Las Vegas, NV, United States
Las Vegas, NV, United States

Nevada Cancer Institute , founded in 2002, was the official cancer institute for the state of Nevada from 2003 to 2013, located in Summerlin, Nevada. The Institute became part of the UC San Diego Health System in February, 2012. A non-profit organization, NVCI served patients throughout the greater Las Vegas area, offering full-service clinics in Summerlin, Nevada, and at University Medical Center, in the downtown medical district. The Institute’s mobile screening unit, the Hope Coach, has provided mammography services throughout the state.NVCI has served more than 17,000 patients since opening in 2005. The Institute was dedicated to providing innovative and collaborative cancer care, clinical trials and community education.The Institute closed on January 31, 2013. Wikipedia.


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News Article | October 31, 2016
Site: marketersmedia.com

— Des Hague, Froozer® Chairman of the Board, and Rich Naha, Froozer® CEO, recently announced that Joseph C. Essa, President of Wolfgang Puck Worldwide, has been appointed to the Board of Directors, effective immediately. "We are delighted to have Joe join our Board of Directors," stated Des Hague, "and we are confident that Joe will have an immediate positive impact on Froozer®. He will be able to share best practices in navigating our retail channels, accelerating key introductions in the military channel, expanding our broker network in numerous channels and helping us refine our overall position in the market." As President of Wolfgang Puck Worldwide, Essa's responsibilities include building and leading an executive team as well as the related strategic plan and systems for this successful casual restaurant and consumer product business with annual retail revenues of $250 million. Prior to joining the Wolfgang Puck Fine Dining Group, Essa worked with restaurateur Pino Luongo in New York City as Vice President of Operations at TOSCORP, Inc., which includes the restaurant concepts Coco Pazzo, Le Madri and Tuscan Square. He also founded and operated two successful restaurants, Assaggio in West Hartford, Connecticut and Café Pasta in Greensboro, North Carolina. Essa graduated cum laude from Boston College with a bachelor of science in accounting and finance. He is a Certified Public Accountant and is accredited by the National Restaurant Association. His community involvement includes personal work with charitable organizations benefiting Meals on Wheels, Alzheimer's research, Nevada Cancer Institute, Nevada Public Education Foundation and March of Dimes, among others. "Joe's experience and proven track record in managing global brands is invaluable to Froozer®," stated Naha. "We believe that Joe will truly help to accelerate the growth and relevance of the brand." "I am honored to join the Froozer® board, and look forward to supporting Rich Naha, his talented team of industry professionals and the very exciting Froozer® product line," said Essa. About Froozer® - "simple ingredients. real nutrition." Froozer® products, the official healthy frozen fruit & veggie snack partner of US Speed Skating, represent the pure goodness of freshly harvested fruits & veggies picked at the peak of their ripeness, flash-frozen whole and blended for optimal taste, nutrition and digestion. Natural fruits and veggies in all their glory, nothing added or subtracted, not even a drop of water. Available in three delicious flavors - STRAWBANANA BLISS, TROPICAL SUNSET and BLUE ALOHA - in 6-pack boxes. Look for Froozer® in your local grocery store freezer at select fine retail locations in the Denver Area, including WholeFoods and Alfalfa's, and various select retailers in Arizona, California, Connecticut, Oregon, Washington State, Rhode Island and Alaska, or place your order for a 48-count box at http://www.Froozer.com or http://www.amazon.com to have your Froozer® delivered directly to your home or office. For more information, please visit http://froozer.com


Foon K.A.,Nevada Cancer Institute | Hallek M.J.,University of Cologne
Leukemia | Year: 2010

Progress in our understanding of chronic lymphocytic leukemia and its treatment has resulted in a more tailored approach to patient management, with different therapeutic regimens for different patient populations. The current standard of care has evolved from single-agent therapy with chlorambucil or cyclophosphamide, through the introduction of purine analogs to the more recent introduction of chemoimmunotherapy. Selection of appropriate initial therapy should be based primarily on patient characteristics such as age, performance status and the expected clinical course of the leukemia based on established risk factors. Achieving a complete and durable response is the major goal for fit patients; chemoimmunotherapy with fludarabine, cyclophosphamide and rituximab would be advantageous. Alternatively, in unfit patients, controlling symptoms is the essential treatment goal and a regimen with a more favorable toxicity profile should be applied. This manuscript reviews the data that has lead to current treatment choices, advises on tailored therapies and discusses emerging trends. Data for this review was identified by a search of electronic information including Medline and PubMed databases, conference proceedings and trial registers. Critical analysis of extracted data was undertaken with attention to trial phase, treatment schedules and end points, including response rates, follow-up times, progression-free survival and overall survival. © 2010 Macmillan Publishers Limited All rights reserved.


