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141 citation(s) found for "Mukhopadhyay, Debabrata".

Non-metastatic 2 (NME2)-mediated suppression of lung cancer metastasis involves transcriptional regulation of key cell adhesion factor vinculin
Thakur, Ram Krishna, Yadav, Vinod Kumar , Kumar, Akinchan, Singh, Ankita, Pal, Krishnendu , Hoeppner, Luke H. , Saha, Dhurjhoti , Purohit, Gunjan , Basundra, Richa, Kar, Anirban, Halder, Rashi , Kumar, Pankaj, Baral, Aradhita, Kumar, MJ Mahesh, Baldi, Alfonso , Banerjee‬‬‬‬‬‬‬‬‬, Rintu , Kumar, Praveen , Shridhar, Viji , Chowdhury, Shantanu , Hoeppner, Luke, Kumar, Pankaj, Vincenzi, Bruno , Lorenzon, Laura , Mukhopadhyay, Debabrata , Pal, Krishnendu , Banerjee, Rajkumar

Mayo Clinic

Nucleic Acids Research | September 23, 2014 | Volume: 42 | Issue: 18 | Pages: 11589-11600

10.1093/nar/gku860 | PMID 25249619 Get It

Abstract Tumor metastasis refers to spread of a tumor from site of its origin to distant organs and causes majority of cancer deaths. Although >30 metastasis suppressor genes (MSGs) that negatively regulate metastasis have been identified so far, two issues are poorly understood: first, which MSGs oppose metastasis in a tumor type, and second, which molecular function of MSG controls metastasis. Herein, integrative analyses of tumor-transcriptomes (n = 382), survival data (n = 530) and lymph node metastases (n = 100) in lung cancer patients identified non-metastatic 2 (NME2) as a key MSG from a pool of >30 metastasis suppressors. Subsequently, we generated a promoter-wide binding map for NME2 using chromatin immunoprecipitation with promoter microarrays (ChIP-chip), and transcriptome profiling. We discovered novel targets of NME2 which are involved in focal adhesion signaling. Importantly, we detected binding of NME2 in promoter of focal adhesion factor, vinculin. Reduced expression of NME2 led to enhanced transcription of vinculin. In comparison, NME1, a close homolog of NME2, did not bind to vinculin promoter nor regulate its expression. In line, enhanced metastasis of NME2-depleted lung cancer cells was found in zebrafish and nude mice tumor models. The metastatic potential of NME2-depleted cells was remarkably diminished upon selective RNA-i-mediated silencing of vinculin. Together, we demonstrate that reduced NME2 levels lead to transcriptional de-repression of vinculin and regulate lung cancer metastasis.
Selective Assembly of DNA-Conjugated Single-Walled Carbon Nanotubes from the Vascular Secretome
Gong, Xun , Sharma, Anil Kumar , Strano, Michael S. , Sharma, Anil K. , Mukhopadhyay, Debabrata , Gong, Xun

Mayo Clinic

ACS Nano | September 3, 2014 | Volume: 8 | Issue: 9 | Pages: 9126-9136

10.1021/nn5026912 | PMID 25184956 Get It

Abstract Colloidal dispersion of single-walled carbon nanotubes (SWCNTs) is often the first processing step to many of their unique applications. However, dispersed SWCNTs often exist in kinetically trapped states where aggregation can be of concern. Recent work revealed prominent DNA–SWCNT aggregation following intravascular injection. In this study, we performed detailed analysis of DNA–SWCNT aggregate formation, structure, and composition in the context of endothelial cell condition media. Interestingly, we found that aggregates formed within condition media from cells that have undergone a stress response differ in size and organization from that of the control. We also found that temperature increases also promote DNA–SWCNT associations. A mathematical model was developed to describe the kinetics of SWCNT extraction from solution. Through orthogonal optical analysis and imaging modalities, we verified that proteins form the bulk of the aggregate structure and dictate aggregate assembly at multiple levels of organization. Finally, physiochemical analysis indicated preferential extraction of low-abundance hydrophobic and charged proteins. The formed aggregates also remain relatively stable in solution, making them potential macroscopic indicators of solution content.
Inhibition of Endoglin–GIPC Interaction Inhibits Pancreatic Cancer Cell Growth
Pal, Krishnendu , Pletnev, Alexandre A., Dutta, Shamit K., Wang, Enfeng , Zhao, Ruizhi , Baral, Aradhita, Yadav, Vinod Kumar , Aggarwal, Suruchi , Krishnaswamy, Soundararajan, Alkharfy, Khalid M. , Chowdhury, Shantanu , Spaller, Mark R., Mukhopadhyay, Debabrata , Pal, Krishnendu

