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  • American Association for Cancer Research (AACR)  (43)
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  • 1
    Online Resource
    Online Resource
    Abstract 3794: CCL5 from tumor-associated macrophages/microglia (TAMs) regulates glioma migration and invasion via calcium-dependent matrix metalloproteinase-2
    American Association for Cancer Research (AACR) ; 2018
    In:  Cancer Research Vol. 78, No. 13_Supplement ( 2018-07-01), p. 3794-3794
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 78, No. 13_Supplement ( 2018-07-01), p. 3794-3794
    Abstract: Tumor-associated macrophages/microglia (TAMs) are either macrophages of peripheral origin or brain-intrinsic microglia, and represent a considerable portion of the glioma mass, which facilitate gliomagenesis. Chemokine C-C motif ligand 5 (CCL5) is an inflammatory mediator produced by immune cells, and involves in tumor growth, and migration in serval cancers including glioma. However, the mechanism of how CCL5 facilitates glioma invasion remains largely unresolved. In this study, we demonstrate that CCL5 modulate human glioma cell lines, A172 and U87, migratory and invasive activities along with MMPs expression. In response to CCL5, glioma synchronized an increase of intracellular calcium levels, and kinase elevations including p-CaMKII, and p-Akt expressions in time and dosage manners. Importantly, glioma invasion along with MMPs elevation are dependent on CCL5-propogated p-CaMKII expression, and inhibition of p-CaMKII effectively reduced CCL5-directed glioma MMPs expression and invasion. Using three-dimensional cultures, we demonstrated that glioma cells tend to homing toward GM-CSF-activated TAM condition media. This homing effect associated with MMPs elevation which can be ameliorated either by controlling the intracellular and extracellular calcium levels or by CCL5 antagonism. Clinical results also reveal association of CCL5 with TAM activation, and patients' overall survival. Our results suggest that modulation of glioma CaMKII may restrict the effect of CCL5 on glioma migration and could be a potential therapeutic strategy for alleviating glioma invasion. Citation Format: Caren Yu-Ju Wu, Chia-Hua Chen, Chun-Yen Lin, Li-Ying Feng, Yung-Chang Lin, Kuo-Chen Wei, Chiung-Yin Huang, Jia-You Fang, Pin-Yuan Chen. CCL5 from tumor-associated macrophages/microglia (TAMs) regulates glioma migration and invasion via calcium-dependent matrix metalloproteinase-2 [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2018; 2018 Apr 14-18; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2018;78(13 Suppl):Abstract nr 3794.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2018-3794
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2018
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  • 2
    Online Resource
    Online Resource
    Tumor-associated Lymphatic Endothelial Cells Promote Lymphatic Metastasis By Highly Expressing and Secreting SEMA4C
    American Association for Cancer Research (AACR) ; 2017
    In:  Clinical Cancer Research Vol. 23, No. 1 ( 2017-01-01), p. 214-224
    Details
    In: Clinical Cancer Research, American Association for Cancer Research (AACR), Vol. 23, No. 1 ( 2017-01-01), p. 214-224
    Abstract: Purpose: Lymphatic vessels are mainly regarded as passive conduits for the dissemination of cancer cells. In this study, we investigate whether and how the tumor-associated lymphatic vessels may play an active role in tumor metastasis. Experimental Design: In situ laser capture microdissection of lymphatic vessels followed by cDNA microarray analysis was used to determine the expression profiling of lymphatic endothelial cells (LEC). Gene expression levels and activity of signaling pathways were measured by real-time RT-PCR, ELISA, or immunoblotting. Lymphangiogenesis was assessed by IHC. Lymph node metastasis was measured using fluorescence imaging. The effects of SEMA4C on lymphangiogenesis in vitro were evaluated using migration assay and tube-formation assay of LECs. Results: Tumor-associated LECs are molecularly and functionally different from their normal counterparts. In addition to expressing high levels of membrane-bound SEMA4C, tumor-associated LECs also produced soluble SEMA4C (sSEMA4C). Increased serum sSEMA4C was detected in patients with breast cancer and cervical cancer. Patients with metastasis had much higher levels of serum sSEMA4C. sSEMA4C promoted lymphangiogenesis by activating PlexinB2-ERBB2 signaling in LECs, and promoted the proliferation and migration of tumor cells by activating PlexinB2-MET signaling, thus promoting lymphatic metastasis. Although the SEMA4C signaling pathways differ between LECs and tumor cells, RHOA activation was necessary for the effects of SEMA4C in both types of cells. Conclusions: Tumor-associated LECs produce sSEMA4C to promote lymphatic metastasis of tumors. Our results suggest that SEMA4C and RHOA might be potential therapeutic targets, and that higher serum sSEMA4C could be a marker for breast cancer and cervical cancer. Clin Cancer Res; 23(1); 214–24. ©2016 AACR.