Lorico A.,Nevada Cancer Institute | Rappa G.,Nevada Cancer Institute
Journal of Oncology | Year: 2011

Many types of tumors are organized in a hierarchy of heterogeneous cell populations, with only a small proportion of cancer stem cells (CSCs) capable of sustaining tumor formation and growth, giving rise to differentiated cells, which form the bulk of the tumor. Proof of the existence of CSC comes from clinical experience with germ-cell cancers, where the elimination of a subset of undifferentiated cells can cure patients (Horwich et al., 2006), and from the study of leukemic cells (Bonnet and Dick, 1997; Lapidot et al., 1994; and Yilmaz et al., 2006). The discovery of CSC in leukemias as well as in many solid malignancies, including breast carcinoma (Al-Hajj et al. 2003; Fang et al., 2005; Hemmati et al., 2003; Kim et al., 2005; Lawson et al., 2007; Li et al., 2007; Ricci-Vitiani et al., 2007; Singh et al., 2003; and Xin et al., 2005), has suggested a unifying CSC theory of cancer development. The reported general insensitivity of CSC to chemotherapy and radiation treatment (Bao et al., 2006) has suggested that current anticancer drugs, which inhibit bulk replicating cancer cells, may not effectively inhibit CSC. The clinical relevance of targeting CSC-associated genes is supported by several recent studies, including CD44 targeting for treatment of acute myeloid leukemia (Jin et al., 2006), CD24 targeting for treatment of colon and pancreatic cancer (Sagiv et al., 2008), and CD133 targeting for hepatocellular and gastric cancer (Smith et al., 2008). One promising approach is to target CSC survival signaling pathways, where leukemia stem cell research has already made some progress (Mikkola et al., 2010). © 2011 Aurelio Lorico and Germana Rappa.


Le T.T.,Nevada Cancer Institute
BMC pharmacology & toxicology | Year: 2014

Tamoxifen, an agonist of estrogen receptor, is widely prescribed for the prevention and long-term treatment of breast cancer. A side effect of tamoxifen is fatty liver, which increases the risk for non-alcoholic fatty liver disease. Prevention of tamoxifen-induced fatty liver has the potential to improve the safety of long-term tamoxifen usage. Uridine, a pyrimidine nucleoside with reported protective effects against drug-induced fatty liver, was co-administered with tamoxifen in C57BL/6J mice. Liver lipid levels were evaluated with lipid visualization using coherent anti-Stokes Raman scatting (CARS) microscopy, biochemical assay measurement of triacylglyceride (TAG), and liquid chromatography coupled with mass spectrometry (LC-MS) measurement of membrane phospholipid. Blood TAG and cholesterol levels were measured. Mitochondrial respiration of primary hepatocytes in the presence of tamoxifen and/or uridine was evaluated by measuring oxygen consumption rate with an extracellular flux analyzer. Liver protein lysine acetylation profiles were evaluated with 1D and 2D Western blots. In addition, the relationship between endogenous uridine levels, fatty liver, and tamoxifen administration was evaluated in transgenic mice UPase1-/-and UPase1-TG. Uridine co-administration prevented tamoxifen-induced liver lipid droplet accumulation in mice. The most prominent effect of uridine co-administration with tamoxifen was the stimulation of liver membrane phospholipid biosynthesis. Uridine had no protective effect against tamoxifen-induced impairment to mitochondrial respiration of primary hepatocytes or liver TAG and cholesterol export. Uridine had no effect on tamoxifen-induced changes to liver protein acetylation profile. Transgenic mice UPase1-/-with increased pyrimidine salvage activity were protected against tamoxifen-induced liver lipid droplet accumulation. In contrast, UPase1-TG mice with increased pyrimidine catabolism activity had intrinsic liver lipid droplet accumulation, which was aggravated following tamoxifen administration. Uridine co-administration was effective at preventing tamoxifen-induced liver lipid droplet accumulation. The ability of uridine to prevent tamoxifen-induced fatty liver appeared to depend on the pyrimidine salvage pathway, which promotes biosynthesis of membrane phospholipid.