Mayo Clinic

Molecular Cancer Therapeutics | August 15, 2014 | Volume: 13 | Issue: 10 | Pages: 2264-2275

10.1158/1535-7163.mct-14-0291 | PMID 25125675 Get It

Abstract Endoglin, a 180-kDa disulfide-linked homodimeric transmembrane receptor protein mostly expressed in tumor-associated endothelial cells, is an endogenous binding partner of GAIP-interacting protein, C terminus (GIPC). Endoglin functions as a coreceptor of TβRII that binds TGFβ and is important for vascular development, and consequently has become a compelling target for antiangiogenic therapies. A few recent studies in gastrointestinal stromal tumor (GIST), breast cancer, and ovarian cancer, however, suggest that endoglin is upregulated in tumor cells and is associated with poor prognosis. These findings indicate a broader role of endoglin in tumor biology, beyond angiogenic effects. The goal of our current study is to evaluate the effects of targeting endoglin in pancreatic cancer both in vitro and in vivo. We analyzed the antiproliferative effect of both RNAi-based and peptide ligand-based inhibition of endoglin in pancreatic cancer cell lines, the latter yielding a GIPC PDZ domain-targeting lipopeptide with notable antiproliferative activity. We further demonstrated that endoglin inhibition induced a differentiation phenotype in the pancreatic cancer cells and sensitized them against conventional chemotherapeutic drug gemcitabine. Most importantly, we have demonstrated the antitumor effect of both RNAi-based and competitive inhibitor–based blocking of endoglin in pancreatic cancer xenograft models in vivo. To our knowledge, this is the first report exploring the effect of targeting endoglin in pancreatic cancer cells. Mol Cancer Ther; 13(10); 2264–75. ©2014 AACR.
Inhibition of GSK-3 Induces Differentiation and Impaired Glucose Metabolism in Renal Cancer
Pal, Krishnendu , Cao, Ying , Gaisina, Irina N. , Dutta, Shamit K., Wang, Enfeng , Gunosewoyo, Hendra , Kozikowski, Alan P. , Billadeau, Daniel D. , Bhattacharya, Santanu , Mukhopadhyay, Debabrata , Pal, Krishnendu

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Molecular Cancer Therapeutics | December 10, 2013 | Volume: 13 | Issue: 2 | Pages: 285-296

10.1158/1535-7163.mct-13-0681 | PMID 24327518 Get It

Abstract Glycogen synthase kinase-3 (GSK-3), a constitutively active serine/threonine kinase, is a key regulator of numerous cellular processes ranging from glycogen metabolism to cell-cycle regulation and proliferation. Consistent with its involvement in many pathways, it has also been implicated in the pathogenesis of various human diseases, including type II diabetes, Alzheimer disease, bipolar disorder, inflammation, and cancer. Consequently, it is recognized as an attractive target for the development of new drugs. In the present study, we investigated the effect of both pharmacologic and genetic inhibition of GSK-3 in two different renal cancer cell lines. We have shown potent antiproliferative activity of 9-ING-41, a maleimide-based GSK-3 inhibitor. The antiproliferative activity is most likely caused by G0–G1 and G2–M phase arrest as evident from cell-cycle analysis. We have established that inhibition of GSK-3 imparted a differentiated phenotype in renal cancer cells. We have also shown that GSK-3 inhibition induced autophagy, likely as a result of imbalanced energy homeostasis caused by impaired glucose metabolism. In addition, we have demonstrated the antitumor activity of 9-ING-41 in two different subcutaneous xenograft renal cell carcinoma tumor models. To our knowledge, this is the first report describing autophagy induction due to GSK-3 inhibition in renal cancer cells. Mol Cancer Ther; 13(2); 285–96. ©2013 AACR.
Neuropilin-2 Promotes Extravasation and Metastasis by Interacting with Endothelial α5 Integrin
Cao, Ying , Hoeppner, Luke H. , Bach, Steven , Guangqi, E, Wang, Enfeng , Wu, Jianmin , Cowley, Mark J. , Chang, David K. , Waddell, Nicola , Grimmond, Sean M. , Biankin, Andrew V. , Daly, Roger J. , Zhang, Xiao Hui , E, Guangqi, Guo, Yan , Mukhopadhyay, Debabrata , Waddell, Nicola , Chang, David , Grimmond, Sean M , Biankin, Andrew V

