The intertwining roles of caveolin, oxytocin receptor, and the associated signalling pathways in prostate cancer progression
M. L. Gould
A *
+ Author Affiliations
- Author Affiliations
A Department of Anatomy, University of Otago, P.O. Box 913, Dunedin 9054, New Zealand.
Reproduction, Fertility and Development 35(9) 493-503 https://doi.org/10.1071/RD22283
Published online: 23 May 2023
© 2023 The Author(s) (or their employer(s)). Published by CSIRO Publishing. This is an open access article distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (CC BY-NC-ND)
Abstract
Caveolae are invaginations in the plasma membrane of most cell types and are present in the cells of normal prostate tissue. Caveolins are a family of highly conserved integral membrane proteins that oligomerise to form caveolae and interact with signalling molecules by providing a scaffold that sequesters signal transduction receptors in close proximity to each other. Signal transduction G proteins and G-protein-coupled receptors (GPCR), including oxytocin receptor (OTR), are localised within caveolae. Only one OTR has been identified, and yet, this single receptor both inhibits and stimulates cell proliferation. As caveolae sequester lipid-modified signalling molecules, these differing effects may be due to a change in location. The cavin1 necessary for caveolae formation is lost in prostate cancer progression. With the loss of caveolae, the OTR moves out onto the cell membrane influencing the proliferation and survival of prostate cancer cells. Caveolin-1 (cav-1) is reportedly overexpressed in prostate cancer cells and is associated with disease progression. This review focuses on the position of OTRs within caveolae, and their movement out onto the cell membrane. It explores whether movement of the OTR is related to changes in the activation of the associated cell signalling pathways that may increase cell proliferation and analyse whether caveolin and particularly cavin1 might be a target for future therapeutic stratagies.
Keywords: cancer progression, caveolae, cavin1, cell signalling pathways, GPCR, lipid rafts, proliferation, sequestration.
References
Anderson, RGW (1998). The caveolae membrane system. Annual Review of Biochemistry 67, 199–225.| The caveolae membrane system.Crossref | GoogleScholarGoogle Scholar |
Arnold, JT, and Isaacs, JT (2002). Mechanisms involved in the progression of androgen-independent prostate cancers: it is not only the cancer cell’s fault. Endocrine-Related Cancer 9, 61–73.
| Mechanisms involved in the progression of androgen-independent prostate cancers: it is not only the cancer cell’s fault.Crossref | GoogleScholarGoogle Scholar |
Aung, CS, Hill, MM, Bastiani, M, Parton, RG, and Parat, M-O (2011). PTRF–cavin-1 expression decreases the migration of PC3 prostate cancer cells: role of matrix metalloprotease 9. European Journal of Cell Biology 90, 136–142.
| PTRF–cavin-1 expression decreases the migration of PC3 prostate cancer cells: role of matrix metalloprotease 9.Crossref | GoogleScholarGoogle Scholar |
Bachmann, N, Haeusler, J, Luedeke, M, Kuefer, R, Perner, S, Assum, G, Paiss, T, Hoegel, J, Vogel, W, and Maier, C (2008). Expression changes of CAV1 and EZH2, located on 7q31~q36, are rarely related to genomic alterations in primary prostate carcinoma. Cancer Genetics and Cytogenetics 182, 103–110.
| Expression changes of CAV1 and EZH2, located on 7q31~q36, are rarely related to genomic alterations in primary prostate carcinoma.Crossref | GoogleScholarGoogle Scholar |
Blando, JM, Carbajal, S, Abel, E, Beltran, L, Conti, C, Fischer, S, and DiGiovanni, J (2011). Cooperation between Stat3 and Akt signaling leads to prostate tumor development in transgenic mice. Neoplasia 13, 254–265.
| Cooperation between Stat3 and Akt signaling leads to prostate tumor development in transgenic mice.Crossref | GoogleScholarGoogle Scholar |
Bocci, G, Fioravanti, A, Orlandi, P, Di Desidero, T, Natale, G, Fanelli, G, Viacava, P, Naccarato, AG, Francia, G, and Danesi, R (2012). Metronomic ceramide analogs inhibit angiogenesis in pancreatic cancer through up-regulation of caveolin-1 and thrombospondin-1 and down-regulation of cyclin D1. Neoplasia 14, 833–845.