    Type of Medium: Online Resource
    ISSN: 1078-0432 , 1557-3265
    URL: Article
    DOI: 10.1158/1078-0432.CCR-16-0741
    RVK:
    XA 36791
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2017
    detail.hit.zdb_id: 1225457-5
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  • 3
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    Online Resource
    Hyperthermia Selectively Destabilizes Oncogenic Fusion Proteins
    American Association for Cancer Research (AACR) ; 2021
    In:  Blood Cancer Discovery Vol. 2, No. 4 ( 2021-07-01), p. 388-401
    Details
    In: Blood Cancer Discovery, American Association for Cancer Research (AACR), Vol. 2, No. 4 ( 2021-07-01), p. 388-401
    Abstract: The PML/RARα fusion protein is the oncogenic driver in acute promyelocytic leukemia (APL). Although most APL cases are cured by PML/RARα-targeting therapy, relapse and resistance can occur due to drug-resistant mutations. Here we report that thermal stress destabilizes the PML/RARα protein, including clinically identified drug-resistant mutants. AML1/ETO and TEL/AML1 oncofusions show similar heat shock susceptibility. Mechanistically, mild hyperthermia stimulates aggregation of PML/RARα in complex with nuclear receptor corepressors leading to ubiquitin-mediated degradation via the SIAH2 E3 ligase. Hyperthermia and arsenic therapy destabilize PML/RARα via distinct mechanisms and are synergistic in primary patient samples and in vivo, including three refractory APL cases. Collectively, our results suggest that by taking advantage of a biophysical vulnerability of PML/RARα, thermal therapy may improve prognosis in drug-resistant or otherwise refractory APL. These findings serve as a paradigm for therapeutic targeting of fusion oncoprotein–associated cancers by hyperthermia. Significance: Hyperthermia destabilizes oncofusion proteins including PML/RARα and acts synergistically with standard arsenic therapy in relapsed and refractory APL. The results open up the possibility that heat shock sensitivity may be an easily targetable vulnerability of oncofusion-driven cancers. See related commentary by Wu et al., p. 300.
    Type of Medium: Online Resource
    ISSN: 2643-3230 , 2643-3249
    URL: Article
    DOI: 10.1158/2643-3230.BCD-20-0188
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2021
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  • 4
    Online Resource
    Online Resource
    Silencing PinX1 Compromises Telomere Length Maintenance As Well As Tumorigenicity in Telomerase-Positive Human Cancer Cells
    American Association for Cancer Research (AACR) ; 2009
    In:  Cancer Research Vol. 69, No. 1 ( 2009-01-01), p. 75-83
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 69, No. 1 ( 2009-01-01), p. 75-83
    Abstract: The nucleolar protein PinX1 has been proposed to be a putative tumor suppressor due to its binding to and inhibition of the catalytic activity of telomerase, an enzyme that is highly expressed in most human cancers in which it counteracts telomere shortening–induced senescence to confer cancer cell immortalization. However, the role of PinX1 in telomere regulation, as well as in cancer, is still poorly understood. In this study, we showed that the PinX1 protein is constitutively expressed in various human cells regardless of their telomerase activity and malignant status. Most interestingly, we found that silencing PinX1 expression by a potent short hairpin RNA construct led to a robust telomere length shortening and growth inhibition in telomerase-positive but not in telomerase-negative human cancer cells. We further showed that silencing PinX1 significantly reduced the endogenous association of telomerase with the Pot1-containing telomeric protein complex, and therefore, could account for the phenotypic telomere shortening in the affected telomerase-positive cancer cells. Our results thus reveal a novel positive role for PinX1 in telomerase/telomere regulations and suggest that the constitutive expression of PinX1 attributes to telomere maintenance by telomerase and tumorigenicity in cancer cells. [Cancer Res 2009;69(1):75–83]
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/0008-5472.CAN-08-1393
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2009
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  • 5
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    Abstract LB-288: An allosteric PRC2 inhibitor targeting the H3K27me3 binding pocket of EED
