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Up-Regulated Expression of LAMP2 and Autophagy Activity during Neuroendocrine Differentiation of Prostate Cancer LNCaP Cells

Morell, Cecilia, Bort, Alicia, Vara-Ciruelos, Diana, Ramos-Torres, Ágata, Altamirano-Dimas, Manuel, Díaz-Laviada, Inés, Rodríguez-Henche, Nieves·2016·PLOS ONE
DOI 10.1371/journal.pone.0162977PMC PMC5023108
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Figures

Fig 1 Serum withdrawal induces reversible neuroendocrine differentiation of LNCaP cells. (A) LNCaP cells cultured in serum-containing medium (C, control cells) or in serum-free medium (NE, neuroendocrine cells) during 6 days were lysed and neuron-specific enolase (NSE), βIII tubulin (βIII Tub) and androgen receptor (AR) were measured in whole lysates by western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. (B) Quantification of neuron-specific enolase (NSE) mRNA in control and NE cells by real time qRT-PCR. (C) LNCaP cells were grown in serum-containing medium (C, control cells), serum-free medium (NE* cells) during 12 days or serum-free medium for the first 6 days and then the medium was replaced by a serum-containing medium and cells were cultured for another 6 days (NE+FBS). Thereafter, cells were lysed and neuron-specific enolase (NSE) and βIII tubulin (βIII Tub) were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 and ** p<0.01 versus control cells and # p<0.05 versus neuroendocrine cells, compared by the Student’s t test).
Fig 1 Serum withdrawal induces reversible neuroendocrine differentiation of LNCaP cells. (A) LNCaP cells cultured in serum-containing medium (C, control cells) or in serum-free medium (NE, neuroendocrine cells) during 6 days were lysed and neuron-specific enolase (NSE), βIII tubulin (βIII Tub) and androgen receptor (AR) were measured in whole lysates by western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. (B) Quantification of neuron-specific enolase (NSE) mRNA in control and NE cells by real time qRT-PCR. (C) LNCaP cells were grown in serum-containing medium (C, control cells), serum-free medium (NE* cells) during 12 days or serum-free medium for the first 6 days and then the medium was replaced by a serum-containing medium and cells were cultured for another 6 days (NE+FBS). Thereafter, cells were lysed and neuron-specific enolase (NSE) and βIII tubulin (βIII Tub) were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 and ** p<0.01 versus control cells and # p<0.05 versus neuroendocrine cells, compared by the Student’s t test).CC BY · PubMed Central
Fig 2 Heat map showing enrichment in membrane components from DEGs between NE and control cells. DEGs between NE and control cells were functionally assessed using GSEA. Gene Ontology gene sets were downloaded from the Broad Institute’s Molecular Signature Database (version 4.0). Enrichment on gene set “intrinsic _to_membrane” is shown. Up-regulated (red) and down-regulated (blue) genes in NE and control cells are shown.
Fig 2 Heat map showing enrichment in membrane components from DEGs between NE and control cells. DEGs between NE and control cells were functionally assessed using GSEA. Gene Ontology gene sets were downloaded from the Broad Institute’s Molecular Signature Database (version 4.0). Enrichment on gene set “intrinsic _to_membrane” is shown. Up-regulated (red) and down-regulated (blue) genes in NE and control cells are shown.CC BY · PubMed Central
Fig 3 Lysosomal-associated membrane protein 2 (LAMP2) is over-expressed in neuroendocrine differentiated LNCaP cells. LNCaP cells were grown in serum-containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days. (A) LAMP2 was measured in whole lysates of C and NE cells by western blot along with neuroendocrine markers neuron-specific enolase (NSE) and βIII tubulin (βIII Tub). GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. (B) Quantification of LAMP2 mRNA in control and NE cells by real time qRT-PCR. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 versus control cells compared by the Student’s t test). (C) Detection of LAMP2 by immunofluorescence (green). Nuclei are stained with DAPI (blue). Immunofluorescence was analyzed by confocal microscopy. Quantitative analysis of lysotracker and LAMP2 was performed using ImageJ software (NIH).