| Metronomic ceramide analogs inhibit angiogenesis in pancreatic cancer through up-regulation of caveolin-1 and thrombospondin-1 and down-regulation of cyclin D1.Crossref | GoogleScholarGoogle Scholar |
Bussolati, G, and Cassoni, P (2001). Editorial: the oxytocin/oxytocin receptor system – expect the unexpected. Endocrinology 142, 1377–1379.
| Editorial: the oxytocin/oxytocin receptor system – expect the unexpected.Crossref | GoogleScholarGoogle Scholar |
Chang, WJ, Ying, YS, Rothberg, KG, Hooper, NM, Turner, AJ, Gambliel, HA, De Gunzburg, J, Mumby, SM, Gilman, AG, and Anderson, RG (1994). Purification and characterization of smooth muscle cell caveolae. The Journal of Cell Biology 126, 127–138.
| Purification and characterization of smooth muscle cell caveolae.Crossref | GoogleScholarGoogle Scholar |
Cui, J, Rohr, LR, Swanson, G, Speights, VO, Maxwell, T, and Brothman, AR (2001). Hypermethylation of the caveolin-1 gene promoter in prostate cancer. Prostate 46, 249–256.
Di Vizio, D, Morello, M, Sotgia, F, Pestell, RG, Freeman, MR, and Lisanti, MP (2009). An absence of stromal caveolin-1 is associated with advanced prostate cancer, metastatic disease and epithelial Akt activation. Cell Cycle 8, 2420–2424.
| An absence of stromal caveolin-1 is associated with advanced prostate cancer, metastatic disease and epithelial Akt activation.Crossref | GoogleScholarGoogle Scholar |
Engelman, JA, Wykoff, CC, Yasuhara, S, Song, KS, Okamoto, T, and Lisanti, MP (1997). Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth. Journal of Biological Chemistry 272, 16374–16381.
| Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth.Crossref | GoogleScholarGoogle Scholar |
Engelman, JA, Zhang, XL, Galbiati, F, and Lisanti, MP (1998a). Chromosomal localization, genomic organization, and developmental expression of the murine caveolin gene family (Cav-1, -2, and -3): Cav-1 and Cav-2 genes map to a known tumor suppressor locus (6-a2/7q31). FEBS Letters 429, 330–336.
| Chromosomal localization, genomic organization, and developmental expression of the murine caveolin gene family (Cav-1, -2, and -3): Cav-1 and Cav-2 genes map to a known tumor suppressor locus (6-a2/7q31).Crossref | GoogleScholarGoogle Scholar |
Engelman, JA, Zhang, XL, and Lisanti, MP (1998b). Genes encoding human caveolin-1 and -2 are co-localized to the D7S522 locus (7q31.1), a known fragile site (FRA7G) that is frequently deleted in human cancers. FEBS Letters 436, 403–410.
| Genes encoding human caveolin-1 and -2 are co-localized to the D7S522 locus (7q31.1), a known fragile site (FRA7G) that is frequently deleted in human cancers.Crossref | GoogleScholarGoogle Scholar |
Engelman, JA, Zhang, XL, Razani, B, Pestell, RG, and Lisanti, MP (1999). p42/44 MAP kinase-dependent and -independent signaling pathways regulate caveolin-1 gene expression: activation of Ras-MAP kinase and protein kinase a signaling cascades transcriptionally down-regulates caveolin-1 promoter activity. Journal of Biological Chemistry 274, 32333–32341.
| p42/44 MAP kinase-dependent and -independent signaling pathways regulate caveolin-1 gene expression: activation of Ras-MAP kinase and protein kinase a signaling cascades transcriptionally down-regulates caveolin-1 promoter activity.Crossref | GoogleScholarGoogle Scholar |
Farina-Lipari, E, Lipari, D, Bellafiore, M, Anzalone, R, Cappello, F, and Valentino, B (2003). Presence of atrial natriuretic factor in normal and hyperplastic human prostate and its relationship with oxytocin localisation. European Journal of Histochemistry 47, 133–138.
