Journal articles: 'DAB2IP'

1

Liu, Liang, Cong Xu, Jer-Tsong Hsieh, Jianping Gong, and Daxing Xie. "DAB2IP in cancer." Oncotarget 7, no. 4 (December 8, 2015): 3766–76. http://dx.doi.org/10.18632/oncotarget.6501.

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Sun, Liang, Yizhou Yao, Ting Lu, Zengfu Shang, Shenghua Zhan, Weiqiang Shi, Guofeng Pan, Xinguo Zhu, and Songbing He. "DAB2IP Downregulation Enhances the Proliferation and Metastasis of Human Gastric Cancer Cells by Derepressing the ERK1/2 Pathway." Gastroenterology Research and Practice 2018 (March 21, 2018): 1–10. http://dx.doi.org/10.1155/2018/2968252.

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DAB2IP (DOC2/DAB2 interactive protein) is downregulated in several cancer types, and its downregulation is involved in tumor cell proliferation, apoptosis, metastasis, and epithelial-mesenchymal transition (EMT). We aimed to investigate the potential role of DAB2IP in the development and progression of gastric cancer. DAB2IP levels were analyzed in human gastric cancer and adjacent normal tissues by Western blots and immunohistochemistry. Potential roles of DAB2IP in regulating gastric cancer cell growth and metastasis were examined by genetic manipulation in vitro. The molecular signaling was determined to understand the mechanisms of observed DAB2IP effects. DAB2IP level is lower in gastric cancer tissues as compared to paired normal tissues. Knockdown of DAB2IP enhanced gastric cancer cell growth and metastasis in vitro and promoted EMT progress at both protein and mRNA levels. Silencing DAB2IP activated extracellular signal-regulated kinase 1/2 (ERK1/2) pathway, and the enhanced proliferation and migration ability induced by DAB2IP knockdown were reduced after incubation with U0126 in SGC7901 gastric cancer cells. Inhibition of DAB2IP enhances gastric cancer cell growth and metastasis through targeting the ERK1/2 signaling, indicating that it may serve as a potential target for treatment of gastric cancer.

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Yu, Lan, Yue Lang, Ching-Cheng Hsu, Wei-Min Chen, Jui-Chung Chiang, Jer-Tsong Hsieh, Michael D. Story, Zeng-Fu Shang, Benjamin P. C. Chen, and Debabrata Saha. "Mitotic phosphorylation of tumor suppressor DAB2IP maintains spindle assembly checkpoint and chromosomal stability through activating PLK1-Mps1 signal pathway and stabilizing mitotic checkpoint complex." Oncogene 41, no. 4 (November 13, 2021): 489–501. http://dx.doi.org/10.1038/s41388-021-02106-8.

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AbstractChromosomal instability (CIN) is a driving force for cancer development. The most common causes of CIN include the dysregulation of the spindle assembly checkpoint (SAC), which is a surveillance mechanism that prevents premature chromosome separation during mitosis by targeting anaphase-promoting complex/cyclosome (APC/C). DAB2IP is frequently silenced in advanced prostate cancer (PCa) and is associated with aggressive phenotypes of PCa. Our previous study showed that DAB2IP activates PLK1 and functions in mitotic regulation. Here, we report the novel mitotic phosphorylation of DAB2IP by Cdks, which mediates DAB2IP’s interaction with PLK1 and the activation of the PLK1-Mps1 pathway. DAB2IP interacts with Cdc20 in a phosphorylation-independent manner. However, the phosphorylation of DAB2IP inhibits the ubiquitylation of Cdc20 in response to SAC, and blocks the premature release of the APC/C-MCC. The PLK1-Mps1 pathway plays an important role in mitotic checkpoint complex (MCC) assembly. It is likely that DAB2IP acts as a scaffold to aid PLK1-Mps1 in targeting Cdc20. Depletion or loss of the Cdks-mediated phosphorylation of DAB2IP destabilizes the MCC, impairs the SAC, and increases chromosome missegregation and subsequent CIN, thus contributing to tumorigenesis. Collectively, these results demonstrate the mechanism of DAB2IP in SAC regulation and provide a rationale for targeting the SAC to cause lethal CIN against DAB2IP-deficient aggressive PCa, which exhibits a weak SAC.

