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Dutta, Shamit K.

Mayo Clinic

Mayo Clinic

Citations 44

Molecular Inhibitor of QSOX1 Suppresses Tumor Growth In Vivo
Fifield, Amber L. , Hanavan, Paul D., Faigel, Douglas O. , Sergienko, Eduard , Bobkov, Andrey A. , Meurice, Nathalie , Polito, Alysia, Caulfield, Thomas R. , Castle, Erik P., Copland, John A. , Pal, Krishnendu , Dutta, Shamit K., Luo, Huijun , Ho, Thai H. , Lake, Douglas F. , Petit, Joachim L. , Pal, Krishnendu , Ho, Thai , Caulfield, Thomas R , Meurice, Nathalie , Mukhopadhyay, Debabrata

Molecular Cancer Therapeutics | October 1, 2019 | Volume: 19 | Issue: 1 | Pages: 112-122

10.1158/1535-7163.mct-19-0233 Get It

Abstract Quiescin sulfhydryl oxidase 1 (QSOX1) is an enzyme overexpressed by many different tumor types. QSOX1 catalyzes the formation of disulfide bonds in proteins. Because short hairpin knockdowns (KD) of QSOX1 have been shown to suppress tumor growth and invasion in vitro and in vivo, we hypothesized that chemical compounds inhibiting QSOX1 enzymatic activity would also suppress tumor growth, invasion, and metastasis. High throughput screening using a QSOX1-based enzymatic assay revealed multiple potential QSOX1 inhibitors. One of the inhibitors, known as “SBI-183,” suppresses tumor cell growth in a Matrigel-based spheroid assay and inhibits invasion in a modified Boyden chamber, but does not affect viability of nonmalignant cells. Oral administration of SBI-183 inhibits tumor growth in 2 independent human xenograft mouse models of renal cell carcinoma. We conclude that SBI-183 warrants further exploration as a useful tool for understanding QSOX1 biology and as a potential novel anticancer agent in tumors that overexpress QSOX1.
DNA–SWCNT Biosensors Allow Real-Time Monitoring of Therapeutic Responses in Pancreatic Ductal Adenocarcinoma
Gong, Xun , Wang, Enfeng , Dutta, Shamit K., Caplette, Joseph R., Son, Manki, Nguyen, Freddy T. , Strano, Michael S. , Gong, Xun , Nguyen, Freddy T , Bhattacharya, Santanu , Mukhopadhyay, Debabrata

Cancer Research | July 10, 2019 | Volume: 79 | Issue: 17 | Pages: 4515-4523

10.1158/0008-5472.can-18-3337 Get It

Abstract Pancreatic ductal adenocarcinoma (PDAC) is a highly desmoplastic cancer with limited treatment options. There is an urgent need for tools that monitor therapeutic responses in real time. Drugs such as gemcitabine and irinotecan elicit their therapeutic effect in cancer cells by producing hydrogen peroxide (H2O2). In this study, specific DNA-wrapped single-walled carbon nanotubes (SWCNT), which precisely monitor H2O2, were used to determine the therapeutic response of PDAC cells in vitro and tumors in vivo. Drug therapeutic efficacy was evaluated in vitro by monitoring H2O2 differences in situ using reversible alteration of Raman G-bands from the nanotubes. Implantation of the DNA–SWCNT probe inside the PDAC tumor resulted in approximately 50% reduction of Raman G-band intensity when treated with gemcitabine versus the pretreated tumor; the Raman G-band intensity reversed to its pretreatment level upon treatment withdrawal. In summary, using highly specific and sensitive DNA-SWCNT nanosensors, which can determine dynamic alteration of hydrogen peroxide in tumor, can evaluate the effectiveness of chemotherapeutics. Significance: A novel biosensor is used to detect intratumoral hydrogen peroxide, allowing real-time monitoring of responses to chemotherapeutic drugs.
Multifaceted peptide assisted one-pot synthesis of gold nanoparticles for plectin-1 targeted gemcitabine delivery in pancreatic cancer
Pal, Krishnendu , Al-suraih, Farah, González-Rodríguez, Roberto , Dutta, Shamit K., Wang, Enfeng , Kwak, H. Shaun , Caulfield, Thomas R. , Coffer, Jeffery L. , Bhattacharya, Santanu , Caulfield, Thomas R , Pal, Krishnendu , Bhattacharya, Santanu