| Presence of atrial natriuretic factor in normal and hyperplastic human prostate and its relationship with oxytocin localisation.Crossref | GoogleScholarGoogle Scholar |
Fiucci, G, Ravid, D, Reich, R, and Liscovitch, M (2002). Caveolin-1 inhibits anchorage-independent growth, anoikis and invasiveness in MCF-7 human breast cancer cells. Oncogene 21, 2365–2375.
| Caveolin-1 inhibits anchorage-independent growth, anoikis and invasiveness in MCF-7 human breast cancer cells.Crossref | GoogleScholarGoogle Scholar |
Fra, AM, Williamson, E, Simons, K, and Parton, RG (1995). De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proceedings of the National Academy of Sciences of the United States of America 92, 8655–8659.
| De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin.Crossref | GoogleScholarGoogle Scholar |
Friedrich, T, Richter, B, Gaiser, T, Weiss, C, Janssen, K-P, Einwachter, H, Schmid, RM, Ebert, MPA, and Burgermeister, E (2013). Deficiency of caveolin-1 in Apcmin/+ mice promotes colorectal tumorigenesis. Carcinogenesis 34, 2109–2118.
| Deficiency of caveolin-1 in Apcmin/+ mice promotes colorectal tumorigenesis.Crossref | GoogleScholarGoogle Scholar |
Galbiati, F, Volonte, D, Engelman, JA, Watanabe, G, Burk, R, Pestell, RG, and Lisanti, MP (1998). Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. The EMBO Journal 17, 6633–6648.
| Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade.Crossref | GoogleScholarGoogle Scholar |
Galbiati, F, Engelman, JA, Volonte, D, Zhang, XL, Minetti, C, Li, M, Hou, H, Kneitz, B, Edelmann, W, and Lisanti, MP (2001). Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities. Journal of Biological Chemistry 276, 21425–21433.
| Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities.Crossref | GoogleScholarGoogle Scholar |
Garnett, DJ (2016). Caveolae as a target to quench autoinduction of the metastatic phenotype in lung cancer. Journal of Cancer Research and Clinical Oncology 142, 611–618.
| Caveolae as a target to quench autoinduction of the metastatic phenotype in lung cancer.Crossref | GoogleScholarGoogle Scholar |
Gioeli, D, Mandell, JW, Petroni, GR, Frierson, HF, and Weber, MJ (1999). Activation of mitogen-activated protein kinase associated with prostate cancer progression. Cancer Research 59, 279–284.
Gould, ML, and Nicholson, HD (2019). Changes in receptor location affect the ability of oxytocin to stimulate proliferative growth in prostate epithelial cells. Reproduction, Fertility and Development 31, 1166–1179.
| Changes in receptor location affect the ability of oxytocin to stimulate proliferative growth in prostate epithelial cells.Crossref | GoogleScholarGoogle Scholar |
Gould, ML, Williams, G, and Nicholson, HD (2010). Changes in caveolae, caveolin, and polymerase 1 and transcript release factor (PTRF) expression in prostate cancer progression. The Prostate 70, 1609–1621.
| Changes in caveolae, caveolin, and polymerase 1 and transcript release factor (PTRF) expression in prostate cancer progression.Crossref | GoogleScholarGoogle Scholar |
Guzzi, F, Zanchetta, D, Cassoni, P, Guzzi, V, Francolini, M, Parenti, M, and Chini, B (2002). Localization of the human oxytocin receptor in caveolin-1 enriched domains turns the receptor-mediated inhibition of cell growth into a proliferative response. Oncogene 21, 1658–1667.
| Localization of the human oxytocin receptor in caveolin-1 enriched domains turns the receptor-mediated inhibition of cell growth into a proliferative response.Crossref | GoogleScholarGoogle Scholar |
Han, S, Brenner, JC, Sabolch, A, Jackson, W, Speers, C, Wilder-Romans, K, Knudsen, KE, Lawrence, TS, Chinnaiyan, AM, and Feng, FY (2013). Targeted radiosensitization of ETS fusion-positive prostate cancer through PARP1 inhibition. Neoplasia 15, 1207–IN36.