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Qiao, Shuhong, and Ramin Homayouni. "Dab2IP Regulates Neuronal Positioning, Rap1 Activity and Integrin Signaling in the Developing Cortex." Developmental Neuroscience 37, no. 2 (2015): 131–41. http://dx.doi.org/10.1159/000369092.

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Dab2IP (DOC-2/DAB2 interacting protein) is a GTPase-activating protein which is involved in various aspects of brain development in addition to its roles in tumor formation and apoptosis in other systems. In this study, we carefully examined the expression profile of Dab2IP and investigated its physiological role during brain development using a Dab2IP-knockdown (KD) mouse model created by retroviral insertion of a LacZ-encoding gene-trapping cassette. LacZ staining revealed that Dab2IP is expressed in the ventricular zone as well as the cortical plate and the intermediate zone. Immunohistochemical analysis showed that Dab2IP protein is localized in the leading process and proximal cytoplasmic regions of migrating neurons in the intermediate zone. Bromodeoxyuridine birth dating experiments in combination with immunohistochemical analysis using layer-specific markers showed that Dab2IP is important for proper positioning of a subset of layer II-IV neurons in the developing cortex. Notably, neuronal migration was not completely disrupted in the cerebral cortex of Dab2IP-KD mice and disruption of migration was not strictly layer specific. Previously, we found that Dab2IP regulates multipolar transition in cortical neurons. Others have shown that Rap1 regulates the transition from multipolar to bipolar morphology in migrating postmitotic neurons through N-cadherin signaling and somal translocation in the superficial layer of the cortical plate through integrin signaling. Therefore, we examined whether Rap1 and integrin signaling were affected in Dab2IP-KD brains. We found that Dab2IP-KD resulted in higher levels of activated Rap1 and integrin in the developing cortex. Taken together, our results suggest that Dab2IP plays an important role in the migration and positioning of a subpopulation of later-born (layers II-IV) neurons, likely through the regulation of Rap1 and integrin signaling.

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Duan, Yifan, Xiaoyu Yin, Xiaorong Lai, Chao Liu, Wenjing Nie, Dongfeng Li, Zijun Xie, Zijun Li, and Fan Meng. "Upregulation of DAB2IP Inhibits Ras Activity and Tumorigenesis in Human Pancreatic Cancer Cells." Technology in Cancer Research & Treatment 19 (January 1, 2020): 153303381989549. http://dx.doi.org/10.1177/1533033819895494.

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KRAS mutation-induced Ras activation plays an important role in the pathogenesis of pancreatic cancer, but the role of wild-type Ras and Ras GTPase-activating proteins remains unclear. The present study was designed to determine the expression spectra of Ras GTPase-activating proteins genes in pancreatic cancer cells, and the role of DAB2IP, a Ras GTPase-activating proteins gene, in the development and progression of pancreatic cancer. Following the analyses of the expression profiles of 16 Ras GTPase-activating proteins in 6 pancreatic cancer cell lines including Bxpc-3 (with wild-type KRAS), Capan-2, Sw1990, Aspc-1, CFPAC-1, and Panc-1 (with mutant KRAS) and 1 normal human pancreatic ductal epithelial cell line, H6C7, the expression of DAB2IP messenger RNA was further analyzed by quantitative real-time polymerase chain reaction. The role of DAB2IP in pancreatic cancer was further investigated in vitro and in vivo by upregulating DAB2IP in Bxpc-3 cells through transfection of DAB2IP into Bxpc-3 cells with recombinant lentivirus. The DAB2IP expression in pancreatic cancer cells and tissues with wild-type KRAS was significantly lower than that in cells and tissues with mutant KRAS ( P < .05). In Bxpc-3 cells with wild-type KRAS, overexpression of DAB2IP decreased the expression of P-AKT and P-ERK and the Ras activity; increased the expression of P-JNK and caspase 3; inhibited cell proliferation, invasiveness, and migration; and increased the cell sensitivity to cetuximab. Overexpression of DAB2IP inhibited tumor progression in a mouse model. In conclusion, DAB2IP downregulates Ras activity in wild-type pancreatic cancer cells. Overexpression of DAB2IP decreases the Ras activity, inhibits cell proliferation, and increases sensitivity to cetuximab in wild-type pancreatic cancer cells. In conclusion, DAB2IP may serve as a potential molecular therapeutic target for the treatment of pancreatic cancer.