Fig 3 Lysosomal-associated membrane protein 2 (LAMP2) is over-expressed in neuroendocrine differentiated LNCaP cells. LNCaP cells were grown in serum-containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days. (A) LAMP2 was measured in whole lysates of C and NE cells by western blot along with neuroendocrine markers neuron-specific enolase (NSE) and βIII tubulin (βIII Tub). GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. (B) Quantification of LAMP2 mRNA in control and NE cells by real time qRT-PCR. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 versus control cells compared by the Student’s t test). (C) Detection of LAMP2 by immunofluorescence (green). Nuclei are stained with DAPI (blue). Immunofluorescence was analyzed by confocal microscopy. Quantitative analysis of lysotracker and LAMP2 was performed using ImageJ software (NIH).CC BY · PubMed Central
Fig 4 Autophagy is activated in neuroendocrine differentiated LNCaP cells. LNCaP cells were grown in serum containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days, and when indicated 100 nM Bafilomycin A1 was added to the culture medium for the last three hours. (A) Autophagy activation markers, LC3 and p62, along with neuroendocrine markers NSE and βIII Tub were measured in whole lysates of C and NE cells by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. (B) Detection of LC3 protein by immunofluorescence (green) and nuclei with DAPI (blue). Immunofluorescence was analyzed by confocal microscopy. Quantitative analysis of LC3 was performed using ImageJ software (NIH). (C) Quantification of LC3 and Atg5 mRNA in control and NE cells by real time qRT-PCR. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 and ** p<0.01 versus control cells and # p<0.05 versus neuroendocrine cells, compared by the Student’s t test).
Fig 4 Autophagy is activated in neuroendocrine differentiated LNCaP cells. LNCaP cells were grown in serum containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days, and when indicated 100 nM Bafilomycin A1 was added to the culture medium for the last three hours. (A) Autophagy activation markers, LC3 and p62, along with neuroendocrine markers NSE and βIII Tub were measured in whole lysates of C and NE cells by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. (B) Detection of LC3 protein by immunofluorescence (green) and nuclei with DAPI (blue). Immunofluorescence was analyzed by confocal microscopy. Quantitative analysis of LC3 was performed using ImageJ software (NIH). (C) Quantification of LC3 and Atg5 mRNA in control and NE cells by real time qRT-PCR. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 and ** p<0.01 versus control cells and # p<0.05 versus neuroendocrine cells, compared by the Student’s t test).CC BY · PubMed Central
Fig 5 Autophagy blocking prevents neuroendocrine differentiation of LNCaP cells. LNCaP cells grown in serum-containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) were transfected with negative control siRNA (siC) or siRNA targeting Beclin1 (siBeclin1) or siRNA targeting Atg5 (siATG5) during 6 days. Thereafter, cells were lysed and Beclin1 or Atg5, autophagy markers, LC3 and p62, and neuroendocrine markers, NSE and βIII Tub were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. Results are the mean ± S.D. of at least three independent experiments (*p<0.05 and **p<0.01 versus non-treated control cells and # p<0.05 versus non-treated neuroendocrine cells, compared by the Student’s t test).
Fig 5 Autophagy blocking prevents neuroendocrine differentiation of LNCaP cells. LNCaP cells grown in serum-containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) were transfected with negative control siRNA (siC) or siRNA targeting Beclin1 (siBeclin1) or siRNA targeting Atg5 (siATG5) during 6 days. Thereafter, cells were lysed and Beclin1 or Atg5, autophagy markers, LC3 and p62, and neuroendocrine markers, NSE and βIII Tub were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. Results are the mean ± S.D. of at least three independent experiments (*p<0.05 and **p<0.01 versus non-treated control cells and # p<0.05 versus non-treated neuroendocrine cells, compared by the Student’s t test).CC BY · PubMed Central
Fig 6 LAMP2 knockdown prevents autophagy, neuroendocrine differentiation and survival of LNCaP cells. LNCaP cells were transfected with negative control siRNA (siC) or siRNA targeting LAMP2 (siLAMP2) and grown in serum-containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days. (A) Cells were lysed and LAMP2, autophagy markers, LC3 and p62, and neuroendocrine markers, NSE and βIII Tub, were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. (B) Cell viability of control and NE cells treated with siC or siLAMP2 was monitored by MTT assay. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 and ** p<0.01 versus siC transfected control cells and # p<0.05 and ## p<0.01 versus siC transfected neuroendocrine cells, compared by the Student’s t test).
