The neuroblastoma tumour-suppressor TrkAI and its oncogenic alternative TrkAIII splice variant exhibit geldanamycin-sensitive interactions with Hsp90 in human neuroblastoma cells (494 views)
Oncogene (ISSN: 1476-5594, 0950-9232), 2009 Nov 19; 28(46): 4075-4094.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 7.135, 5-year impact factor: 6.73
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-70450280545&partnerID=40&md5=c6fc9adf243e6cc3ad9c1ad11c5d3645
Keywords: Geldanamycin, Hsp90, Neuroblastoma, Trkai, Heat Shock Protein 90, Protein Tyrosine Kinase A, Alternative Rna Splicing, Apoptosis, Article, Cancer Inhibition, Carcinogenesis, Controlled Study, Endoplasmic Reticulum, Human, Human Cell, Neuroblastoma Cell, Priority Journal, Protein Analysis, Protein Function, Protein Protein Interaction, Alternative Splicing, Antigens, Surface, Benzoquinones, Enzyme Stability, Tumor Suppressor, Hsp90 Heat-Shock Proteins, Isoenzymes, Lactams, Macrocyclic, Oncogenes, Phosphorylation, Protein Binding, Protein Kinase Inhibitors, Protein Transport, Receptor, Transfection, Tumor Cells, Cultured,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine, University of L'Aquila, L'Aquila, Italy.
Department of Biological Science, University of Naples Federico II, Naples, Italy
References:
Not available.
Oncogene (ISSN: 1476-5594, 0950-9232), 2009 Nov 19; 28(46): 4075-4094.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 7.135, 5-year impact factor: 6.73
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-70450280545&partnerID=40&md5=c6fc9adf243e6cc3ad9c1ad11c5d3645
Keywords: Geldanamycin, Hsp90, Neuroblastoma, Trkai, Heat Shock Protein 90, Protein Tyrosine Kinase A, Alternative Rna Splicing, Apoptosis, Article, Cancer Inhibition, Carcinogenesis, Controlled Study, Endoplasmic Reticulum, Human, Human Cell, Neuroblastoma Cell, Priority Journal, Protein Analysis, Protein Function, Protein Protein Interaction, Alternative Splicing, Antigens, Surface, Benzoquinones, Enzyme Stability, Tumor Suppressor, Hsp90 Heat-Shock Proteins, Isoenzymes, Lactams, Macrocyclic, Oncogenes, Phosphorylation, Protein Binding, Protein Kinase Inhibitors, Protein Transport, Receptor, Transfection, Tumor Cells, Cultured,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine, University of L'Aquila, L'Aquila, Italy.
Department of Biological Science, University of Naples Federico II, Naples, Italy
References:
Not available.
The neuroblastoma tumour-suppressor TrkAI and its oncogenic alternative TrkAIII splice variant exhibit geldanamycin-sensitive interactions with Hsp90 in human neuroblastoma cells
Hsp90 chaperones stabilize many tyrosine kinases including several oncogenes, which are inhibited or induced to degrade by the Hsp90 inhibitor geldanamycin (GA). As a consequence, GA has been developed for future chemotherapeutic use in several tumour types including neuroblastoma (NB). Alternative splicing of the neurotrophin receptor tyrosine kinase TrkA may have a pivotal function in regulating NB behaviour, with reports suggesting that tumour-suppressing signals from TrkA may be converted to oncogenic signals by stress-regulated alternative TrkAIII splicing. Within this context, it is important to know whether Hsp90 interacts with TrkA variants in NB cells and how GA influences this. Here, we report that both TrkAI and TrkAIII are Hsp90 clients in human NB cells. TrkAI exhibits GA-sensitive interaction with Hsp90 required for receptor endoplasmic reticulum export, maturation, cell surface stabilization and ligand-mediated activation, whereas TrkAIII exhibits GA-sensitive interactions with Hsp90 required for spontaneous activity and to a lesser extent stability. We show that GA inhibits proliferation and induces apoptosis of TrkAI expressing NB cells, whereas TrkAIII reduces the sensitivity of NB cells to GA-induced elimination. Our data suggest that GA-sensitive interactions with Hsp90 are critical for both TrkAI tumour suppressor and TrkAIII oncogenic function in NB and that TrkAIII expression exerts a negative impact on GA-induced NB cell eradication, which can be counteracted by a novel TrkAIII-specific peptide nucleic acid inhibitor.