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Xu, He, Dapeng Wei, Jianxin Xue, and Lijuan Hu. "A Novel Monoclonal Antibody Against Human DAB2IP." Monoclonal Antibodies in Immunodiagnosis and Immunotherapy 34, no. 4 (August 2015): 251–56. http://dx.doi.org/10.1089/mab.2015.0011.

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Perurena, Naiara, Natalie Pilla, Amy Schade, Marina Watanabe, Patrick Loi, Carrie L. Rodriguez, Alycia M. Gardner, and Karen Cichowski. "Abstract P1-13-06: Loss of emerging tumor and metastasis suppressor RasGAPs mediates therapeutic resistance in HER2+ breast cancer." Cancer Research 83, no. 5_Supplement (March 1, 2023): P1–13–06—P1–13–06. http://dx.doi.org/10.1158/1538-7445.sabcs22-p1-13-06.

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Abstract Resistance to HER2 inhibitors remains a clinical challenge in HER2+ breast cancer. Therefore, there is an urgent need to 1) understand the mechanisms that underlie resistance to these current treatments and 2) develop improved, and more importantly, curative combination therapies. We recently discovered that two emerging tumor suppressor RasGAPs, DAB2IP and RASAL2, cooperatively drive metastatic breast cancer when lost or inactivated. Interestingly, we have now generated robust data demonstrating that the loss of these RasGAPs also induces resistance to HER2 inhibitors in breast cancer. First, we genetically ablated both RASAL2 and DAB2IP in multiple HER2+ breast cancer cell lines (SKBR3, EFM192A, SUM190, BT474) and performed manual counting experiments after 6 days of TKI (lapatinib, tucatinib) treatment. In all cell lines, RASAL2/DAB2IP knockdown conferred resistance to HER2 inhibitors. Moreover, loss of these RasGAPs prevented TKI-induced caspase-3/7 activation, measured by Incucyte live cell imaging, and enabled the regrowth of cells in long-term 10-day treatment and drug washout experiments, monitored by Incucyte or crystal violet staining. Next, we sought to investigate the individual contribution of each RasGAP to these phenotypes. Surprisingly, we found that RASAL2 and DAB2IP functioned quite differently in this context. Specifically, while RASAL2 loss prevented apoptosis, DAB2IP loss prevented irreversible cell cycle arrest (measured by functional long-term experiments and EdU staining assays). Mechanistically, RASAL2 loss uniquely impaired BIM induction at both mRNA and protein levels, which is required for lapatinib-induced cell death of HER2+ cancer cells. By contrast, cell cycle progression pathways were uniquely enriched in DAB2IP-deficient cells on lapatinib treatment and immunoblots revealed higher residual levels of pRb and low levels of p27 in these cells. These data suggest that RASAL2 and DAB2IP (loss) mediate resistance to HER2 inhibitors by differentially deregulating unique pathways/phenotypes. We next evaluated the relevance of these findings in a SUM190 orthotopic xenograft model. Importantly, while control tumors (expressing both RASAL2 and DAB2IP) regressed upon lapatinib treatment, DAB2IP- and RASAL2-deficient tumors did not regress and grew with kinetics comparable to vehicle-treated tumors after few days on treatment. These data suggest that the unique phenotypes/pathways induced by both RASAL2 and DAB2IP are important mediators of resistance to HER2 inhibitors. Further understanding the contribution of these pathways to anti-HER2 resistance and determining how RASAL2 and DAB2IP differentially function will be essential for developing effective therapeutic strategies to bypass each type of resistance. Citation Format: Naiara Perurena, Natalie Pilla, Amy Schade, Marina Watanabe, Patrick Loi, Carrie L. Rodriguez, Alycia M. Gardner, Karen Cichowski. Loss of emerging tumor and metastasis suppressor RasGAPs mediates therapeutic resistance in HER2+ breast cancer [abstract]. In: Proceedings of the 2022 San Antonio Breast Cancer Symposium; 2022 Dec 6-10; San Antonio, TX. Philadelphia (PA): AACR; Cancer Res 2023;83(5 Suppl):Abstract nr P1-13-06.

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Su, Yintao, Fangyuan Shi, Zhanzhuang Zeng, Xiuling Wu, Yanhe Zhao, Lei Zhang, Zuofu Xie, and Yunkun Wu. "A Versatile Monoclonal Antibody Specific Against Human DAB2IP." Monoclonal Antibodies in Immunodiagnosis and Immunotherapy 34, no. 4 (August 2015): 246–50. http://dx.doi.org/10.1089/mab.2015.0012.

