Biological relevance of Hsp90-binding immunophilins in cancer development and treatment
Immunophilins are a family of intracellular receptors for immunosuppressive drugs. Those immunophilins that are related to immunosuppression are the smallest proteins of the family, i.e., FKBP12 and CyPA, whereas the other members of the family have higher molecular weight because the show additiona...
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2016
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207136_v138_n4_p797_Mazaira http://hdl.handle.net/20.500.12110/paper_00207136_v138_n4_p797_Mazaira |
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paper:paper_00207136_v138_n4_p797_Mazaira2023-06-08T14:41:21Z Biological relevance of Hsp90-binding immunophilins in cancer development and treatment FKBP38 FKBP51 FKBP52 FKBPL NF-κB steroid receptor 1 (3,3 dimethyl 1,2 dioxopentyl) 2 pyrrolidinecarboxylic acid 3 (3 pyridyl)propyl ester alm 201 bicalutamide calcineurin inhibitor calcium cisplatin cycloheximide cyclophilin 40 cyclophilin A etoposide fk 506 binding protein 12 fk 506 binding protein 38 fk 506 binding protein 51 fk 506 binding protein 52 glucocorticoid receptor heat shock protein 90 immunophilin methotrexate n (n',n' dimethylcarboxamidomethyl)cycloheximide paclitaxel rapamycin staurosporine steroid receptor tacrolimus unclassified drug heat shock protein 90 immunophilin amino acid sequence antineoplastic activity breast cancer cancer inhibition carcinogenesis colorectal carcinoma complex formation drug effect drug resistance glioma human lymphoma melanoma neoplasm nonhuman pancreas cancer priority journal prostate cancer protein protein interaction Review signal transduction animal metabolism neoplasm Animals HSP90 Heat-Shock Proteins Humans Immunophilins Neoplasms Immunophilins are a family of intracellular receptors for immunosuppressive drugs. Those immunophilins that are related to immunosuppression are the smallest proteins of the family, i.e., FKBP12 and CyPA, whereas the other members of the family have higher molecular weight because the show additional domains to the drug-binding site. Among these extra domains, the TPR-domain is perhaps the most relevant because it permits the interaction of high molecular weight immunophilins with the 90-kDa heat-shock protein, Hsp90. This essential molecular chaperone regulates the biological function of several protein-kinases, oncogenes, protein phosphatases, transcription factors and cofactors. Hsp90-binding immunophilins where first characterized due to their association with steroid receptors. They regulate the cytoplasmic transport and the subcellular localization of these and other Hsp90 client proteins, as well as transcriptional activity, cell proliferation, cell differentiation and apoptosis. Hsp90-binding immunophilins are frequently overexpressed in several types of cancers and play a key role in cell survival. In this article we analyze the most important biological actions of the best characterized Hsp90-binding immunophilins in both steroid receptor function and cancer development and discuss the potential use of these immunophilins for therapeutic purposes as potential targets of specific small molecules. © 2015 UICC. 2016 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207136_v138_n4_p797_Mazaira http://hdl.handle.net/20.500.12110/paper_00207136_v138_n4_p797_Mazaira |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
FKBP38 FKBP51 FKBP52 FKBPL NF-κB steroid receptor 1 (3,3 dimethyl 1,2 dioxopentyl) 2 pyrrolidinecarboxylic acid 3 (3 pyridyl)propyl ester alm 201 bicalutamide calcineurin inhibitor calcium cisplatin cycloheximide cyclophilin 40 cyclophilin A etoposide fk 506 binding protein 12 fk 506 binding protein 38 fk 506 binding protein 51 fk 506 binding protein 52 glucocorticoid receptor heat shock protein 90 immunophilin methotrexate n (n',n' dimethylcarboxamidomethyl)cycloheximide paclitaxel rapamycin staurosporine steroid receptor tacrolimus unclassified drug heat shock protein 90 immunophilin amino acid sequence antineoplastic activity breast cancer cancer inhibition carcinogenesis colorectal carcinoma complex formation drug effect drug resistance glioma human lymphoma melanoma neoplasm nonhuman pancreas cancer priority journal prostate cancer protein protein interaction Review signal transduction animal metabolism neoplasm Animals HSP90 Heat-Shock Proteins Humans Immunophilins Neoplasms |