Hsp90 chaperones stabilize many tyrosine kinases including several oncogenes, which are inhibited or induced to degrade by the Hsp90 inhibitor geldanamycin (GA). As a consequence, GA has been developed for future chemotherapeutic use in several tumour types including neuroblastoma (NB). Alternative splicing of the neurotrophin receptor tyrosine kinase TrkA may have a pivotal function in regulating NB behaviour, with reports suggesting that tumour-suppressing signals from TrkA may be converted to oncogenic signals by stress-regulated alternative TrkAIII splicing. Within this context, it is important to know whether Hsp90 interacts with TrkA variants in NB cells and how GA influences this. Here, we report that both TrkAI and TrkAIII are Hsp90 clients in human NB cells. TrkAI exhibits GA-sensitive interaction with Hsp90 required for receptor endoplasmic reticulum export, maturation, cell surface stabilization and ligand-mediated activation, whereas TrkAIII exhibits GA-sensitive interactions with Hsp90 required for spontaneous activity and to a lesser extent stability. We show that GA inhibits proliferation and induces apoptosis of TrkAI expressing NB cells, whereas TrkAIII reduces the sensitivity of NB cells to GA-induced elimination. Our data suggest that GA-sensitive interactions with Hsp90 are critical for both TrkAI tumour suppressor and TrkAIII oncogenic function in NB and that TrkAIII expression exerts a negative impact on GA-induced NB cell eradication, which can be counteracted by a novel TrkAIII-specific peptide nucleic acid inhibitor.
The neuroblastoma tumour-suppressor TrkAI and its oncogenic alternative TrkAIII splice variant exhibit geldanamycin-sensitive interactions with Hsp90 in human neuroblastoma cells
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The neuroblastoma tumour-suppressor TrkAI and its oncogenic alternative TrkAIII splice variant exhibit geldanamycin-sensitive interactions with Hsp90 in human neuroblastoma cells
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 5.686
View Export to BibTeX Export to EndNote
Travaglia A, Arena G, Fattorusso R, Isernia C, La Mendola D, Malgieri G, Nicoletti VG, Rizzarelli E
* The inorganic perspective of nerve growth factor: interactions of Cu2+ and Zn2+ with the N-terminus fragment of nerve growth factor encompassing the recognition domain of the TrkA receptor (603 views)
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Impact Factor: 5.925
View Export to BibTeX Export to EndNote
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Impact Factor: 5.036
View Export to BibTeX Export to EndNote
Farina AR, Tacconelli A, Cappabianca L, Cea G, Panella S, Chioda A, Romanelli A, Pedone C, Gulino A, Mackay AR
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Mol Cell Biol (ISSN: 1098-5549, 0270-7306), 2009 Sep 1; 29(17): 4812-4830.
Impact Factor: 6.057
View Export to BibTeX Export to EndNote
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Impact Factor: 7.452
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 1.623
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 3.491
View Export to BibTeX Export to EndNote
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Ital J Ophthalmol (ISSN: 0394-610x), 1993; 7(3): 147-152.
Impact Factor: 0
View Export to BibTeX Export to EndNote
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Impact Factor: 6.772
View Export to BibTeX Export to EndNote
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Impact Factor: 0.967
View Export to BibTeX Export to EndNote
22 Records (21 excluding Abstracts).
Total impact factor: 107.272 (102.194 excluding Abstracts).
Total 5 year impact factor: 109.405 (104.327 excluding Abstracts).
Total impact factor: 107.272 (102.194 excluding Abstracts).
Total 5 year impact factor: 109.405 (104.327 excluding Abstracts).
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