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27 results on '"Zucker, Shoshanna N."'

1. The Development of Nonthermal Plasma and Tirapazamine as a Novel Combination Therapy to Treat Melanoma In Situ

Author

Yehl, Matthew, primary, Kucharski, Dominik, additional, Eubank, Michelle, additional, Gulledge, Brandon, additional, Rayan, Gamal, additional, Uddin, Md Gias, additional, Remmers, Genevieve, additional, Kandel, Eugene S., additional, DuFaux, Douglas P., additional, Hutcherson, Timothy C., additional, Sexton, Sandra, additional, and Zucker, Shoshanna N., additional

Published
2023
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6. Abstract B32: A novel combination therapy for metastatic melanoma potentiates a gap junction positive feedback mechanism

Author

Bagati, Archis, primary, Koch, Zethan, additional, Hutcherson, Timothy C., additional, Pechette, Joseph, additional, Dianat, Hossein, additional, Higley, Cory, additional, Chiu, Lisa, additional, Song, Yesul, additional, Shah, Jay, additional, Chazen, Elana, additional, Nicolais, Andrew, additional, Casey, Peter, additional, Thompson, Kyle, additional, Nikiforov, Mikhail A., additional, Zirnheld, Jennifer, additional, and Zucker, Shoshanna N., additional

Published
2020
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7. Novel combination therapy for melanoma induces apoptosis via a gap junction positive feedback mechanism

Author

Bagati, Archis, primary, Hutcherson, Timothy C., additional, Koch, Zethan, additional, Pechette, Joseph, additional, Dianat, Hossein, additional, Higley, Cory, additional, Chiu, Lisa, additional, Song, Yesul, additional, Shah, Jay, additional, Chazen, Elana, additional, Nicolais, Andrew, additional, Casey, Peter, additional, Thompson, Kyle, additional, Burke, Kevin, additional, Nikiforov, Mikhail A., additional, Zirnheld, Jennifer, additional, and Zucker, Shoshanna N., additional

Published
2020
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10. A Modified In vitro Invasion Assay to Determine the Potential Role of Hormones, Cytokines and/or Growth Factors in Mediating Cancer Cell Invasion

Author

Bagati, Archis, Koch, Zethan, Bofinger, Diane, Goli, Haneesha, Weiss, Laura S., Dau, Rosie, Thomas, Megha, and Zucker, Shoshanna N.

Subjects
Cell Culture Techniques, In Vitro Techniques, Hormones, Culture Media, Cell Movement, Cell Line, Tumor, Neoplasms, Medicine, Animals, Cytokines, Humans, Intercellular Signaling Peptides and Proteins, Cattle, Neoplasm Invasiveness, sense organs
Abstract

Blood serum serves as a chemoattractant towards which cancer cells migrate and invade, facilitating their intravasation into microvessels. However, the actual molecules towards which the cells migrate remain elusive. This modified invasion assay has been developed to identify targets which drive cell migration and invasion. This technique compares the invasion index under three conditions to determine whether a specific hormone, growth factor, or cytokine plays a role in mediating the invasive potential of a cancer cell. These conditions include i) normal fetal bovine serum (FBS), ii) charcoal-stripped FBS (CS-FBS), which removes hormones, growth factors, and cytokines and iii) CS-FBS + molecule (denoted "X"). A significant change in cell invasion with CS-FBS as compared to FBS, indicates the involvement of hormones, cytokines or growth factors in mediating the change. Individual molecules can then be added back to CS-FBS to assay their ability to reverse or rescue the invasion phenotype. Furthermore, two or more factors can be combined to evaluate the additive or synergistic effects of multiple molecules in driving or inhibiting invasion. Overall, this method enables the investigator to determine whether hormones, cytokines, and/or growth factors play a role in cell invasion by serving as chemoattractants or inhibitors of invasion for a particular type of cancer cell or a specific mutant. By identifying specific chemoattractants and inhibitors, this modified invasion assay may help to elucidate signaling pathways that direct cancer cell invasion.

Published
2015

15. Cell coupling mediated by connexin 26 selectively contributes to reduced adhesivity and increased migration.

Author

Polusani, Srikanth R., Kalmykov, Edward A., Chandrasekhar, Anjana, Zucker, Shoshanna N., and Nicholson, Bruce J.