Fig 6 LAMP2 knockdown prevents autophagy, neuroendocrine differentiation and survival of LNCaP cells. LNCaP cells were transfected with negative control siRNA (siC) or siRNA targeting LAMP2 (siLAMP2) and grown in serum-containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days. (A) Cells were lysed and LAMP2, autophagy markers, LC3 and p62, and neuroendocrine markers, NSE and βIII Tub, were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. (B) Cell viability of control and NE cells treated with siC or siLAMP2 was monitored by MTT assay. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 and ** p<0.01 versus siC transfected control cells and # p<0.05 and ## p<0.01 versus siC transfected neuroendocrine cells, compared by the Student’s t test).CC BY · PubMed Central
Fig 7 Autophagy inhibition decrease LAMP2 levels and survival of neuroendocrine differentiated LNCaP cells. LNCaP cells were transfected with negative control siRNA (siC) or siRNA targeting Beclin1 (siBeclin1) or si RNA targeting Atg5 (SiATG5) and grown in serum containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days. (A) Cells were lysed and Beclin1 (left), Atg5 (right) and LAMP2 were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown below. (B) Cell viability of control and NE cells treated with siC, siBeclin1 (left) or SiATG5 (right) was monitored by MTT assay. Results are the mean ± S.D. of three independent experiments (* p<0.05 versus siC transfected control cells and # p<0.05 and ## p<0.01 versus siC transfected neuroendocrine cells, compared by the Student’s t test).
Fig 7 Autophagy inhibition decrease LAMP2 levels and survival of neuroendocrine differentiated LNCaP cells. LNCaP cells were transfected with negative control siRNA (siC) or siRNA targeting Beclin1 (siBeclin1) or si RNA targeting Atg5 (SiATG5) and grown in serum containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days. (A) Cells were lysed and Beclin1 (left), Atg5 (right) and LAMP2 were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown below. (B) Cell viability of control and NE cells treated with siC, siBeclin1 (left) or SiATG5 (right) was monitored by MTT assay. Results are the mean ± S.D. of three independent experiments (* p<0.05 versus siC transfected control cells and # p<0.05 and ## p<0.01 versus siC transfected neuroendocrine cells, compared by the Student’s t test).CC BY · PubMed Central
Fig 8 Pharmacological inhibition of AKT prevents autophagy, LAMP2 overexpression and neuroendocrine differentiation of LNCaP cells. LNCaP cells were grown in serum-containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days. Cells where treated with vehicle (vhc) or 1 μM AKT inhibitor IV for 6 days. When indicated, cells were treated with 100 nM bafilomycin A1 for the last three hours in culture. Thereafter cells were lysed and autophagy markers, LC3 and p62, LAMP2 and neuroendocrine markers, NSE and βIII Tub, were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 and **p<0.01 versus not treated control cells and # p<0.05 versus not treated neuroendocrine cells, compared by the Student’s t test).