| spellingShingle |
FKBP38 FKBP51 FKBP52 FKBPL NF-κB steroid receptor 1 (3,3 dimethyl 1,2 dioxopentyl) 2 pyrrolidinecarboxylic acid 3 (3 pyridyl)propyl ester alm 201 bicalutamide calcineurin inhibitor calcium cisplatin cycloheximide cyclophilin 40 cyclophilin A etoposide fk 506 binding protein 12 fk 506 binding protein 38 fk 506 binding protein 51 fk 506 binding protein 52 glucocorticoid receptor heat shock protein 90 immunophilin methotrexate n (n',n' dimethylcarboxamidomethyl)cycloheximide paclitaxel rapamycin staurosporine steroid receptor tacrolimus unclassified drug heat shock protein 90 immunophilin amino acid sequence antineoplastic activity breast cancer cancer inhibition carcinogenesis colorectal carcinoma complex formation drug effect drug resistance glioma human lymphoma melanoma neoplasm nonhuman pancreas cancer priority journal prostate cancer protein protein interaction Review signal transduction animal metabolism neoplasm Animals HSP90 Heat-Shock Proteins Humans Immunophilins Neoplasms Biological relevance of Hsp90-binding immunophilins in cancer development and treatment |
| topic_facet |
FKBP38 FKBP51 FKBP52 FKBPL NF-κB steroid receptor 1 (3,3 dimethyl 1,2 dioxopentyl) 2 pyrrolidinecarboxylic acid 3 (3 pyridyl)propyl ester alm 201 bicalutamide calcineurin inhibitor calcium cisplatin cycloheximide cyclophilin 40 cyclophilin A etoposide fk 506 binding protein 12 fk 506 binding protein 38 fk 506 binding protein 51 fk 506 binding protein 52 glucocorticoid receptor heat shock protein 90 immunophilin methotrexate n (n',n' dimethylcarboxamidomethyl)cycloheximide paclitaxel rapamycin staurosporine steroid receptor tacrolimus unclassified drug heat shock protein 90 immunophilin amino acid sequence antineoplastic activity breast cancer cancer inhibition carcinogenesis colorectal carcinoma complex formation drug effect drug resistance glioma human lymphoma melanoma neoplasm nonhuman pancreas cancer priority journal prostate cancer protein protein interaction Review signal transduction animal metabolism neoplasm Animals HSP90 Heat-Shock Proteins Humans Immunophilins Neoplasms |
| description |
Immunophilins are a family of intracellular receptors for immunosuppressive drugs. Those immunophilins that are related to immunosuppression are the smallest proteins of the family, i.e., FKBP12 and CyPA, whereas the other members of the family have higher molecular weight because the show additional domains to the drug-binding site. Among these extra domains, the TPR-domain is perhaps the most relevant because it permits the interaction of high molecular weight immunophilins with the 90-kDa heat-shock protein, Hsp90. This essential molecular chaperone regulates the biological function of several protein-kinases, oncogenes, protein phosphatases, transcription factors and cofactors. Hsp90-binding immunophilins where first characterized due to their association with steroid receptors. They regulate the cytoplasmic transport and the subcellular localization of these and other Hsp90 client proteins, as well as transcriptional activity, cell proliferation, cell differentiation and apoptosis. Hsp90-binding immunophilins are frequently overexpressed in several types of cancers and play a key role in cell survival. In this article we analyze the most important biological actions of the best characterized Hsp90-binding immunophilins in both steroid receptor function and cancer development and discuss the potential use of these immunophilins for therapeutic purposes as potential targets of specific small molecules. © 2015 UICC. |
| title |
Biological relevance of Hsp90-binding immunophilins in cancer development and treatment |
| title_short |
Biological relevance of Hsp90-binding immunophilins in cancer development and treatment |
| title_full |
Biological relevance of Hsp90-binding immunophilins in cancer development and treatment |
| title_fullStr |
Biological relevance of Hsp90-binding immunophilins in cancer development and treatment |
| title_full_unstemmed |
Biological relevance of Hsp90-binding immunophilins in cancer development and treatment |
| title_sort |
biological relevance of hsp90-binding immunophilins in cancer development and treatment |
| publishDate |
2016 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207136_v138_n4_p797_Mazaira http://hdl.handle.net/20.500.12110/paper_00207136_v138_n4_p797_Mazaira |
| _version_ |
1768546752465469440 |