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9

Dai, Xiangpeng, Brian J. North, and Hiroyuki Inuzuka. "Negative regulation of DAB2IP by Akt and SCFFbw7 pathways." Oncotarget 5, no. 10 (May 1, 2014): 3307–15. http://dx.doi.org/10.18632/oncotarget.1939.

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10

Liu, S., N. Zhu, and H. Chen. "Expression patterns of human DAB2IP protein in fetal tissues." Biotechnic & Histochemistry 87, no. 5 (March 12, 2012): 350–59. http://dx.doi.org/10.3109/10520295.2012.664658.

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Li, Xiaoning, Xiangpeng Dai, Lixin Wan, Hiroyuki Inuzuka, Liankun Sun, and Brian J. North. "Smurf1 regulation of DAB2IP controls cell proliferation and migration." Oncotarget 7, no. 18 (March 27, 2016): 26057–69. http://dx.doi.org/10.18632/oncotarget.8424.

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12

Lin, Chun-Jung, Andrew Dang, Elizabeth Hernandez, and Jer-Tsong Hsieh. "DAB2IP modulates primary cilia formation associated with renal tumorigenesis." Neoplasia 23, no. 1 (January 2021): 169–80. http://dx.doi.org/10.1016/j.neo.2020.12.002.

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13

Harrell Stewart, Desmond R., M. Lee Schmidt, Howard Donninger, and Geoffrey J. Clark. "The RASSF1A Tumor Suppressor Binds the RasGAP DAB2IP and Modulates RAS Activation in Lung Cancer." Cancers 12, no. 12 (December 17, 2020): 3807. http://dx.doi.org/10.3390/cancers12123807.

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Lung cancer is the leading cause of cancer-related death worldwide. Lung cancer is commonly driven by mutations in the RAS oncogenes, the most frequently activated oncogene family in human disease. RAS-induced tumorigenesis is inhibited by the tumor suppressor RASSF1A, which induces apoptosis in response to hyperactivation of RAS. RASSF1A expression is suppressed in cancer at high rates, primarily owing to promoter hypermethylation. Recent reports have shown that loss of RASSF1A expression uncouples RAS from apoptotic signaling in vivo, thereby enhancing tumor aggressiveness. Moreover, a concomitant upregulation of RAS mitogenic signaling upon RASSF1A loss has been observed, suggesting RASSF1A may directly regulate RAS activation. Here, we present the first mechanistic evidence for control of RAS activation by RASSF1A. We present a novel interaction between RASSF1A and the Ras GTPase Activating Protein (RasGAP) DAB2IP, an important negative regulator of RAS. Using shRNA-mediated knockdown and stable overexpression approaches, we demonstrate that RASSF1A upregulates DAB2IP protein levels in NSCLC cells. Suppression of RASSF1A and subsequent downregulation of DAB2IP enhances GTP loading onto RAS, thus increasing RAS mitogenic signaling in both mutant- and wildtype-RAS cells. Moreover, co-suppression of RASSF1A and DAB2IP significantly enhances in vitro and in vivo growth of wildtype-RAS cells. Tumors expressing wildtype RAS, therefore, may still suffer from hyperactive RAS signaling when RASSF1A is downregulated. This may render them susceptible to the targeted RAS inhibitors currently in development.

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14

Wu, Kaijie, Daxing Xie, Yonglong Zou, Tingting Zhang, Rey-Chen Pong, Guanghua Xiao, Ladan Fazli, et al. "The Mechanism of DAB2IP in Chemoresistance of Prostate Cancer Cells." Clinical Cancer Research 19, no. 17 (July 9, 2013): 4740–49. http://dx.doi.org/10.1158/1078-0432.ccr-13-0954.

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Xiao, Tian, Junchao Xue, Ming Shi, Chao Chen, Fei Luo, Hui Xu, Xiong Chen, et al. "Circ008913,viamiR-889 regulation of DAB2IP/ZEB1, is involved in the arsenite-induced acquisition of CSC-like properties by human keratinocytes in carcinogenesis." Metallomics 10, no. 9 (2018): 1328–38. http://dx.doi.org/10.1039/c8mt00207j.