| Targeted radiosensitization of ETS fusion-positive prostate cancer through PARP1 inhibition.Crossref | GoogleScholarGoogle Scholar |
Harris, WP, Mostaghel, EA, Nelson, PS, and Montgomery, B (2009). Androgen deprivation therapy: progress in understanding mechanisms of resistance and optimizing androgen depletion. Nature Clinical Practice Urology 6, 76–85.
| Androgen deprivation therapy: progress in understanding mechanisms of resistance and optimizing androgen depletion.Crossref | GoogleScholarGoogle Scholar |
Hermans, E (2003). Biochemical and pharmacological control of the multiplicity of coupling at G-protein-coupled receptors. Pharmacology & Therapeutics 99, 25–44.
| Biochemical and pharmacological control of the multiplicity of coupling at G-protein-coupled receptors.Crossref | GoogleScholarGoogle Scholar |
Hill, MM, Bastiani, M, Luetterforst, R, Kirkham, M, Kirkham, A, Nixon, SJ, Walser, P, Abankwa, D, Oorschot, VMJ, Martin, S, Hancock, JF, and Parton, RG (2008). PTRF-cavin, a conserved cytoplasmic protein required for caveola formation and function. Cell 132, 113–124.
| PTRF-cavin, a conserved cytoplasmic protein required for caveola formation and function.Crossref | GoogleScholarGoogle Scholar |
Hill, MM, Daud, NH, Aung, CS, Loo, D, Martin, S, Murphy, S, Black, DM, Barry, R, Simpson, F, Liu, L, Pilch, PF, Hancock, JF, Parat, M-O, and Parton, RG (2012). Co-regulation of cell polarization and migration by caveolar proteins PTRF/cavin-1 and caveolin-1. PLoS ONE 7, e43041.
| Co-regulation of cell polarization and migration by caveolar proteins PTRF/cavin-1 and caveolin-1.Crossref | GoogleScholarGoogle Scholar |
Hooper, NM (1999). Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review). Molecular Membrane Biology 16, 145–156.
| Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review).Crossref | GoogleScholarGoogle Scholar |
Huang, C, Qiu, Z, Wang, L, Peng, Z, Jia, Z, Logsdon, CD, Le, X, Wei, D, Huang, S, and Xie, K (2012). A novel foxM1-caveolin signaling pathway promotes pancreatic cancer invasion and metastasis. Cancer Research 72, 655–665.
| A novel foxM1-caveolin signaling pathway promotes pancreatic cancer invasion and metastasis.Crossref | GoogleScholarGoogle Scholar |
Hurlstone, AFL, Reid, G, Reeves, JR, Fraser, J, Strathdee, G, Rahilly, M, Parkinson, EK, and Black, DM (1999). Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines. Oncogene 18, 1881–1890.
| Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines.Crossref | GoogleScholarGoogle Scholar |
Inder, KL, Zheng, YZ, Davis, MJ, Moon, H, Loo, D, Nguyen, H, Clements, JA, Parton, RG, Foster, LJ, and Hill, MM (2012). Expression of PTRF in PC-3 cells modulates cholesterol dynamics and the actin cytoskeleton impacting secretion pathways. Molecular & Cellular Proteomics 11, M111.012245.
| Expression of PTRF in PC-3 cells modulates cholesterol dynamics and the actin cytoskeleton impacting secretion pathways.Crossref | GoogleScholarGoogle Scholar |
Kaplan, DH, Shankaran, V, Dighe, AS, Stockert, E, Aguet, M, Old, LJ, and Schreiber, RD (1998). Demonstration of an interferon γ-dependent tumor surveillance system in immunocompetent mice. Proceedings of the National Academy of Sciences of the United States of America 95, 7556–7561.
| Demonstration of an interferon γ-dependent tumor surveillance system in immunocompetent mice.Crossref | GoogleScholarGoogle Scholar |
Koleske, AJ, Baltimore, D, and Lisanti, MP (1995). Reduction of caveolin and caveolae in oncogenically transformed cells. Proceedings of the National Academy of Sciences of the United States of America 92, 1381–1385.
| Reduction of caveolin and caveolae in oncogenically transformed cells.Crossref | GoogleScholarGoogle Scholar |
Kreisberg, JI, Malik, SN, Prihoda, TJ, Bedolla, RG, Troyer, DA, Kreisberg, S, and Ghosh, PM (2004). Phosphorylation of akt (ser473) is an excellent predictor of poor clinical outcome in prostate cancer. Cancer Research 64, 5232–5236.