Fig 8 Pharmacological inhibition of AKT prevents autophagy, LAMP2 overexpression and neuroendocrine differentiation of LNCaP cells. LNCaP cells were grown in serum-containing medium (C, control cells) or serum-free medium (NE, neuroendocrine cells) during 6 days. Cells where treated with vehicle (vhc) or 1 μM AKT inhibitor IV for 6 days. When indicated, cells were treated with 100 nM bafilomycin A1 for the last three hours in culture. Thereafter cells were lysed and autophagy markers, LC3 and p62, LAMP2 and neuroendocrine markers, NSE and βIII Tub, were measured in whole lysates by Western blot. GAPDH was used as a loading control. Densitometric analysis of the Western blot bands are shown on the right. Results are the mean ± S.D. of at least three independent experiments (* p<0.05 and **p<0.01 versus not treated control cells and # p<0.05 versus not treated neuroendocrine cells, compared by the Student’s t test).CC BY · PubMed Central

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Cites

Research works printed but not linked: 58

  1. J Ferlay, 2015, Cancer incidence and mortality worldwide: sources, methods and major patterns in GLOBOCAN 2012, International journal of cancer Journal international du cancer, 136, E359, 10.1002/ijc.29210 · DOI · Paper page
  2. FG Rick, 2015, Bench-to-bedside development of agonists and antagonists of luteinizing hormone-releasing hormone for treatment of advanced prostate cancer, Urologic oncology, 33, 270, 10.1016/j.urolonc.2014.11.006 · DOI
  3. DJ Samson, 2002, Systematic review and meta-analysis of monotherapy compared with combined androgen blockade for patients with advanced prostate carcinoma, Cancer, 95, 361, 10.1002/cncr.10647 · DOI
  4. AA Shafi, 2013, Androgen receptors in hormone-dependent and castration-resistant prostate cancer, Pharmacology & therapeutics, 140, 223, 10.1016/j.pharmthera.2013.07.003 · DOI
  5. F Saad, 2015, Androgen Deprivation Therapy and Secondary Hormone Therapy in the Management of Hormone-sensitive and Castration-resistant Prostate Cancer, Urology, 86, 852, 10.1016/j.urology.2015.07.034 · DOI
  6. T Karantanos, 2013, Prostate cancer progression after androgen deprivation therapy: mechanisms of castrate resistance and novel therapeutic approaches, Oncogene, 32, 5501, 10.1038/onc.2013.206 · DOI
  7. D Hirano, 2004, Neuroendocrine differentiation in hormone refractory prostate cancer following androgen deprivation therapy, European urology, 45, 586, 10.1016/j.eururo.2003.11.032 · DOI
  8. H Beltran, 2014, Aggressive variants of castration-resistant prostate cancer. Clinical cancer research: an official journal of the, American Association for Cancer Research, 20, 2846
  9. AW Wyatt, 2015, Targeting the adaptive molecular landscape of castration-resistant prostate cancer, EMBO molecular medicine, 7, 878, 10.15252/emmm.201303701 · DOI
  10. O Cussenot, 1996, Plasma neuroendocrine markers in patients with benign prostatic hyperplasia and prostatic carcinoma, The Journal of urology, 155, 1340, 10.1016/S0022-5347(01)66261-X · DOI
  11. S Isshiki, 2002, Chromogranin a concentration as a serum marker to predict prognosis after endocrine therapy for prostate cancer, The Journal of urology, 167, 512, 10.1016/S0022-5347(01)69075-X · DOI
  12. T Hvamstad, 2003, Neuroendocrine serum tumour markers in hormone-resistant prostate cancer, European urology, 44, 215, 10.1016/S0302-2838(03)00257-4 · DOI
  13. Y Sun, 2009, Neuroendocrine differentiation in prostate cancer, American journal of translational research, 1, 148
  14. PA Abrahamsson, 1999, Neuroendocrine cells in tumour growth of the prostate, Endocrine-related cancer, 6, 503, 10.1677/erc.0.0060503 · DOI
  15. S Terry, 2014, The many faces of neuroendocrine differentiation in prostate cancer progression, Frontiers in oncology, 4, 60, 10.3389/fonc.2014.00060 · DOI
  16. CG Sauer, 2006, Genetic analysis of neuroendocrine tumor cells in prostatic carcinoma, The Prostate, 66, 227, 10.1002/pros.20338 · DOI
