane. Furthermore, cleavage took place at the plasma membrane, and cleaved ErbB2 was internalized and degraded far more efficiently than full-length ErbB2. Concordantly, a C-terminally truncated ErbB2 was also readily endocytosed and degraded in lysosomes compared with full-length ErbB2. Altogether, we suggest that geldanamycin leads to C-terminal cleavage of ErbB2, which releases the receptor from a retention mechanism and causes endocytosis and lysosomal degradation of ErbB2.

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Suttayasorranakhom, Satipat, Chanjira Jaramornburapong, Waya Phuthawong, and Jitnapa Sirirak. "Newly Designed Geldanamycin Analogues for Targeted Cancer-Causing Hsp90 Protein Inhibitor: Molecular Docking Study." Key Engineering Materials 914 (March 21, 2022): 111–16. http://dx.doi.org/10.4028/p-983h53.

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Cancer is currently a major public health concern worldwide. Previous studies have shown that heat shock protein 90 (Hsp90) is the key common cause of cancer. Thus, Hsp90 is one of the important molecular targets for the development of Hsp90 cancer drug based on geldanamycin (GDM) and alvespimycin (17-DMAG). Herein, novel geldanamycin derivatives, S1-S6 were designed as potential Hsp90 cancer drug by targeting signal transduction pathway, especially against oncogenic client protein from Hsp90. The binding of S1-S6 in the cavity of Hsp90 were investigated by molecular docking using the iGEMDOCK v2.1 software. The results illustrated that S1-S6 bound in the binding site of Hsp90 with similar manner to GDM and 17-DMAG. The binding energies of S1-S6 in Hsp90 (PDB ID:1YET) (-137.49 to -123.24 kcal/mol) were comparable to that of GDM (-133.06 kcal/mol) while the binding energies of S1-S6 in Hsp90 (PDB ID:1OSF) (-137.49 to -131.22 kcal/mol) were slightly higher than that of 17-DMAG (-145.31 kcal/mol). S1-S6 interacted well by hydrogen bonding with key amino acids in the binding site of Hsp90, which could inhibit the cancer cell growth. Therefore, S1-S6 containing novel geldanamycin derivatives could be promising molecules for anti-cancer drug against Hsp90 2 types in the future.

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Hermane, Jekaterina, Simone Eichner, Lena Mancuso, Benjamin Schröder, Florenz Sasse, Carsten Zeilinger, and Andreas Kirschning. "New geldanamycin derivatives with anti Hsp properties by mutasynthesis." Organic & Biomolecular Chemistry 17, no. 21 (2019): 5269–78. http://dx.doi.org/10.1039/c9ob00892f.

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Four new non hydroquinone derivatives of geldanamycin are prepared by mutasynthesis and their antiproliferative as well as inhibitory properties for human as well as bacterial heatshock proteins are evaluated.

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44

Wiesgigl, Martina, and Joachim Clos. "Heat Shock Protein 90 Homeostasis Controls Stage Differentiation in Leishmania donovani." Molecular Biology of the Cell 12, no. 11 (November 2001): 3307–16. http://dx.doi.org/10.1091/mbc.12.11.3307.

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The differentiation of Leishmania parasites from the insect stage, the promastigote, toward the pathogenic mammalian stage, the amastigote, is triggered primarily by the rise in ambient temperature encountered during the insect-to-mammal transmission. We show here that inactivation of heat shock protein (Hsp) 90, with the use of the drugs geldanamycin or radicicol, mimics transmission and induces the differentiation from the promastigote to the amastigote stage. Geldanamycin also induces a growth arrest of cultured promastigotes that can be forestalled by overexpression of the cytoplasmic Hsp90. Moreover, we demonstrate that Hsp90 serves as a feedback inhibitor of the cellular heat shock response inLeishmania. Our results are consistent with Hsp90 homeostasis serving as cellular thermometer for these primitive eukaryotes, controlling both the heat shock response and morphological differentiation.

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45

Kampmueller, Kathryn M., and David J. Miller. "The Cellular Chaperone Heat Shock Protein 90 Facilitates Flock House Virus RNA Replication in Drosophila Cells." Journal of Virology 79, no. 11 (June 1, 2005): 6827–37. http://dx.doi.org/10.1128/jvi.79.11.6827-6837.2005.