Nanoscale | September 29, 2017 | Volume: 9 | Issue: 40 | Pages: 15622-15634

10.1039/c7nr03172f Get It

Tumor-selective uptake of plectin-1 targeting peptide-modified gold nanoparticles ameliorates targeted delivery of gemcitabine in pancreatic ductal adenocarcinoma.
Preclinical efficacy of the novel competitive NAMPT inhibitor STF-118804 in pancreatic cancer
Espíndola‐Netto, Jair Machado , Chini, Claudia C.S. , Tarragó, Mariana G., Wang, Enfeng , Dutta, Shamit K., Pal, Krishnendu , Sola‐Penna, Mauro , Chini, Eduardo N. , Tarragó, Mariana, Dutta, Shamit, Mukhopadhyay, Debabrata , Pal, Krishnendu

Oncotarget | June 29, 2017 | Volume: 8 | Issue: 49 | Pages: 85054-85067

10.18632/oncotarget.18841 Get It

Immunosuppressive CD14 + HLA-DR lo/neg monocytes are elevated in pancreatic cancer and “primed” by tumor-derived exosomes
Javeed, Naureen , Gustafson, Michael P. , Dutta, Shamit K., Lin, Yi , Bamlet, William R. , Oberg, Ann L. , Petersen, Gloria M. , Chari, Suresh T. , Dietz, Allan B. , Mukhopadhyay, Debabrata , Dietz, Allan B , Bamlet, William R , Lin, Yi , Chari, Suresh T

OncoImmunology | November 2, 2016 | Volume: 6 | Issue: 1 | Pages: e1252013

10.1080/2162402x.2016.1252013 Get It

Mutant BRAF Upregulates MCL-1 to Confer Apoptosis Resistance that Is Reversed by MCL-1 Antagonism and Cobimetinib in Colorectal Cancer
Kawakami, Hisato , Huang, Shengbing, Dutta, Shamit K., Pal, Krishnendu , Mukhopadhyay, Debabrata , Sinicrope, Frank A.

Molecular Cancer Therapeutics | October 8, 2016 | Volume: 15 | Issue: 12 | Pages: 3015-3027

10.1158/1535-7163.mct-16-0017 Get It

Abstract Oncogenic BRAFV600E mutations activate MAPK signaling and are associated with treatment resistance and poor prognosis in patients with colorectal cancer. In BRAFV600E-mutant colorectal cancers, treatment failure may be related to BRAFV600E-mediated apoptosis resistance that occurs by an as yet undefined mechanism. We found that BRAFV600E can upregulate anti-apoptotic MCL-1 in a gene dose-dependent manner using colorectal cancer cell lines isogenic for BRAF. BRAFV600E-induced MCL-1 upregulation was confirmed by ectopic BRAFV600E expression that activated MEK/ERK signaling to phosphorylate (MCL-1Thr163) and stabilize MCL-1. Upregulation of MCL-1 was mediated by MEK/ERK shown by the ability of ERK siRNA to suppress MCL-1. Stabilization of MCL-1 by phosphorylation was shown by a phosphorylation-mimicking mutant and an unphosphorylated MCL-1 mutant that decreased or increased MCL-1 protein turnover, respectively. MEK/ERK inhibition by cobimetinib suppressed MCL-1 expression/phosphorylation and induced proapoptotic BIM to a greater extent than did vemurafenib in BRAFV600E cell lines. MCL-1 knockdown versus control shRNA significantly enhanced cobimetinib-induced apoptosis in vitro and in HT29 colon cancer xenografts. The small-molecule MCL-1 inhibitor, A-1210477, also enhanced cobimetinib-induced apoptosis in vitro that was due to disruption of the interaction of MCL-1 with proapoptotic BAK and BIM. Knockdown of BIM attenuated BAX, but not BAK, activation by cobimetinib plus A-1210477. In summary, BRAFV600E-mediated MEK/ERK activation can upregulate MCL-1 by phosphorylation/stabilization to confer apoptosis resistance that can be reversed by MCL-1 antagonism combined with cobimetinib, suggesting a novel therapeutic strategy against BRAFV600E-mutant CRCs. Mol Cancer Ther; 15(12); 3015–27. ©2016 AACR.
Glucocorticoid Receptor-Targeted Liposomal Codelivery of Lipophilic Drug and Anti-Hsp90 Gene: Strategy to Induce Drug-Sensitivity, EMT-Reversal, and Reduced Malignancy in Aggressive Tumors
Mondal, Sujan Kumar , Jinka, Sudhakar , Pal, Krishnendu , Nelli, Swetha, Dutta, Shamit K., Wang, Enfeng , Ahmad, Ajaz , Alkharfy, Khalid M. , Banerjee‬‬‬‬‬‬‬‬‬, Rintu , Dutta, Shamit Kumar, Mukhopadhyay, Debabrata , Pal, Krishnendu , Banerjee, Rajkumar