| Phosphorylation of akt (ser473) is an excellent predictor of poor clinical outcome in prostate cancer.Crossref | GoogleScholarGoogle Scholar |
Li, S, Couet, J, and Lisanti, MP (1996). Src tyrosine kinases, Gα subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin: caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. Journal of Biological Chemistry 271, 29182–29190.
| Src tyrosine kinases, Gα subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin: caveolin binding negatively regulates the auto-activation of Src tyrosine kinases.Crossref | GoogleScholarGoogle Scholar |
Li, S, Galbiati, F, Volonte, D, Sargiacomo, M, Engelman, JA, Das, K, Scherer, PE, and Lisanti, MP (1998). Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes. FEBS Letters 434, 127–134.
| Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes.Crossref | GoogleScholarGoogle Scholar |
Li, L, Yang, G, Ebara, S, Satoh, T, Nasu, Y, Timme, TL, Ren, C, Wang, J, Tahir, SA, and Thompson, TC (2001). Caveolin-1 mediates testosterone-stimulated survival/clonal growth and promotes metastatic activities in prostate cancer cells. Cancer Research 61, 4386–4392.
Lin, C-J, Yun, E-J, Lo, U-G, Tai, Y-L, Deng, S, Hernandez, E, Dang, A, Chen, Y-A, Saha, D, Mu, P, Lin, H, Li, T-K, Shen, T-L, Lai, C-H, and Hsieh, J-T (2019). The paracrine induction of prostate cancer progression by caveolin-1. Cell Death & Disease 10, 834.
| The paracrine induction of prostate cancer progression by caveolin-1.Crossref | GoogleScholarGoogle Scholar |
Low, J-Y, and Nicholson, HD (2016). The up-stream regulation of polymerase-1 and transcript release factor(PTRF/Cavin-1) in prostate cancer: an epigenetic analysis. AIMS Molecular Science 3, 466–478.
| The up-stream regulation of polymerase-1 and transcript release factor(PTRF/Cavin-1) in prostate cancer: an epigenetic analysis.Crossref | GoogleScholarGoogle Scholar |
Low, J-Y, and Nicholson, HD (2017). Investigating the role of caveolin-2 in prostate cancer cell line. AIMS Molecular Science 4, 82–88.
| Investigating the role of caveolin-2 in prostate cancer cell line.Crossref | GoogleScholarGoogle Scholar |
Mohammed, DA, and Helal, DS (2017). Prognostic significance of epithelial/stromal caveolin-1 expression in prostatic hyperplasia, high grade prostatic intraepithelial hyperplasia and prostatic carcinoma and its correlation with microvessel density. Journal of the Egyptian National Cancer Institute 29, 25–31.
| Prognostic significance of epithelial/stromal caveolin-1 expression in prostatic hyperplasia, high grade prostatic intraepithelial hyperplasia and prostatic carcinoma and its correlation with microvessel density.Crossref | GoogleScholarGoogle Scholar |
Moon, H, Lee, CS, Inder, KL, Sharma, S, Choi, E, Black, DM, Lê Cao, K-A, Winterford, C, Coward, JI, Ling, MT, Australian Prostate Cancer BioResource Craik, DJ, Parton, RG, Russell, PJ, and Hill, MM (2014). PTRF/cavin-1 neutralizes non-caveolar caveolin-1 microdomains in prostate cancer. Oncogene 33, 3561–3570.
| PTRF/cavin-1 neutralizes non-caveolar caveolin-1 microdomains in prostate cancer.Crossref | GoogleScholarGoogle Scholar |
Nasu, Y, Timme, TL, Yang, G, Bangma, CH, Li, L, Ren, C, Park, SH, DeLeon, M, Wang, J, and Thompson, TC (1998). Suppression of caveolin expression induces androgen sensitivity in metastatic androgen-insensitive mouse prostate cancer cells. Nature Medicine 4, 1062–1064.