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Bellazzo, Arianna, Giulio Di Minin, and Licio Collavin. "Block one, unleash a hundred. Mechanisms of DAB2IP inactivation in cancer." Cell Death & Differentiation 24, no. 1 (November 18, 2016): 15–25. http://dx.doi.org/10.1038/cdd.2016.134.

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Lee, Gum Hwa, Sun Hong Kim, Ramin Homayouni, and Gabriella D'Arcangelo. "Dab2ip Regulates Neuronal Migration and Neurite Outgrowth in the Developing Neocortex." PLoS ONE 7, no. 10 (October 4, 2012): e46592. http://dx.doi.org/10.1371/journal.pone.0046592.

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Harrison, Seamus C., Jackie A. Cooper, Kawah Li, Phillipa J. Talmud, Reecha Sofat, Jeffery W. Stephens, Anders Hamsten, et al. "Association of a sequence variant in DAB2IP with coronary heart disease." European Heart Journal 33, no. 7 (March 28, 2011): 881–88. http://dx.doi.org/10.1093/eurheartj/ehr075.

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Duan, Yi-Fan, Dong-Feng Li, Yan-Hui Liu, Ping Mei, Yu-Xuan Qin, Liang-Fang Li, Qiu-Xiong Lin, and Zi-Jun Li. "Decreased expression of DAB2IP in pancreatic cancer with wild-type KRAS." Hepatobiliary & Pancreatic Diseases International 12, no. 2 (April 2013): 204–9. http://dx.doi.org/10.1016/s1499-3872(13)60032-6.

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Son, Hyun Ji, Yun Sol Jo, Min Sung Kim, Nam Jin Yoo, and Sug Hyung Lee. "DAB2IP with tumor-inhibiting activities exhibits frameshift mutations in gastrointestinal cancers." Pathology - Research and Practice 214, no. 12 (December 2018): 2075–80. http://dx.doi.org/10.1016/j.prp.2018.10.005.

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Xu, Yanting, Jiangtu He, Yue Wang, Xinyi Zhu, Qiuhui Pan, Qiuling Xie, and Fenyong Sun. "miR-889 promotes proliferation of esophageal squamous cell carcinomas through DAB2IP." FEBS Letters 589, no. 10 (April 1, 2015): 1127–35. http://dx.doi.org/10.1016/j.febslet.2015.03.027.

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Zheng, Linfeng, Kaiyan Chen, Liang Zhu, Dan Su, and Guoping Cheng. "Low expression of DAB2IP predicts an unfavorable prognosis in human bladder carcinoma." OncoTargets and Therapy Volume 10 (November 2017): 5719–26. http://dx.doi.org/10.2147/ott.s146952.

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Bellazzo, Arianna, and Licio Collavin. "A mechanism for cell non-autonomous inactivation of the tumor suppressor DAB2IP." Oncoscience 5, no. 5-6 (June 29, 2018): 177–78. http://dx.doi.org/10.18632/oncoscience.441.

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Zhou, Yunjiao, Zhenwei Yang, Hailin Zhang, Haiou Li, Meng Zhang, Haizhou Wang, Mengna Zhang, Peishan Qiu, Ruike Zhang, and Jing Liu. "DNMT3A facilitates colorectal cancer progression via regulating DAB2IP mediated MEK/ERK activation." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1868, no. 4 (April 2022): 166353. http://dx.doi.org/10.1016/j.bbadis.2022.166353.

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Shan, Nan, Xiaoqiu Xiao, Ying Chen, Xin Luo, Nanlin Yin, Qinyin Deng, and Hongbo Qi. "Expression of DAB2IP in human trophoblast and its role in trophoblast invasion." Journal of Maternal-Fetal & Neonatal Medicine 29, no. 3 (January 21, 2015): 393–99. http://dx.doi.org/10.3109/14767058.2014.1001974.

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Wu, K., J. Liu, S.-F. Tseng, C. Gore, Z. Ning, N. Sharifi, L. Fazli, et al. "The role of DAB2IP in androgen receptor activation during prostate cancer progression." Oncogene 33, no. 15 (April 22, 2013): 1954–63. http://dx.doi.org/10.1038/onc.2013.143.