    American Association for Cancer Research (AACR) ; 2017
    In:  Cancer Research Vol. 77, No. 13_Supplement ( 2017-07-01), p. LB-288-LB-288
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 77, No. 13_Supplement ( 2017-07-01), p. LB-288-LB-288
    Abstract: Polycomb repressive complex 2 (PRC2) consists of three core subunits, EZH2, EED and SUZ12 and plays pivotal roles in transcriptional regulation through its histone H3K27 methyltransferase activity. Dysregulation of PRC2 is observed in multiple human cancers, for example, the catalytic subunit EZH2 is overexpressed in a wide range of human cancers and gain-of-function mutations of EZH2 within its catalytic site have been reported in human B-cell lymphoma, parathyroid carcinoma and melanoma. Small molecule inhibitors that compete with the cofactor S-adenosylmethionine (SAM) have been reported and showed anti-lymphoma efficacy in pre-clinical studies. EED within the PRC2 complex allosterically activate the enzymatic activity by binding to tri-methylated H3K27 (H3K27me3). Here we report the discovery of EED226, a potent and selective PRC2 inhibitor directly binding to the H3K27me3 binding pocket of EED. EED226 induces conformational change upon binding EED leading to loss of PRC2 activity. EED226 shows similar activity as SAM-competitive inhibitors in blocking H3K27 methylation of PRC2 target genes and inducing regression of human lymphoma xenograft tumors. Interestingly, EED226 also effectively inhibits PRC2 containing mutant EZH2 protein resistant to SAM-competitive inhibitors. Together, we show EED226 inhibits PRC2 activity via an allosteric mechanism and offers opportunity for treatment of PRC2-dependent cancers. Citation Format: Wei Qi, Kehao Zhao, Justin Gu, Ying Huang, Youzhen Wang, Hailong Zhang, Man Zhang, Jeff Zhang, Zhengtian Yu, Ling Li, Lin Teng, Shannon Chuai, Chao Zhang, Mengxi Zhao, HoMan Chan, Zijun Chen, Douglas Fang, Fei Qi, Leying Feng, Lijian Feng, Yuan Gao, Hui Ge, Xinjian Ge, Andreas Lingel, Guobin Li, Ying Lin, Yueqin Liu, Fangjun Luo, Minlong Shi, Long Wang, Zhaofu Wang, Yanyan Yu, Jue Zeng, Chenhui Zeng, Lijun Zhang, Qiong Zhang, Shaolian Zhou, Counde Oyang, Peter Atadja, En Li. An allosteric PRC2 inhibitor targeting the H3K27me3 binding pocket of EED [abstract] . In: Proceedings of the American Association for Cancer Research Annual Meeting 2017; 2017 Apr 1-5; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2017;77(13 Suppl):Abstract nr LB-288. doi:10.1158/1538-7445.AM2017-LB-288
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2017-LB-288
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2017
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  • 6
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    Abstract A028: The Early Detection Initiative trial version 2: A platform trial to test novel approaches to pancreatic cancer screening in patients with new onset hyperglycemia and diabetes
    American Association for Cancer Research (AACR) ; 2022
    In:  Cancer Research Vol. 82, No. 22_Supplement ( 2022-11-15), p. A028-A028
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 82, No. 22_Supplement ( 2022-11-15), p. A028-A028
    Abstract: The Early Detection Initiative (EDI) is an innovative study designed to build a platform that will evaluate novel approaches to early detection of resectable pancreatic ductal adenocarcinoma (PDAC) in patients over age 50 with new onset hyperglycemia and diabetes (NOD). This randomized controlled trial (RCT) of algorithm-based screening for PDAC uses a modified Zelen’s design with post-randomization consent. Eligible subjects are identified through electronic medical record (EMR) surveillance and randomized 1:1 to the Observation or Intervention Arm. The Enriching New-onset Diabetes for Pancreatic Cancer (ENDPAC) score, an algorithm that further risk stratifies NOD based on age and changes in weight and glycemic parameters, is calculated in the Intervention Arm. Consenting subjects with ENDPAC & gt;0 have Computerized Tomography (CT) scan imaging for PDAC detection; potential harm, including over-diagnosis, is also estimated. At the time of abstract submission & gt;2000 individuals have been randomized and & gt;50 subjects consented for CT imaging. EDI version 2 adds several innovations in response to challenges encountered