| Suppression of caveolin expression induces androgen sensitivity in metastatic androgen-insensitive mouse prostate cancer cells.Crossref | GoogleScholarGoogle Scholar |
Nicholson, HD (1996). Oxytocin: a paracrine regulator of prostatic function. Reviews of Reproduction 1, 69–72.
| Oxytocin: a paracrine regulator of prostatic function.Crossref | GoogleScholarGoogle Scholar |
Oh, P, and Schnitzer, JE (2001). Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default. Molecular Biology of the Cell 12, 685–698.
| Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default.Crossref | GoogleScholarGoogle Scholar |
Ostrom, RS, and Insel, PA (2004). The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology. British Journal of Pharmacology 143, 235–245.
| The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology.Crossref | GoogleScholarGoogle Scholar |
Ostrom, RS, Gregorian, C, Drenan, RM, Xiang, Y, Regan, JW, and Insel, PA (2001). Receptor number and caveolar co-localization determine receptor coupling efficiency to adenylyl cyclase. Journal of Biological Chemistry 276, 42063–42069.
| Receptor number and caveolar co-localization determine receptor coupling efficiency to adenylyl cyclase.Crossref | GoogleScholarGoogle Scholar |
Pike, LJ (2003). Lipid rafts: bringing order to chaos. Journal of Lipid Research 44, 655–667.
| Lipid rafts: bringing order to chaos.Crossref | GoogleScholarGoogle Scholar |
Razani, B, Wang, XB, Engelman, JA, Battista, M, Lagaud, G, Zhang, XL, Kneitz, B, Hou, H, Christ, GJ, Edelmann, W, and Lisanti, MP (2002). Caveolin-2-deficient mice show evidence of severe pulmonary dysfunction without disruption of caveolae. Molecular and Cellular Biology 22, 2329–2344.
| Caveolin-2-deficient mice show evidence of severe pulmonary dysfunction without disruption of caveolae.Crossref | GoogleScholarGoogle Scholar |
Rick, FG, Schally, AV, Szalontay, L, Block, NL, Szepeshazi, K, Nadji, M, Zarandi, M, Hohla, F, Buchholz, S, and Seitz, S (2012). Antagonists of growth hormone-releasing hormone inhibit growth of androgen-independent prostate cancer through inactivation of ERK and Akt kinases. Proceedings of the National Academy of Sciences of the United States of America 109, 1655–1660.
| Antagonists of growth hormone-releasing hormone inhibit growth of androgen-independent prostate cancer through inactivation of ERK and Akt kinases.Crossref | GoogleScholarGoogle Scholar |
Rimoldi, V, Reversi, A, Taverna, E, Rosa, P, Francolini, M, Cassoni, P, Parenti, M, and Chini, B (2003). Oxytocin receptor elicits different EGFR/MAPK activation patterns depending on its localization in caveolin-1 enriched domains. Oncogene 22, 6054–6060.
| Oxytocin receptor elicits different EGFR/MAPK activation patterns depending on its localization in caveolin-1 enriched domains.Crossref | GoogleScholarGoogle Scholar |
Rybin, VO, Xu, X, Lisanti, MP, and Steinberg, SF (2000). Differential targeting of β-adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae. A mechanism to functionally regulate the camp signaling pathway. Journal of Biological Chemistry 275, 41447–41457.
| Differential targeting of β-adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae. A mechanism to functionally regulate the camp signaling pathway.Crossref | GoogleScholarGoogle Scholar |
Sargiacomo, M, Scherer, PE, Tang, Z, Kubler, E, Song, KS, Sanders, MC, and Lisanti, MP (1995). Oligomeric structure of caveolin: implications for caveolae membrane organization. Proceedings of the National Academy of Sciences of the United States of America 92, 9407–9411.
| Oligomeric structure of caveolin: implications for caveolae membrane organization.Crossref | GoogleScholarGoogle Scholar |
Scherer, PE, Okamoto, T, Chun, M, Nishimoto, I, Lodish, HF, and Lisanti, MP (1996). Identification, sequence, and expression of caveolin-2 defines a caveolin gene family. Proceedings of the National Academy of Sciences of the United States of America 93, 131–135.