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Jacobs, Corbin, Vasu Tumati, Payal Kapur, Raquibul Hannan, Jer-Tsong Hsieh, Dong W. Kim, and Debabrata Saha. "Association of decreased tumor DAB2IP and high-risk prostate cancer-specific survival." Journal of Clinical Oncology 34, no. 15_suppl (May 20, 2016): e16553-e16553. http://dx.doi.org/10.1200/jco.2016.34.15_suppl.e16553.

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Qiao, Shuhong, Sun-Hong Kim, Detlef Heck, Daniel Goldowitz, Mark S. LeDoux, and Ramin Homayouni. "Dab2IP GTPase Activating Protein Regulates Dendrite Development and Synapse Number in Cerebellum." PLoS ONE 8, no. 1 (January 9, 2013): e53635. http://dx.doi.org/10.1371/journal.pone.0053635.

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Salami, Farimah, Shuhong Qiao, and Ramin Homayouni. "Expression of mouse Dab2ip transcript variants and gene methylation during brain development." Gene 568, no. 1 (August 2015): 19–24. http://dx.doi.org/10.1016/j.gene.2015.05.012.

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Wang, Guannan, Xu Wang, Meng Han, and Xiaoming Wang. "Loss of DAB2IP Contributes to Cell Proliferation and Cisplatin Resistance in Gastric Cancer." OncoTargets and Therapy Volume 14 (February 2021): 979–88. http://dx.doi.org/10.2147/ott.s289722.

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Luo, Xiaomin, Chunman Li, Ran Tan, Xiaohui Xu, William K. K. Wu, Ayano Satoh, Tuanlao Wang, and Sidney Yu. "A RasGAP, DAB2IP, regulates lipid droplet homeostasis by serving as GAP toward RAB40C." Oncotarget 8, no. 49 (August 3, 2017): 85415–27. http://dx.doi.org/10.18632/oncotarget.19960.

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Zhang, Tingting, Yijun Shen, Ying Chen, Jer-Tsong Hsieh, and Zhaolu Kong. "The ATM inhibitor KU55933 sensitizes radioresistant bladder cancer cells with DAB2IP gene defect." International Journal of Radiation Biology 91, no. 4 (February 6, 2015): 368–78. http://dx.doi.org/10.3109/09553002.2015.1001531.

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Feng, Shengjie, Qingwen Huang, Jiao Deng, Weiyi Jia, Jianping Gong, Daxing Xie, Jie Shen, and Liang Liu. "DAB2IP suppresses tumor malignancy by inhibiting GRP75-driven p53 ubiquitination in colon cancer." Cancer Letters 532 (April 2022): 215588. http://dx.doi.org/10.1016/j.canlet.2022.215588.

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Xie, D., C. Gore, J. Liu, R. C. Pong, R. Mason, G. Hao, M. Long, et al. "Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis." Proceedings of the National Academy of Sciences 107, no. 6 (January 13, 2010): 2485–90. http://dx.doi.org/10.1073/pnas.0908133107.

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Xie, D., C. Gore, J. Zhou, R. C. Pong, H. Zhang, L. Yu, R. L. Vessella, W. Min, and J. T. Hsieh. "DAB2IP coordinates both PI3K-Akt and ASK1 pathways for cell survival and apoptosis." Proceedings of the National Academy of Sciences 106, no. 47 (November 10, 2009): 19878–83. http://dx.doi.org/10.1073/pnas.0908458106.

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Homayouni, Ramin, Susan Magdaleno, Lakhu Keshvara, Dennis S. Rice, and Tom Curran. "Interaction of Disabled-1 and the GTPase activating protein Dab2IP in mouse brain." Molecular Brain Research 115, no. 2 (July 2003): 121–29. http://dx.doi.org/10.1016/s0169-328x(03)00176-1.

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Qiao, Shuhong, Farimah Salami, and Ramin Homayouni. "ISDN2014_0390: REMOVED: Dab2IP regulates neuronal migration and Rap1 activity in the developing cortex." International Journal of Developmental Neuroscience 47, Part_A (December 2015): 115. http://dx.doi.org/10.1016/j.ijdevneu.2015.04.310.

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Huang, Jun, Bin Wang, Ke Hui, Jin Zeng, Jinhai Fan, Xinyang Wang, Jer-Tsong Hsieh, Dalin He, and Kaijie Wu. "miR-92b targets DAB2IP to promote EMT in bladder cancer migration and invasion." Oncology Reports 36, no. 3 (July 15, 2016): 1693–701. http://dx.doi.org/10.3892/or.2016.4940.