Molecular Pharmaceutics | May 17, 2016 | Volume: 13 | Issue: 7 | Pages: 2507-2523

10.1021/acs.molpharmaceut.6b00230 Get It

RhoC maintains vascular homeostasis by regulating VEGF-induced signaling in endothelial cells
Hoeppner, Luke H. , Wang, Ying , Dutta, Shamit K., Gong, Xun , Bedell, Victoria M. , Suresh, Sandip , Chun, Chang Zoon, Ramchandran, Ramani , Ekker, Stephen C. , Bhattacharya, Resham , Dutta, Shamit, Sinha, Sutapa , Mukhopadhyay, Debabrata , Ekker, Stephen C , Gong, Xun , Wang, Ying

Journal of Cell Science | July 2, 2015 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.1242/jcs.167601 Get It

Vasculogenesis and angiogenesis are controlled by vascular permeability factor/vascular endothelial growth factor A (VEGF). Dysregulation of these physiological processes contributes to the pathologies of heart disease, cancer and stroke. Rho GTPase proteins play an integral role in VEGF-mediated formation and maintenance of blood vessels. The regulatory functions of RhoA and RhoB in vasculogenesis and angiogenesis are well defined, whereas the purpose of RhoC remains poorly understood. Here, we describe how RhoC promotes vascular homeostasis by modulating endothelial cell migration, proliferation, and permeability. RhoC stimulates proliferation of human umbilical vein endothelial cells (HUVEC) by stabilizing nuclear β-catenin, which promotes transcription of cyclin D1 and subsequently drives cell cycle progression. RhoC negatively regulates endothelial cell migration through MAPK and downstream MLC-2 signaling and decreases vascular permeability through downregulation of the phospholipase Cγ (PLCγ)/Ca2+/eNOS cascade in HUVEC. Using a VEGF-inducible zebrafish (Danio rerio) model, we observed significantly less vascular permeability in RhoC morpholino (MO)-injected zebrafish than control MO-injected zebrafish. Taken together, our findings suggest RhoC is a key regulator of vascular homeostasis in endothelial cells.
Pathogenesis of pancreatic cancer exosome-induced lipolysis in adipose tissue
Sagar, Gunisha, Sah, Raghuwansh P., Javeed, Naureen , Dutta, Shamit K., Smyrk, Thomas C. , Lau, Julie S., Giorgadze, Nino, Tchkonia, Tamar , Kirkland, James L. , Chari, Suresh T. , Mukhopadhyay, Debabrata , Tchkonia, T , Chari, Suresh T