  17. YJ Bang, 1994, Terminal neuroendocrine differentiation of human prostate carcinoma cells in response to increased intracellular cyclic AMP, Proceedings of the National Academy of Sciences of the United States of America, 91, 5330, 10.1073/pnas.91.12.5330 · DOI
  18. ME Cox, 1999, Acquisition of neuroendocrine characteristics by prostate tumor cells is reversible: implications for prostate cancer progression, Cancer research, 59, 3821
  19. PD Deeble, 2001, Interleukin-6- and cyclic AMP-mediated signaling potentiates neuroendocrine differentiation of LNCaP prostate tumor cells, Molecular and cellular biology, 21, 8471, 10.1128/MCB.21.24.8471-8482.2001 · DOI
  20. I Gutierrez-Canas, 2005, Vasoactive intestinal peptide induces neuroendocrine differentiation in the LNCaP prostate cancer cell line through PKA, ERK, and PI3K, The Prostate, 63, 44, 10.1002/pros.20173 · DOI
  21. R Shen, 1997, Transdifferentiation of cultured human prostate cancer cells to a neuroendocrine cell phenotype in a hormone-depleted medium, Urologic oncology, 3, 67, 10.1016/S1078-1439(97)00039-2 · DOI
  22. P Saftig, 2009, Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function, Nature reviews Molecular cell biology, 10, 623, 10.1038/nrm2745 · DOI · Paper page
  23. M Fukuda, 1991, Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking, The Journal of biological chemistry, 266, 21327, 10.1016/S0021-9258(18)54636-6 · DOI
  24. EL Eskelinen, 2006, Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy, Molecular aspects of medicine, 27, 495, 10.1016/j.mam.2006.08.005 · DOI
  25. Y Tanaka, 2000, Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice, Nature, 406, 902, 10.1038/35022595 · DOI · Paper page
  26. I Nishino, 2000, Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease), Nature, 406, 906, 10.1038/35022604 · DOI · Paper page
  27. Y Endo, 2015, Danon disease: a phenotypic expression of LAMP-2 deficiency, Acta neuropathologica, 129, 391, 10.1007/s00401-015-1385-4 · DOI
  28. EL Eskelinen, 2005, Unifying nomenclature for the isoforms of the lysosomal membrane protein LAMP-2, Traffic, 6, 1058, 10.1111/j.1600-0854.2005.00337.x · DOI
  29. AM Cuervo, 2014, Chaperone-mediated autophagy: roles in disease and aging, Cell research, 24, 92, 10.1038/cr.2013.153 · DOI
  30. Y Fujiwara, 2013, Discovery of a novel type of autophagy targeting RNA, Autophagy, 9, 403, 10.4161/auto.23002 · DOI
  31. Y Fujiwara, 2013, Direct uptake and degradation of DNA by lysosomes, Autophagy, 9, 1167, 10.4161/auto.24880 · DOI
  32. F Janku, 2011, Autophagy as a target for anticancer therapy, Nature reviews Clinical oncology, 8, 528, 10.1038/nrclinonc.2011.71 · DOI
  33. L Galluzzi, 2015, Autophagy in malignant transformation and cancer progression, The EMBO journal, 34, 856, 10.15252/embj.201490784 · DOI · Paper page
  34. JM Farrow, 2014, Autophagy as a modulator and target in prostate cancer, Nature reviews Urology, 11, 508, 10.1038/nrurol.2014.196 · DOI
  35. ME Wright, 2003, Androgen receptor represses the neuroendocrine transdifferentiation process in prostate cancer cells, Molecular endocrinology, 17, 1726, 10.1210/me.2003-0031 · DOI · Paper page
  36. AM Cuervo, 1996, A receptor for the selective uptake and degradation of proteins by lysosomes, Science, 273, 501, 10.1126/science.273.5274.501 · DOI · Paper page
  37. JP Luzio, 2007, Lysosomes: fusion and function, Nature reviews Molecular cell biology, 8, 622, 10.1038/nrm2217 · DOI
  38. K Kannan, 1996, Lysosome-associated membrane proteins h-LAMP1 (CD107a) and h-LAMP2 (CD107b) are activation-dependent cell surface glycoproteins in human peripheral blood mononuclear cells which mediate cell adhesion to vascular endothelium, Cellular immunology, 171, 10, 10.1006/cimm.1996.0167 · DOI
  39. M Damaghi, 2015, Chronic acidosis in the tumour microenvironment selects for overexpression of LAMP2 in the plasma membrane, Nature communications, 6, 8752, 10.1038/ncomms9752 · DOI