Mayo Clinic

Cancer Research | May 21, 2013 | Volume: 73 | Issue: 14 | Pages: 4579-4590

10.1158/0008-5472.can-13-0529 | PMID 23689123 Get It

Abstract Metastasis, the leading cause of cancer death, requires tumor cell intravasation, migration through the bloodstream, arrest within capillaries, and extravasation to invade distant tissues. Few mechanistic details have been reported thus far regarding the extravasation process or re-entry of circulating tumor cells at metastatic sites. Here, we show that neuropilin-2 (NRP-2), a multifunctional nonkinase receptor for semaphorins, vascular endothelial growth factor (VEGF), and other growth factors, expressed on cancer cells interacts with α5 integrin on endothelial cells to mediate vascular extravasation and metastasis in zebrafish and murine xenograft models of clear cell renal cell carcinoma (RCC) and pancreatic adenocarcinoma. In tissue from patients with RCC, NRP-2 expression is positively correlated with tumor grade and is highest in metastatic tumors. In a prospectively acquired cohort of patients with pancreatic cancer, high NRP-2 expression cosegregated with poor prognosis. Through biochemical approaches as well as Atomic Force Microscopy (AFM), we describe a unique mechanism through which NRP-2 expressed on cancer cells interacts with α5 integrin on endothelial cells to mediate vascular adhesion and extravasation. Taken together, our studies reveal a clinically significant role of NRP-2 in cancer cell extravasation and promotion of metastasis. Cancer Res; 73(14); 4579–90. ©2013 AACR.
Antibody modified Bovine Serum Albumin microspheres for targeted delivery of anticancer agent Gemcitabine
Grinberg, Olga, Gedanken, Aharon , Patra, Chitta Ranjan , Mukhopadhyay, Debabrata

Mayo Clinic

Polymers for Advanced Technologies | October 23, 2012 | Volume: 24 | Issue: 3 | Pages: 294-299

10.1002/pat.3081 Get It

Inhibition of the EGFR signaling pathway is one of the attractive therapeutic targets for pancreatic cancer as recent studies demonstrated that EGFR is over‐expressed in pancreatic cancer. In this article we have demonstrated the design of targeted drug delivery system containing Bovine Serum Albumin (BSA) microspheres as delivery vehicle, gemcitabine as anticancer drug and anti‐EGFR (epidermal growth factor receptor) monoclonal antibody as targeting agent. The conjugated BSA microspheres were characterized by several physico‐chemical techniques such as scanning electron microscope, optical microscopy, fluorescent microscopy etc. Administration of these BSA microspheres containing gemcitabine and anti‐EGFR (BSA‐Gem‐EGFR) shows significant inhibition of pancreatic cancer cells (AsPC1) compared to the cells treated with only BSA microspheres, BSA with gemcitabine (BSA‐Gem), and free gemcitabine. This strategy could be used as a generalized approach for the treatment of pancreatic cancer along with other cancers which overexpress EGFR on cell surface. Copyright © 2012 John Wiley & Sons, Ltd.
Tumor Angiogenesis 2012
Dudek, Arkadiusz Z. , Gupta, Kalpna , Ramakrishnan, Sundaram , Mukhopadhyay, Debabrata , Dudek, Arkadiusz Z

Mayo Clinic

Journal of Oncology | August 2, 2012 | Volume: 2012 | Issue: No issue available | Pages: 1-2

10.1155/2012/857383 | PMID 22919384 Get It

Neuropilin-1 Stimulates Tumor Growth by Increasing Fibronectin Fibril Assembly in the Tumor Microenvironment
Yaqoob, Usman , Cao, Sheng , Shergill, Uday, Jagavelu, Kumaravelu , Geng, Zhimin , Yin, Meng , Assuncao, Thiago M. de , Cao, Ying , Szabolcs, Anna, Thorgeirsson, Snorri S., Yang, Ju , Roberts, Lewis R. , Shah, Vijay H. , Yaqoob, Usman , Schwartz, Martin A. , Ehman, Richard L. , Mukhopadhyay, Debabrata , Roberts, Lewis R , Yin, Meng