| Identification, sequence, and expression of caveolin-2 defines a caveolin gene family.Crossref | GoogleScholarGoogle Scholar |
Scherer, PE, Lewis, RY, Volonte, D, Engelman, JA, Galbiati, F, Couet, J, Kohtz, DS, van Donselaar, E, Peters, P, and Lisanti, MP (1997). Cell-type and tissue-specific expression of caveolin-2: caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo. Journal of Biological Chemistry 272, 29337–29346.
| Cell-type and tissue-specific expression of caveolin-2: caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo.Crossref | GoogleScholarGoogle Scholar |
Shen, X-J, Zhang, H, Tang, G-S, Wang, X-D, Zheng, R, Wang, Y, Zhu, Y, Xue, X-C, and Bi, J-W (2015). Caveolin-1 is a modulator of fibroblast activation and a potential biomarker for gastric cancer. International Journal of Biological Sciences 11, 370–379.
| Caveolin-1 is a modulator of fibroblast activation and a potential biomarker for gastric cancer.Crossref | GoogleScholarGoogle Scholar |
Simpkins, SA, Hanby, AM, Holliday, DL, and Speirs, V (2012). Clinical and functional significance of loss of caveolin-1 expression in breast cancer-associated fibroblasts. The Journal of Pathology 227, 490–498.
| Clinical and functional significance of loss of caveolin-1 expression in breast cancer-associated fibroblasts.Crossref | GoogleScholarGoogle Scholar |
Smith, AJ, Karpova, Y, D’Agostino, R, Willingham, M, and Kulik, G (2009). Expression of the Bcl-2 protein BAD promotes prostate cancer growth. PLoS ONE 4, e6224.
| Expression of the Bcl-2 protein BAD promotes prostate cancer growth.Crossref | GoogleScholarGoogle Scholar |
Song, KS, Scherer, PE, Tang, ZL, Okamoto, T, Li, S, Chafel, M, Chu, C, Kohtz, DS, and Lisanti, MP (1996). Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells: caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. Journal of Biological Chemistry 271, 15160–15165.
| Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells: caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins.Crossref | GoogleScholarGoogle Scholar |
Steffens, S, Schrader, AJ, Blasig, H, Vetter, G, Eggers, H, Trankenschuh, W, Kuczyk, MA, and Serth, J (2011). Caveolin 1 protein expression in renal cell carcinoma predicts survival. BMC Urology 11, 25.
| Caveolin 1 protein expression in renal cell carcinoma predicts survival.Crossref | GoogleScholarGoogle Scholar |
Steiner, I, Jung, K, Miller, K, Stephan, C, and Erbersdobler, A (2012). Expression of endothelial factors in prostate cancer: a possible role of caveolin-1 for tumour progression. Oncology Reports 27, 389–395.
| Expression of endothelial factors in prostate cancer: a possible role of caveolin-1 for tumour progression.Crossref | GoogleScholarGoogle Scholar |
Tahir, SA, Ren, C, Timme, TL, Gdor, Y, Hoogeveen, R, Morrisett, JD, Frolov, A, Ayala, G, Wheeler, TM, and Thompson, TC (2003). Development of an immunoassay for serum caveolin-1: a novel biomarker for prostate cancer. Clinical Cancer Research 9, 3653–3659.
Tang, ZL, Scherer, PE, Okamoto, T, Song, K, Chu, C, Kohtz, DS, Nishimoto, I, Lodish, HF, and Lisanti, MP (1996). Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. Journal of Biological Chemistry 271, 2255–2261.
| Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle.Crossref | GoogleScholarGoogle Scholar |
Tikhomirov, O, and Carpenter, G (2004). Ligand-induced, p38-dependent apoptosis in cells expressing high levels of epidermal growth factor receptor and ErbB-2. Journal of Biological Chemistry 279, 12988–12996.
| Ligand-induced, p38-dependent apoptosis in cells expressing high levels of epidermal growth factor receptor and ErbB-2.Crossref | GoogleScholarGoogle Scholar |
Ting Tse, EY, Fat Ko, FC, Kwan Tung, EK, Chan, LK, Wah Lee, TK, Wai Ngan, ES, Man, K, Tsai Wong, AS, Ng, IO-L, and Ping Yam, JW (2012). Caveolin-1 overexpression is associated with hepatocellular carcinoma tumourigenesis and metastasis. The Journal of Pathology 226, 645–653.