Rappa G.,Nevada Cancer Institute | Mercapide J.,Nevada Cancer Institute | Lorico A.,Nevada Cancer Institute
American Journal of Pathology | Year: 2012

Breast cancer progression involves cancer cell heterogeneity, with generation of invasive/metastatic breast cancer cells within populations of nonmetastatic cells of the primary tumor. Sequential genetic mutations, epithelial-to-mesenchymal transition, interaction with local stroma, and formation of hybrids between cancer cells and normal bone marrow-derived cells have been advocated as tumor progression mechanisms. We report herein the spontaneous in vitro formation of heterotypic hybrids between human bone marrow-derived multipotent stromal cells (MSCs) and two different breast carcinoma cell lines, MDA-MB-231 (MDA) and MA11. Hybrids showed predominantly mesenchymal morphological characteristics, mixed gene expression profiles, and increased DNA ploidy. Both MA11 and MDA hybrids were tumorigenic in immunodeficient mice, and some MDA hybrids had an increased metastatic capacity. Both in culture and as xenografts, hybrids underwent DNA ploidy reduction and morphological reversal to breast carcinoma-like morphological characteristics, while maintaining a mixed breast cancer-mesenchymal expression profile. Analysis of coding single-nucleotide polymorphisms by RNA sequencing revealed genetic contributions from both parental partners to hybrid tumors and metastasis. Because MSCs migrate and localize to breast carcinoma, our findings indicate that formation of MSC-breast cancer cell hybrids is a potential mechanism of the generation of invasive/metastatic breast cancer cells. Our findings reconcile the fusion theory of cancer progression with the common observation that breast cancer metastases are generally aneuploid, but not tetraploid, and are histopathologically similar to the primary neoplasm. © 2012 American Society for Investigative Pathology.


Roosild T.P.,Nevada Cancer Institute
PloS one | Year: 2010

Uridine phosphorylase (UPP) is a central enzyme in the pyrimidine salvage pathway, catalyzing the reversible phosphorolysis of uridine to uracil and ribose-1-phosphate. Human UPP activity has been a focus of cancer research due to its role in activating fluoropyrimidine nucleoside chemotherapeutic agents such as 5-fluorouracil (5-FU) and capecitabine. Additionally, specific molecular inhibitors of this enzyme have been found to raise endogenous uridine concentrations, which can produce a cytoprotective effect on normal tissues exposed to these drugs. Here we report the structure of hUPP1 bound to 5-FU at 2.3 A resolution. Analysis of this structure reveals new insights as to the conformational motions the enzyme undergoes in the course of substrate binding and catalysis. The dimeric enzyme is capable of a large hinge motion between its two domains, facilitating ligand exchange and explaining observed cooperativity between the two active sites in binding phosphate-bearing substrates. Further, a loop toward the back end of the uracil binding pocket is shown to flexibly adjust to the varying chemistry of different compounds through an "induced-fit" association mechanism that was not observed in earlier hUPP1 structures. The details surrounding these dynamic aspects of hUPP1 structure and function provide unexplored avenues to develop novel inhibitors of this protein with improved specificity and increased affinity. Given the recent emergence of new roles for uridine as a neuron protective compound in ischemia and degenerative diseases, such as Alzheimer's and Parkinson's, inhibitors of hUPP1 with greater efficacy, which are able to boost cellular uridine levels without adverse side-effects, may have a wide range of therapeutic applications.


Johlfs M.G.,Nevada Cancer Institute | Fiscus R.R.,Nevada Cancer Institute
Neurochemistry International | Year: 2010

Previous studies from our laboratory have shown that the cGMP/protein kinase G (PKG) signaling pathway plays an essential role in preventing spontaneous apoptosis in neural cells; however, the mechanism is not understood. A potential downstream target of PKG is the apoptosis-regulating protein Bad, which contains a sequence around its serine 155 (ser155 in mouse Bad, equivalent to ser118 in human Bad) predicted to be a consensus motif for PKG-catalyzed phosphorylation. Using both in vitro and cell-based experiments, we determined if PKG phosphorylates Bad at ser155 and if blocking/stimulating PKG-catalyzed Bad phosphorylation causes pro-apoptotic/anti-apoptotic responses. Recombinant PKG type-Iα (PKG-Iα) was found to directly phosphorylate recombinant Bad at ser155 in vitro. In N1E-115 mouse neural cells, which naturally express PKG-Iα as the predominant PKG isoform, addition of 8-Br-cGMP (0.1-1.0 mM), a cell-permeable direct PKG-Iα activator, increased ser155 phosphorylation of Bad. ODQ (50 μM), a soluble guanylyl cyclase inhibitor that lowers cGMP/PKG activity, decreased serum-induced ser155 phosphorylation of Bad and induced apoptosis in N1E-115 cells. Treatment with DT-2 and DT-3, selective PKG-Iα inhibitors, both decreased Bad ser155 phosphorylation and induced apoptosis. The data indicate that PKG-Iα directly phosphorylates Bad at ser155, which may participate in cGMP/PKG-induced anti-apoptotic/cytoprotective effects in neural cells. © 2010 Elsevier Ltd. All rights reserved.