and experience gained so far. Most significantly, EDI v2 has a platform design with a common control arm and allows for multiple intervention arms. This opens the door for evaluating future new biomarkers for PDAC early detection in a high–risk NOD population, including new blood-based biomarkers for the early detection of cancer that are now commercially available. EDI v2 focuses primarily on co-efficacy endpoints (PDAC stage shift in ENDPAC & gt;0 group, and in all patients, excluding non-consented patients); effectiveness evaluation becomes a secondary objective. This addresses the challenges of low consent rate (~25%) due to lack of awareness of connection between NOD and PDAC and low acceptance for a novel research screening modality. The analyses of primary endpoints were adjusted to accommodate potential over-diagnosis due to screening and imbalance between ENDPAC & gt;0 and ENDPAC ≤0 groups due to low consent rate and likely imperfect enrichment by ENDPAC, when evaluating all patients. Electronic eligibility checks and consent shorten the recruitment time, a critical factor for stage shift due to rapid progression of PDAC. A pre-randomization screening pilot study is planned to enhance the post-randomization consent rate. Intervention to Control randomization ratio is changed to 2:1, allowing more rapid recruitment and, when factoring the consent rate, doubling the sample size of the observation arm. Through these innovations, EDI v2 maintains the full advantage of Zelen’s design that made the trial feasible in sample size and cost. Simulation studies demonstrate that our approach correctly controls the type-1 error and the trial has adequate statistical power. The EDI trial represents an innovative and contemporary approach to developing and refining an early detection strategy for pancreatic cancer. Citation Format: Ying-Qi Zhao, Suresh T. Chari, Anirban Maitra, Lynn M. Matrisian, Eva E. Shrader, Bechien U. Wu, Avinash Kambadakone, Barbara Kenner, Jo Ann S. Rinaudo, Sudhir Srivastava, Ying Huang, Ziding Feng. The Early Detection Initiative trial version 2: A platform trial to test novel approaches to pancreatic cancer screening in patients with new onset hyperglycemia and diabetes [abstract]. In: Proceedings of the AACR Special Conference on Pancreatic Cancer; 2022 Sep 13-16; Boston, MA. Philadelphia (PA): AACR; Cancer Res 2022;82(22 Suppl):Abstract nr A028.
    Type of Medium: Online Resource
    ISSN: 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.PANCA22-A028
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2022
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  • 7
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    Abstract P1-12-03: Antidiarrheal prophylaxis with loperamide for patients with lymph node-negative (N0) or micrometastatic (N1mi), HER2-positive breast cancer who received adjuvant pyrotinib plus nab-paclitaxel: a randomized sub-study of PHAEDRA
    American Association for Cancer Research (AACR) ; 2023
    In:  Cancer Research Vol. 83, No. 5_Supplement ( 2023-03-01), p. P1-12-03-P1-12-03
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 83, No. 5_Supplement ( 2023-03-01), p. P1-12-03-P1-12-03
    Abstract: Background: Diarrhea is the most common adverse event of pan-HER tyrosine kinase inhibitors. There is no consensus on therapeutic or prophylactic strategy of pyrotinib-related diarrhea. PHAEDRA is an ongoing multicenter, single-arm, phase II trial conducted to evaluate adjuvant pyrotinib plus nab-paclitaxel for patients with low-risk HER2-positive breast cancer. Here, we reported the results from the sub-study of PHAEDRA, which investigated the effect of different prophylactic strategies with loperamide for diarrhea. Methods: In PHAEDRA, patients with N0/N1mi, HER2-positive invasive breast cancer and primary tumor ≤3 cm received nab-paclitaxel 260 mg/m2 once every 3 weeks for 12 weeks and pyrotinib 400 mg once daily for one year within 90 days after surgery. In the sub-study, patients were randomly assigned to receive loperamide 4 mg three times a day on days 1-7 and twice a day on days 8-21 (cohort A) or days 8-42 (cohort B) since the initiation of adjuvant therapy. The primary endpoint of the sub-study was the incidence of grade ≥3 diarrhea. Results: Between January 2021 and May 2022, the enrollment of 120 patients in the sub-study was completed. Grade ≥3 diarrhea was