| Caveolin-1 overexpression is associated with hepatocellular carcinoma tumourigenesis and metastasis.Crossref | GoogleScholarGoogle Scholar |
Wang, S, Zhang, C, Liu, Y, Xu, C, and Chen, Z (2014). Functional polymorphisms of caveolin-1 variants as potential biomarkers of esophageal squamous cell carcinoma. Biomarkers 19, 652–659.
| Functional polymorphisms of caveolin-1 variants as potential biomarkers of esophageal squamous cell carcinoma.Crossref | GoogleScholarGoogle Scholar |
Wang, X, Liu, Z, and Yang, Z (2018). Expression and clinical significance of caveolin-1 in prostate cancer after transurethral surgery. BMC Urology 18, 102.
| Expression and clinical significance of caveolin-1 in prostate cancer after transurethral surgery.Crossref | GoogleScholarGoogle Scholar |
Whittington, K, Assinder, S, Gould, M, and Nicholson, H (2004). Oxytocin, oxytocin-associated neurophysin and the oxytocin receptor in the human prostate. Cell and Tissue Research 318, 375–382.
| Oxytocin, oxytocin-associated neurophysin and the oxytocin receptor in the human prostate.Crossref | GoogleScholarGoogle Scholar |
Whittington, K, Connors, B, King, K, Assinder, S, Hogarth, K, and Nicholson, H (2007). The effect of oxytocin on cell proliferation in the human prostate is modulated by gonadal steroids: implications for benign prostatic hyperplasia and carcinoma of the prostate. The Prostate 67, 1132–1142.
| The effect of oxytocin on cell proliferation in the human prostate is modulated by gonadal steroids: implications for benign prostatic hyperplasia and carcinoma of the prostate.Crossref | GoogleScholarGoogle Scholar |
Williams, TM, and Lisanti, MP (2005). Caveolin-1 in oncogenic transformation, cancer, and metastasis. American Journal of Physiology-Cell Physiology 288, C494–C506.
| Caveolin-1 in oncogenic transformation, cancer, and metastasis.Crossref | GoogleScholarGoogle Scholar |
Xu, J, Agyemang, S, Qin, Y, Aysola, K, Giles, M, Oprea, G, O’Regan, RM, Partridge, EE, Harris-Hooker, S, Rice, VM, Reddy, ES, and Rao, VN (2014). A novel pathway that links caveolin-1 down-regulation to BRCA1 dysfunction in serous epithelial ovarian cancer cells. Challenges in Cancer Detection and Therapy 1, 004.
Xu, H, Fu, S, Chen, Q, Gu, M, Zhou, J, Liu, C, Chen, Y, and Wang, Z (2017). The function of oxytocin: a potential biomarker for prostate cancer diagnosis and promoter of prostate cancer. Oncotarget 8, 31215–31226.
| The function of oxytocin: a potential biomarker for prostate cancer diagnosis and promoter of prostate cancer.Crossref | GoogleScholarGoogle Scholar |
Yang, G, Truong, LD, Timme, TL, Ren, C, Wheeler, TM, Park, SH, Nasu, Y, Bangma, CH, Kattan, MW, Scardino, PT, and Thompson, TC (1998). Elevated expression of caveolin is associated with prostate and breast cancer. Clinical Cancer Research 4, 1873–1880.
Yeh, S, Miyamoto, H, Nishimura, K, Kang, H, Ludlow, J, Hsiao, P, Wang, C, Su, C, and Chang, C (1998). Retinoblastoma, a tumor suppressor, is a coactivator for the androgen receptor in human prostate cancer DU145 cells. Biochemical and Biophysical Research Communications 248, 361–367.
| Retinoblastoma, a tumor suppressor, is a coactivator for the androgen receptor in human prostate cancer DU145 cells.Crossref | GoogleScholarGoogle Scholar |
Zenklusen, JC, Thompson, JC, Troncoso, P, Kagan, J, and Conti, CJ (1994). Loss of heterozygosity in human primary prostate carcinomas: a possible tumor suppressor gene at 7q31.1. Cancer Research 54, 6370–6373.