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Zong, Xingyue, Weini Wang, Ali Ozes, Fang Fang, George E. Sandusky, and Kenneth P. Nephew. "EZH2-Mediated Downregulation of the Tumor Suppressor DAB2IP Maintains Ovarian Cancer Stem Cells." Cancer Research 80, no. 20 (August 19, 2020): 4371–85. http://dx.doi.org/10.1158/0008-5472.can-20-0458.

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Samadaian, Niusha, Pouya Salehipour, Mohsen Ayati, Naser Rakhshani, Ali Najafi, Mandana Afsharpad, Fatemeh Yazarlou, and Mohammad Hossein Modarressi. "A potential clinical significance of DAB2IP and SPRY2 transcript variants in prostate cancer." Pathology - Research and Practice 214, no. 12 (December 2018): 2018–24. http://dx.doi.org/10.1016/j.prp.2018.09.019.

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Peng, Chih-Yu, Che-Yi Lin, Szu-Han Chen, Yi-Wen Liao, Cheng-Chia Yu, and Shiao-Pieng Lee. "microRNA-1266-5p directly targets DAB2IP to enhance oncogenicity and metastasis in oral cancer." Journal of Dental Sciences 17, no. 2 (April 2022): 718–24. http://dx.doi.org/10.1016/j.jds.2021.11.001.

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LEGAKI, EVANGELIA, CHRISTOS KLONARIS, DIMITRIOS ATHANASIADIS, NIKOLAOS PATELIS, ANNA SIOZIOU, THEODOROS LIAKAKOS, and MARIA GAZOULI. "DAB2IP Expression in Abdominal Aortic Aneurysm: EZH2 and mir-363-3p as Potential Mediators." In Vivo 33, no. 3 (2019): 737–42. http://dx.doi.org/10.21873/invivo.11533.

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Luo, Xiaomin, Chunman Li, Ran Tan, Xiaohui Xu, William K. K. Wu, Ayano Satoh, Tuanlao Wang, and Sidney Yu. "Correction: A RasGAP, DAB2IP, regulates lipid droplet homeostasis by serving as GAP toward RAB40C." Oncotarget 9, no. 17 (March 2, 2018): 14035. http://dx.doi.org/10.18632/oncotarget.24600.

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Yun, E.-J., S. T. Baek, D. Xie, S.-F. Tseng, T. Dobin, E. Hernandez, J. Zhou, et al. "DAB2IP regulates cancer stem cell phenotypes through modulating stem cell factor receptor and ZEB1." Oncogene 34, no. 21 (July 21, 2014): 2741–52. http://dx.doi.org/10.1038/onc.2014.215.

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Valentino, Elena, Arianna Bellazzo, Giulio Di Minin, Daria Sicari, Mattia Apollonio, Giosuè Scognamiglio, Maurizio Di Bonito, Gerardo Botti, Giannino Del Sal, and Licio Collavin. "Mutant p53 potentiates the oncogenic effects of insulin by inhibiting the tumor suppressor DAB2IP." Proceedings of the National Academy of Sciences 114, no. 29 (June 30, 2017): 7623–28. http://dx.doi.org/10.1073/pnas.1700996114.

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Obesity and type 2 diabetes are significant risk factors for malignancies, being associated with chronic inflammation and hyperinsulinemia. In this context, insulin can synergize with inflammation to promote proliferation, survival, and dissemination of cancer cells. Point mutation of p53 is a frequent event and a significant factor in cancer development and progression. Mutant p53 protein(s) (mutp53) can acquire oncogenic properties that increase metastasis, proliferation, and cell survival. We report that breast and prostate cancer cells with mutant p53 respond to insulin stimulation by increasing cell proliferation and invasivity, and that such a response depends on the presence of mutp53. Mechanistically, we find that mutp53 augments insulin-induced AKT1 activation by binding and inhibiting the tumor suppressor DAB2IP (DAB2-interacting protein) in the cytoplasm. This molecular axis reveals a specific gain of function for mutant p53 in the response to insulin stimulation, offering an additional perspective to understand the relationship between hyperinsulinemia and cancer evolution.