reported in 18 (30%) of 60 patients in cohort A and 19 (32%) of 60 patients in cohort B. The median time to first grade ≥3 diarrhea was 4.5 days (IQR, 1.0-6.5) in cohort A and 4 days (IQR, 1.0-6.0) in cohort B. The median number of grade ≥3 diarrhea episodes was 1 (IQR, 1-1) in both cohorts. Three (5%) patients in each cohort had constipation events, respectively, which were all grade 1 or 2. One (2%) patient in cohort A and two (3%) in cohort B had dose reductions of loperamide due to constipation, and no patients discontinued loperamide. One (2%) patient in cohort A had dose reduction of pyrotinib and one (2%) in each cohort discontinued pyrotinib due to diarrhea. Conclusions: The effects of both loperamide regimens on antidiarrheal prophylaxis were consistent with that of loperamide prophylaxis in the CONTROL trial, but with extremely fewer constipation events. Long-course and short-course loperamide prophylaxis showed numerically similar incidence of grade ≥3 diarrhea. Proactive diarrhea management can promote the full-dose and full-course treatment with pyrotinib. It is still necessary to develop more effective antidiarrheal prophylaxis regimens for pan-HER tyrosine kinase inhibitors. Citation Format: Changjun Wang, Yan Lin, Yidong Zhou, Feng Mao, Jinghong Guan, Songjie Shen, Xuejing Wang, Xiaohui Zhang, Yanna Zhang, Bo Pan, Ying Zhong, Li Peng, Yan Li, Xin Huang, Ying Xu, Qiang Sun. Antidiarrheal prophylaxis with loperamide for patients with lymph node-negative (N0) or micrometastatic (N1mi), HER2-positive breast cancer who received adjuvant pyrotinib plus nab-paclitaxel: a randomized sub-study of PHAEDRA [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 P1-12-03.
    Type of Medium: Online Resource
    ISSN: 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.SABCS22-P1-12-03
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2023
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  • 8
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    Mitochondrial Micropeptide STMP1 Enhances Mitochondrial Fission to Promote Tumor Metastasis
    American Association for Cancer Research (AACR) ; 2022
    In:  Cancer Research Vol. 82, No. 13 ( 2022-07-05), p. 2431-2443
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 82, No. 13 ( 2022-07-05), p. 2431-2443
    Abstract: Micropeptides are a recently discovered class of molecules that play vital roles in various cellular processes, including differentiation, proliferation, and apoptosis. Here, we sought to identify cancer-associated micropeptides and to uncover their mechanistic functions. A micropeptide named short transmembrane protein 1 (STMP1) that localizes at the inner mitochondrial membrane was identified to be upregulated in various cancer types and associated with metastasis and recurrence of hepatocellular carcinoma. Both gain- and loss-of-function studies revealed that STMP1 increased dynamin-related protein 1 (DRP1) activation to promote mitochondrial fission and enhanced migration of tumor cells. STMP1 silencing inhibited in vivo tumor metastasis in xenograft mouse models. Overexpression of STMP1 led to redistribution of mitochondria to the leading edge of cells and enhanced lamellipodia formation. Treatment with a DRP1 inhibitor abrogated the promotive effect of STMP1 on mitochondrial fission, lamellipodia formation, and tumor cell migration in vitro and metastasis in vivo. Furthermore, STMP1 interacted with myosin heavy chain 9 (MYH9), the subunit of nonmuscle myosin II, and silencing MYH9 abrogated STMP1-induced DRP1 activation, mitochondrial fission, and cell migration. Collectively, this study identifies STMP1 as a critical regulator of metastasis and a novel unit of the mitochondrial fission protein machinery, providing a potential therapeutic target for treating metastases. Significance: This study identifies the mitochondrial micropeptide STMP1 as a regulator of metastasis that promotes mitochondrial fission and tumor cell migration via DRP1 and MYH9.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/0008-5472.CAN-21-3910
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2022
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  • 9
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    Histone Demethylase RBP2 Promotes Lung Tumorigenesis and Cancer Metastasis
    American Association for Cancer Research (AACR) ; 2013