Mayo Clinic

Cancer Research | June 27, 2012 | Volume: 72 | Issue: 16 | Pages: 4047-4059

10.1158/0008-5472.can-11-3907 | PMID 22738912 Get It

Abstract The tumor microenvironment, including stromal myofibroblasts and associated matrix proteins, regulates cancer cell invasion and proliferation. Here, we report that neuropilin-1 (NRP-1) orchestrates communications between myofibroblasts and soluble fibronectin that promote α5β1 integrin–dependent fibronectin fibril assembly, matrix stiffness, and tumor growth. Tumor growth and fibronectin fibril assembly were reduced by genetic depletion or antibody neutralization of NRP-1 from stromal myofibroblasts in vivo. Mechanistically, the increase in fibronectin fibril assembly required glycosylation of serine 612 of the extracellular domain of NRP-1, an intact intracellular NRP-1 SEA domain, and intracellular associations between NRP-1, the scaffold protein GIPC, and the nonreceptor tyrosine kinase c-Abl that augmented α5β1 fibronectin fibril assembly activity. Analysis of human cancer specimens established an association between tumoral NRP-1 levels and clinical outcome. Our findings indicate that NRP-1 activates the tumor microenvironment, thereby promoting tumor growth. These results not only identify new molecular mechanisms of fibronectin fibril assembly but also have important implications for therapeutic targeting of the myofibroblast in the tumor microenvironment. Cancer Res; 72(16); 4047–59. ©2012 AACR.
VEGF Exerts an Angiogenesis-Independent Function in Cancer Cells to Promote Their Malignant Progression
Cao, Ying , Guangqi, E, Wang, Enfeng , Pal, Krishnendu , Dutta, Shamit K., Bar‐Sagi, Dafna , Mukhopadhyay, Debabrata , Pal, Krishnendu

Mayo Clinic

Cancer Research | June 13, 2012 | Volume: 72 | Issue: 16 | Pages: 3912-3918

10.1158/0008-5472.can-11-4058 | PMID 22693250 Get It

Abstract VEGF/vascular permeability factor (VEGF/VPF or VEGF-A) is a pivotal driver of cancer angiogenesis that is a central therapeutic target in the treatment of malignancy. However, little work has been devoted to investigating functions of VEGF that are independent of its proangiogenic activity. Here, we report that VEGF produced by tumor cells acts in an autocrine manner to promote cell growth through interaction with the VEGF receptor neuropilin-1 (NRP-1). Reducing VEGF expression by tumor cells induced a differentiated phenotype in vitro and inhibited tumor forming capacity in vivo, independent of effects on angiogenesis. Autocrine activation of tumor cell growth was dependent on signaling through NRP-1, and Ras was determined to be a critical effector signaling molecule downstream of NRP-1. Our findings define a novel function for VEGF in dedifferentiation of tumor cells expanding its role in cancer beyond its known proangiogenic function. Cancer Res; 72(16); 3912–8. ©2012 AACR.
Revealing the role of phospholipase Cβ3 in the regulation of VEGF-induced vascular permeability
Hoeppner, Luke H. , Phoenix, Kathryn N., Clark, Karl J. , Gong, Xun , Sciuto, Tracey , Vohra, Pawan K., Suresh, Sandip , Dvořàk, Ann M., Ekker, Stephen C. , Dvorak, Harold F., Claffey, Kevin P. , Bhattacharya, Resham , Bhattacharya, Santanu , Mukhopadhyay, Debabrata , Ekker, Stephen C , Clark, Karl J , Gong, Xun

Mayo Clinic

Blood | June 7, 2012 | Volume: 120 | Issue: 11 | Pages: 2167-2173

10.1182/blood-2012-03-417824 | PMID 22674805 Get It

AbstractVEGF induces vascular permeability (VP) in ischemic diseases and cancer, leading to many pathophysiological consequences. The molecular mechanisms by which VEGF acts to induce hyperpermeability are poorly understood and in vivo models that easily facilitate real-time, genetic studies of VP do not exist. In the present study, we report a heat-inducible VEGF transgenic zebrafish (Danio rerio) model through which VP can be monitored in real time. Using this approach with morpholino-mediated gene knock-down and knockout mice, we describe a novel role of phospholipase Cβ3 as a negative regulator of VEGF-mediated VP by regulating intracellular Ca2+ release. Our results suggest an important effect of PLCβ3 on VP and provide a new model with which to identify genetic regulators of VP crucial to several disease processes.