Gut | April 28, 2015 | Volume: 65 | Issue: 7 | Pages: 1165-1174

10.1136/gutjnl-2014-308350 Get It

Background and objectives New-onset diabetes and concomitant weight loss occurring several months before the clinical presentation of pancreatic cancer (PC) appear to be paraneoplastic phenomena caused by tumour-secreted products. Our recent findings have shown exosomal adrenomedullin (AM) is important in development of diabetes in PC. Adipose tissue lipolysis might explain early onset weight loss in PC. We hypothesise that lipolysis-inducing cargo is carried in exosomes shed by PC and is responsible for the paraneoplastic effects. Therefore, in this study we investigate if exosomes secreted by PC induce lipolysis in adipocytes and explore the role of AM in PC-exosomes as the mediator of this lipolysis. Design Exosomes from patient-derived cell lines and from plasma of patients with PC and non-PC controls were isolated and characterised. Differentiated murine (3T3-L1) and human adipocytes were exposed to these exosomes to study lipolysis. Glycerol assay and western blotting were used to study lipolysis. Duolink Assay was used to study AM and adrenomedullin receptor (ADMR) interaction in adipocytes treated with exosomes. Results In murine and human adipocytes, we found that both AM and PC-exosomes promoted lipolysis, which was abrogated by ADMR blockade. AM interacted with its receptor on the adipocytes, activated p38 and extracellular signal-regulated (ERK1/2) mitogen-activated protein kinases and promoted lipolysis by phosphorylating hormone-sensitive lipase. PKH67-labelled PC-exosomes were readily internalised into adipocytes and involved both caveolin and macropinocytosis as possible mechanisms for endocytosis. Conclusions PC-secreted exosomes induce lipolysis in subcutaneous adipose tissue; exosomal AM is a candidate mediator of this effect.
Pancreatic Cancer–Derived Exosomes Cause Paraneoplastic β-cell Dysfunction
Javeed, Naureen , Sagar, Gunisha, Dutta, Shamit K., Smyrk, Thomas C. , Lau, Julie S., Truty, Mark J. , Petersen, Gloria M. , Kaufman, Randal J. , Chari, Suresh T. , Truty, Mark, Bhattacharya, Santanu , Mukhopadhyay, Debabrata , Chari, Suresh T

Clinical Cancer Research | October 29, 2014 | Volume: 21 | Issue: 7 | Pages: 1722-1733

10.1158/1078-0432.ccr-14-2022 Get It

Abstract Purpose: Pancreatic cancer frequently causes diabetes. We recently proposed adrenomedullin as a candidate mediator of pancreatic β-cell dysfunction in pancreatic cancer. How pancreatic cancer–derived adrenomedullin reaches β cells remote from the cancer to induce β-cell dysfunction is unknown. We tested a novel hypothesis that pancreatic cancer sheds adrenomedullin-containing exosomes into circulation, which are transported to β cells and impair insulin secretion. Experimental Methods: We characterized exosomes from conditioned media of pancreatic cancer cell lines (n = 5) and portal/peripheral venous blood of patients with pancreatic cancer (n = 20). Western blot analysis showed the presence of adrenomedullin in pancreatic cancer-exosomes. We determined the effect of adrenomedullin-containing pancreatic cancer exosomes on insulin secretion from INS-1 β cells and human islets, and demonstrated the mechanism of exosome internalization into β cells. We studied the interaction between β-cell adrenomedullin receptors and adrenomedullin present in pancreatic cancer-exosomes. In addition, the effect of adrenomedullin on endoplasmic reticulum (ER) stress response genes and reactive oxygen/nitrogen species generation in β cells was shown. Results: Exosomes were found to be the predominant extracellular vesicles secreted by pancreatic cancer into culture media and patient plasma. Pancreatic cancer-exosomes contained adrenomedullin and CA19-9, readily entered β cells through caveolin-mediated endocytosis or macropinocytosis, and inhibited insulin secretion. Adrenomedullin in pancreatic cancer exosomes interacted with its receptor on β cells. Adrenomedullin receptor blockade abrogated the inhibitory effect of exosomes on insulin secretion. β cells exposed to adrenomedullin or pancreatic cancer exosomes showed upregulation of ER stress genes and increased reactive oxygen/nitrogen species. Conclusions: Pancreatic cancer causes paraneoplastic β-cell dysfunction by shedding adrenomedullin+/CA19-9+ exosomes into circulation that inhibit insulin secretion, likely through adrenomedullin-induced ER stress and failure of the unfolded protein response. Clin Cancer Res; 21(7); 1722–33. ©2014 AACR. See related commentary by Korc, p. 1508