    In:  Cancer Research Vol. 73, No. 15 ( 2013-08-01), p. 4711-4721
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 73, No. 15 ( 2013-08-01), p. 4711-4721
    Abstract: The retinoblastoma binding protein RBP2 (KDM5A) is a histone demethylase that promotes gastric cancer cell growth and is enriched in drug-resistant lung cancer cells. In tumor-prone mice lacking the tumor suppressor gene RB or MEN1, genetic ablation of RBP2 can suppress tumor initiation, but the pathogenic breadth and mechanistic aspects of this effect relative to human tumors have not been defined. Here, we approached this question in the context of lung cancer. RBP2 was overexpressed in human lung cancer tissues where its depletion impaired cell proliferation, motility, migration, invasion, and metastasis. RBP2 oncogenicity relied on its demethylase and DNA-binding activities. RBP2 upregulated expression of cyclins D1 and E1 while suppressing the expression of cyclin-dependent kinase inhibitor p27 (CDKN1B), each contributing to RBP2-mediated cell proliferation. Expression microarray analyses revealed that RBP2 promoted expression of integrin-β1 (ITGB1), which is implicated in lung cancer metastasis. Mechanistic investigations established that RBP2 bound directly to the p27, cyclin D1, and ITGB1 promoters and that exogenous expression of cyclin D1, cyclin E1, or ITGB1 was sufficient to rescue proliferation or migration/invasion, respectively. Taken together, our results establish an oncogenic role for RBP2 in lung tumorigenesis and progression and uncover novel RBP2 targets mediating this role. Cancer Res; 73(15); 4711–21. ©2013 AACR.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/0008-5472.CAN-12-3165
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2013
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  • 10
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    Polymorphisms in the Two Helicases ERCC2/XPD and ERCC3/XPB of the Transcription Factor IIH Complex and Risk of Lung Cancer: A Case-Control Analysis in a Chinese Population
    American Association for Cancer Research (AACR) ; 2006
    In:  Cancer Epidemiology, Biomarkers & Prevention Vol. 15, No. 7 ( 2006-07-01), p. 1336-1340
    Details
    In: Cancer Epidemiology, Biomarkers & Prevention, American Association for Cancer Research (AACR), Vol. 15, No. 7 ( 2006-07-01), p. 1336-1340
    Abstract: The transcription factor IIH (TFIIH) helicases ERCC2/XPD and ERCC3/XPB are responsible for opening the DNA strand around the lesion site during nucleotide excision repair process. Genetic variants in these two genes may be markers for interindividual variability in DNA repair capacity and thus predisposition to cancer risk. In this case-control study of 1,010 incident lung cancer cases and 1,011 age and sex frequency–matched cancer-free controls in a Chinese population, we genotyped eight tagging polymorphisms of ERCC2 and ERCC3 using the high-throughput Taqman platform to determine their associations with risk of lung cancer. Although none of the eight polymorphisms was individually associated with lung cancer risk, we found that genetic variants in ERCC2 and ERCC3 jointly contributed to lung cancer risk in a dose-response manner. Compared with those with 0 to 1 “at-risk” locus, subjects carrying & gt;1 at-risk loci were at increased risk for lung cancer [adjusted odds ratio (OR), 1.29; 95% confidence interval (95% CI), 0.98-1.70 for 2 at-risk loci; adjusted OR, 1.38; 95% CI, 1.02-1.85 for 3 at-risk loci; and adjusted OR, 1.51; 95% CI, 1.09-2.10 for ≥4 at-risk loci, respectively; Ptrend = 0.015]. This combined effect was slightly more evident in young subjects ( & lt;60 years), males, current smokers, and those with family history of cancer, particularly for histologic type of adenocarcinomas. No evidence for interaction was found. These findings indicate that these tagSNPs of the ERCC2 and ERCC3 along with their surrounding regions may serve as biomarkers of susceptibility to lung cancer, which warrant further validation by other population-based and phenotypic studies to determine the biological relevance of these tagSNPs. (Cancer Epidemiol Biomarkers Prev 2006;15(7):1336–40)
    Type of Medium: Online Resource
    ISSN: 1055-9965 , 1538-7755
    URL: Article
    DOI: 10.1158/1055-9965.EPI-06-0194
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2006
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