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Zhang, Xiaojing, Ning Li, Xianzheng Li, Wei Zhao, Yudan Qiao, Li Liang, and Yanqing Ding. "Low expression of DAB2IP contributes to malignant development and poor prognosis in hepatocellular carcinoma." Journal of Gastroenterology and Hepatology 27, no. 6 (May 24, 2012): 1117–25. http://dx.doi.org/10.1111/j.1440-1746.2011.07049.x.

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Xie, Daxing, Jun Liu, Crystal Gore, Guiyang Hao, Michael Long, Xiankai Sun, and Jer-Tsong Hsieh. "THE IMPACT OF DAB2IP ON EPITHELIAL-MESENCHYMAL TRANSITION (EMT) LEADING TO PROSTATE CANCER METASTASIS." Journal of Urology 181, no. 4S (April 2009): 512. http://dx.doi.org/10.1016/s0022-5347(09)61446-4.

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Liu, Jing, Meng Zhang, Cong Xu, Haizhou Wang, Ya N. Peng, Chang Gao, Lan Liu, and Qiu Zhao. "Sa1198 - Mechanical Force Regulates Colorectal Tumorrepopulating Cells Self-Renewal Through Dab2Ip Mediated Nanog Expression." Gastroenterology 154, no. 6 (May 2018): S—275. http://dx.doi.org/10.1016/s0016-5085(18)31279-4.

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LIAO, HAIQIU, YANG XIAO, YINGBIN HU, YANGMING XIAO, ZHAOFA YIN, and LIANG LIU. "microRNA-32 induces radioresistance by targeting DAB2IP and regulating autophagy in prostate cancer cells." Oncology Letters 10, no. 4 (July 30, 2015): 2055–62. http://dx.doi.org/10.3892/ol.2015.3551.

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Cao, Haoyuan, Jiandong Zhang, and Wei Wang. "DAB2IP Plays Important Clinical Significance and Correlates With Immune Infiltration in Renal Cell Carcinoma." Technology in Cancer Research & Treatment 19 (January 1, 2020): 153303382093668. http://dx.doi.org/10.1177/1533033820936682.

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Background: Disabled homolog 2-interacting protein is a new member of the Ras GTPase superfamily involved in the regulation of cell proliferation, apoptosis, and metastasis. However, the expression of disabled homolog 2-interacting protein in renal cell carcinoma, its correlation with cancer prognosis, and tumor infiltrating lymphocytes remains unclear. Methods: The expression of disabled homolog 2-interacting protein was analyzed by UALCAN database, GEPIA database and the evaluation of disabled homolog 2-interacting protein effects on clinical prognosis. Prognostic factor analysis was used to identify the correlations between disabled homolog 2-interacting protein and cancer immune infiltration via the TIMER database. In addition, COXPRESdb database was used to analyze the enrichment of disabled homolog 2-interacting protein co-expression genes. Results: Compared to the normal tissues, the messenger RNA expression levels of DAB2IP are higher in 8 while lower in 15 types of tumor tissues. Furthermore, disabled homolog 2-interacting protein has high expression in kidney chromophobe and low expression in both kidney renal clear cell carcinoma and kidney renal papillary cell carcinoma. The messenger RNA expression levels of disabled homolog 2-interacting protein decrease gradually due to the increasing tumor staging which positively correlates with disease-free survival and overall survival in both kidney renal clear cell carcinoma and kidney renal papillary cell carcinoma. The expression levels of disabled homolog 2-interacting protein also positively correlate with the tumor purity of kidney chromophobe, kidney renal clear cell carcinoma, and kidney renal papillary cell carcinoma samples. Besides, the expression of disabled homolog 2-interacting protein in renal cell carcinoma has negative correlation with the immune infiltration, and the immune infiltration of B cells and CD8+ T cells affects the prognosis of kidney renal papillary cell carcinoma. Enrichment analysis of disabled homolog 2-interacting protein co-expressed genes suggested that its biological role was mainly in regulating GTPase activity. Conclusions: These findings suggest that disabled homolog 2-interacting protein functions as a tumor suppressor in the progression of renal cell carcinoma, and the expression of disabled homolog 2-interacting protein is related to the immune infiltrating cells and affects the survival of renal cell carcinoma. Disabled homolog 2-interacting protein can be a novel clinical biomarker for patients with renal cell carcinoma, which also provides new insights for the future treatments of renal cell carcinoma.

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Journal articles on the topic 'DAB2IP'

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