  40. RA Gottlieb, 2015, Untangling autophagy measurements: all fluxed up, Circulation research, 116, 504, 10.1161/CIRCRESAHA.116.303787 · DOI
  41. H Murillo, 2001, Role of PI3K signaling in survival and progression of LNCaP prostate cancer cells to the androgen refractory state, Endocrinology, 142, 4795, 10.1210/endo.142.11.8467 · DOI
  42. S Xie, 2004, Regulation of interleukin-6-mediated PI3K activation and neuroendocrine differentiation by androgen signaling in prostate cancer LNCaP cells, The Prostate, 60, 61, 10.1002/pros.20048 · DOI
  43. C Morell, 2016, The cannabinoid WIN 55,212–2 prevents neuroendocrine differentiation of LNCaP prostate cancer cells, Prostate Cancer Prostatic Dis
  44. H Appelqvist, 2013, The lysosome: from waste bag to potential therapeutic target, Journal of molecular cell biology, 5, 214, 10.1093/jmcb/mjt022 · DOI · Paper page
  45. N Fehrenbacher, 2008, Sensitization to the lysosomal cell death pathway by oncogene-induced down-regulation of lysosome-associated membrane proteins 1 and 2, Cancer research, 68, 6623, 10.1158/0008-5472.CAN-08-0463 · DOI
  46. K Furuta, 2001, Expression of lysosome-associated membrane proteins in human colorectal neoplasms and inflammatory diseases, The American journal of pathology, 159, 449, 10.1016/S0002-9440(10)61716-6 · DOI
  47. T Saha, 2012, LAMP2A overexpression in breast tumors promotes cancer cell survival via chaperone-mediated autophagy, Autophagy, 8, 1643, 10.4161/auto.21654 · DOI
  48. M Kon, 2011, Chaperone-mediated autophagy is required for tumor growth, Science translational medicine, 3, 109ra17
  49. A Ibrahim-Hashim, 2012, Systemic buffers inhibit carcinogenesis in TRAMP mice, The Journal of urology, 188, 624, 10.1016/j.juro.2012.03.113 · DOI
  50. EA Dunlop, 2014, mTOR and autophagy: a dynamic relationship governed by nutrients and energy, Semin Cell Dev Biol, 36, 121, 10.1016/j.semcdb.2014.08.006 · DOI
  51. M Matsuda-Lennikov, 2014, Lysosomal interaction of Akt with Phafin2: a critical step in the induction of autophagy, PloS one, 9, e79795, 10.1371/journal.pone.0079795 · DOI
  52. M Noguchi, 2014, The links between AKT and two intracellular proteolytic cascades: ubiquitination and autophagy, Biochim Biophys Acta, 1846, 342
  53. QW Fan, 2010, Akt and autophagy cooperate to promote survival of drug-resistant glioma, Sci Signal, 3, ra81
  54. PC Chang, 2014, Autophagy pathway is required for IL-6 induced neuroendocrine differentiation and chemoresistance of prostate cancer LNCaP cells, PloS one, 9, e88556, 10.1371/journal.pone.0088556 · DOI
  55. Y Zhu, 2014, Interleukin-6 induces neuroendocrine differentiation (NED) through suppression of RE-1 silencing transcription factor (REST), The Prostate, 74, 1086, 10.1002/pros.22819 · DOI
  56. AV Lapuk, 2012, From sequence to molecular pathology, and a mechanism driving the neuroendocrine phenotype in prostate cancer, The Journal of pathology, 227, 286, 10.1002/path.4047 · DOI
  57. R Manjithaya, 2011, Autophagy: a broad role in unconventional protein secretion?, Trends Cell Biol, 21, 67, 10.1016/j.tcb.2010.09.009 · DOI
  58. M Ponpuak, 2015, Secretory autophagy, Curr Opin Cell Biol, 35, 106, 10.1016/j.ceb.2015.04.016 · DOI

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Metadata

Authors
Morell, C., Bort, A., Vara-Ciruelos, D., Ramos-Torres, Á., Altamirano-Dimas, M., Díaz-Laviada, I., & Rodríguez-Henche, N.
Venue
PLOS ONE
Publisher
Public Library of Science (PLoS)
Published
2016-09-14
Volume
11
Issue
9
Pages
e0162977
ISSN
1932-6203
DOI
10.1371/journal.pone.0162977
PMC
PMC5023108
Cited by
50
References
4
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
  • Spanish Ministry of Economy and Competitiveness (BFU2012-31444)
  • Junta de Comunidades de Castilla-LaMancha and European Commission FEDER Funds (POII11-0159-0054)
  • Comunidad de Madrid (S2010-BMD2308)
  • Fundación Tatiana Pérez de Guzmán el Bueno (2013-001)
  • Universidad de Alcalá (PI2005/063)

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