Rappa G.,Nevada Cancer Institute | Lorico A.,Nevada Cancer Institute
Experimental Cell Research | Year: 2010

The phenotypic diversity of breast carcinoma may be explained by the existence of a sub-population of breast cancer cells, endowed with stem cell-like properties and gene expression profiles, able to differentiate along different pathways. A stem cell-like population of CD44+CD24-/low breast cancer cells was originally identified using cells from metastatic pleural effusions of breast carcinoma patients. We have previously reported that upon in vitro culture as mammospheres under stem cell-like conditions, human MA-11 breast carcinoma cells acquired increased tumorigenicity and lost CD24 expression compared with the parental cell line. We now report that upon passage of MA-11 mammospheres into serum-supplemented cultures, CD24 expression was restored; the rapid increase in CD24 expression was consistent with up-regulation of the antigen, and not with in vitro selection of CD24+ cells. In tumors derived from subcutaneous injection of MA-11 mammospheres in athymic nude mice, 76.1±9.7% of cells expressed CD24, vs. 0.5±1% in MA-11 cells dissociated from mammospheres before injection. The tumorigenicity of sorted CD44+CD24- and CD44+CD24high MA-11 cells was equal. Single cell-sorted CD24- and CD24high MA-11 gave rise in vitro to cell populations with heterogeneous CD24 expression. Also, subcutaneous tumors derived from sorted CD24- sub-populations and single-cell clones had levels of CD24 expression similar to the unsorted cells. To investigate whether the high expression of CD24 contributed to the tumorigenic potential of MA-11 cells, we silenced CD24 by shRNA. CD24 silencing (95%) resulted in no difference in tumorigenicity upon s.c. injection in athymic nude mice compared with mock-transduced MA-11 cells. Since CD24 silencing was maintained in vivo, our data suggest that the level of expression of CD24 is associated with but does not contribute to tumorigenicity. We then compared the molecular profile of the mammospheres with the adherent cell fraction. Gene expression profiling revealed that the increased tumorigenicity of MA-11 mammospheres was associated with changes in 10 signal transduction pathways, including MAP kinase, Notch and Wnt, and increased expression of aldehyde dehydrogenase, a cancer-initiating cell-associated marker. Our data demonstrate that (i) the level of CD24 expression is neither a stable feature of mammosphere-forming cells nor confers tumorigenic potential to MA-11 cells; (ii) cancer-initiating cell-enriched MA-11 mammospheres have activated specific signal transduction pathways, potential targets for anti-breast cancer therapy. © 2010 Elsevier Inc.


Gao Z.,Nevada Cancer Institute | Xu C.W.,Nevada Cancer Institute
Biochemical and Biophysical Research Communications | Year: 2011

Histone modifications play an important role in transcriptional regulation and are intimately involved in important biological and disease processes. Despite their functional significance, whether and how extracellular signals modulate histone modifications are not well defined. Using mono-ubiquitination of histone H2B as a model system, we have previously shown that mono-ubiquitination of histone H2B is induced by glucose through glycolysis in budding yeast Sacchromyces cerevisiae [1]. Because histones are well conserved proteins among eukaryotes and glycolysis is the most conserved metabolic pathway, we reasoned that the glucose-glycolysis-uH2B signal pathway originally discovered in yeast may be conserved in human cells. Using cultured human glioma cells as a model, we show in this report that extracellular media modulated global levels of mono-ubiquitination of histone H2B at K120 (uH2B). Nutrient deprivation removed the ubiquitin moiety of uH2B. Glucose-containing media induced uH2B in the cells while media lacking glucose had no effect on the induction of uH2B, suggesting that glucose was required for inducing uH2B in the cells. In contrast, non-metabolic glucose analogs were defective in inducing uH2B, suggesting that glucose metabolism was required for glucose-induced mono-ubiquitination in the cultured glioma cells. Moreover, shRNA knockdown of PKM2, an essential enzyme for glycolysis in malignant tumors, inhibited mono-ubiquitination of histone H2B in these cells. Taken together, our previous and current results demonstrate that the novel glucose-glycolysis-uH2B signal pathway is well conserved from yeast to mammalian cells, providing an evolutionarily-conserved regulatory mechanism of histone modifications. © 2010 Elsevier Inc.


Patent
Nevada Cancer Institute | Date: 2012-05-15

The present invention relates to the compositions, formulations and methods of treating fatty liver disorders, such as non-alcoholic fatty liver disease (NAFLD) and non-alcoholic steatohepatitis (NASH) and their sequelae by administration of uridine or a compound that modulates one or more uridine phosphorylases in a subject in need thereof.

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