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ABSTRACT The assembly of viral RNA replication complexes on intracellular membranes represents a critical step in the life cycle of positive-strand RNA viruses. We investigated the role of the cellular chaperone heat shock protein 90 (Hsp90) in viral RNA replication complex assembly and function using Flock House virus (FHV), an alphanodavirus whose RNA-dependent RNA polymerase, protein A, is essential for viral RNA replication complex assembly on mitochondrial outer membranes. The Hsp90 chaperone complex transports cellular mitochondrial proteins to the outer mitochondrial membrane import receptors, and thus we hypothesized that Hsp90 may also facilitate FHV RNA replication complex assembly or function. Treatment of FHV-infected Drosophila S2 cells with the Hsp90-specific inhibitor geldanamycin or radicicol potently suppressed the production of infectious virions and the accumulation of protein A and genomic, subgenomic, and template viral RNA. In contrast, geldanamycin did not inhibit the activity of preformed FHV RNA replication complexes. Hsp90 inhibitors also suppressed viral RNA and protein A accumulation in S2 cells expressing an FHV RNA replicon. Furthermore, Hsp90 inhibition with either geldanamycin or RNAi-mediated chaperone downregulation suppressed protein A accumulation in the absence of viral RNA replication. These results identify Hsp90 as a host factor involved in FHV RNA replication and suggest that FHV uses established cellular chaperone pathways to assemble its RNA replication complexes on intracellular membranes.

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46

Crèvecoeur, Julie, Marie-Paule Merville, Jacques Piette, and Geoffrey Gloire. "Geldanamycin inhibits tyrosine phosphorylation-dependent NF-κB activation." Biochemical Pharmacology 75, no. 11 (June 2008): 2183–91. http://dx.doi.org/10.1016/j.bcp.2008.03.009.

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Wenkert, David, Bernadette Ramirez, Yuehai Shen, and Michael A. Kron. "In VitroActivity of Geldanamycin Derivatives againstSchistosoma japonicumandBrugia malayi." Journal of Parasitology Research 2010 (2010): 1–7. http://dx.doi.org/10.1155/2010/716498.

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Geldanamycin (GA) is a benzoquinone-containing ansamycin that inhibits heat shock protein 90. GA derivatives are being evaluated as anti-neoplastic agents, but their utility against parasites whose heat shock proteins (Hsps) have homology with human Hsp90 is unknown. The activities of four synthetic GA derivatives were testedin vitrousing adultBrugia malayiandSchistosoma japonicum. Two of the derivatives, 17-N-allyl-17-demethoxygeldanamycin (17-AAG) and 17-N-(2-dimethylaminoethylamino)-17-demethoxygeldanamycin (DMAG), are currently in human clinical trials as anticancer drugs. Using concentrations considered safe peak plasma concentrations for these two derivatives, all four derivatives were active against both parasites. The less toxic derivative 17-AAG was as effective as GA in killingS. japonicum, and both DMAG and 5′-bromogeldanoxazinone were more active than 17-AAG againstB. malayi. This work supports continued evaluation of ansamycin derivatives as broad spectrum antiparasitic agents.

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McCollum, Andrea K., Kara B. Lukasiewicz, Cynthia J. TenEyck, Wilma L. Lingle, David O. Toft, and Charles Erlichman. "Cisplatin abrogates the geldanamycin-induced heat shock response." Molecular Cancer Therapeutics 7, no. 10 (October 2008): 3256–64. http://dx.doi.org/10.1158/1535-7163.mct-08-0157.

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Jilani, Kashif, Syed M. Qadri, and Florian Lang. "Geldanamycin-Induced Phosphatidylserine Translocation in the Erythrocyte Membrane." Cellular Physiology and Biochemistry 32, no. 6 (2013): 1600–1609. http://dx.doi.org/10.1159/000356596.

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50

Ochel, H. J. "Modulation of prion protein structural integrity by geldanamycin." Glycobiology 13, no. 9 (April 17, 2003): 655–60. http://dx.doi.org/10.1093/glycob/cwg081.

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