Subjects
CONNEXINS, GAP junctions (Cell biology), CELL motility
Abstract

Gap junction proteins (connexins) have crucial effects on cell motility in many systems, from migration of neural crest cells to promotion of metastatic invasiveness. Here, we show that expression of Cx26 (also known as GJB2) in HeLa cells specifically enhances cell motility in scrape wounding and sparse culture models. This effect is dependent on gap junction channels and is isotype specific [Cx26 enhances motility, whereas Cx43 (also known as GJA1) does not and Cx32 (also known as GJB1) has an intermediate effect]. The increased motility is associated with reduced cell adhesiveness, caused by loss of N-cadherin protein and RNA at the wound edge. This in turn causes a redistribution of N-cadherin-binding proteins (p120 catenin and β- catenin) to the cytosol and nucleus, respectively. The former activates Rac-1, which mediates cytoskeletal rearrangements needed for filopod extension. The latter is associated with increased expression of urokinase plasminogen activating receptor (an activator of extracellular proteases) and secretion of extracellular matrix components like collagen. Although these effects were dependent on Cx26-mediated coupling of the cells, they are not mediated by the same signal (i.e. cAMP) through which Cx26 has been shown to suppress proliferation in the same system. [ABSTRACT FROM AUTHOR]

Published
2016
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16. Nrf2 Amplifies Oxidative Stress via Induction of Klf9

Author

Zucker, Shoshanna N., primary, Fink, Emily E., additional, Bagati, Archis, additional, Mannava, Sudha, additional, Bianchi-Smiraglia, Anna, additional, Bogner, Paul N., additional, Wawrzyniak, Joseph A., additional, Foley, Colleen, additional, Leonova, Katerina I., additional, Grimm, Melissa J., additional, Moparthy, Kalyana, additional, Ionov, Yurij, additional, Wang, Jianmin, additional, Liu, Song, additional, Sexton, Sandra, additional, Kandel, Eugene S., additional, Bakin, Andrei V., additional, Zhang, Yuesheng, additional, Kaminski, Naftali, additional, Segal, Brahm H., additional, and Nikiforov, Mikhail A., additional

Published
2014
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18. A Purine Nucleotide Biosynthesis Enzyme Guanosine Monophosphate Reductase Is a Suppressor of Melanoma Invasion

Author

Wawrzyniak, Joseph A., primary, Bianchi-Smiraglia, Anna, additional, Bshara, Wiam, additional, Mannava, Sudha, additional, Ackroyd, Jeff, additional, Bagati, Archis, additional, Omilian, Angela R., additional, Im, Michael, additional, Fedtsova, Natalia, additional, Miecznikowski, Jeffrey C., additional, Moparthy, Kalyana C., additional, Zucker, Shoshanna N., additional, Zhu, Qianqian, additional, Kozlova, Nadezhda I., additional, Berman, Albert E., additional, Hoek, Keith S., additional, Gudkov, Andrei V., additional, Shewach, Donna S., additional, Morrison, Carl D., additional, and Nikiforov, Mikhail A., additional

Published
2013
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24. Mutation of a Conserved Threonine in the Third Transmembrane Helix of α- and β-Connexins Creates a Dominant-negative Closed Gap Junction Channel

Author

Beahm, Derek L., primary, Oshima, Atsunori, additional, Gaietta, Guido M., additional, Hand, Galen M., additional, Smock, Amy E., additional, Zucker, Shoshanna N., additional, Toloue, Masoud M., additional, Chandrasekhar, Anjana, additional, Nicholson, Bruce J., additional, and Sosinsky, Gina E., additional

Published
2006
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26. A dominant negative Cx43 mutant differentially affects tumorigenic and invasive properties in human metastatic melanoma cells.

Author

Zucker, Shoshanna N., Bancroft, Tara A., Place, David E., Des Soye, Benjamin, Bagati, Archis, and Berezney, Ronald

Subjects
*CONNEXINS, *METASTASIS, *CANCER cells, *GENETIC mutation, *CARCINOGENESIS, *CELL migration, *TUMOR suppressor proteins
Abstract

Previous reports have implicated connexin 43 (Cx43) as a tumor suppressor in early stages of tumorigenesis and in some cases as an enhancer of cell migration in later stages. To address the role of Cx43 in melanoma tumor progression, we utilized two melanoma cell lines derived from the same patient in pre-metastasis (WM793B) and following isolation from a lung metastasis in nude mice (1205Lu). Our results demonstrate a strikingly increased expression of Cx43 in both the pre-metastatic and metastatic melanoma cell lines that were actively migrating compared to non-migrating cells. To further investigate the role of Cx43 in these melanoma cells, we overexpressed wild type (wt) Cx43 as well as a mutant dominant negative Cx43 mutant that causes closed channels (T154A). The metastatic 1205Lu cells expressing Cx43-T154A showed a twofold decrease in colony formation on soft agar while the nonmetastatic WM793B cells showed no significant change. In invasion assays through a collagen matrix, the same Cx43-T154A 1205Lu cells demonstrated a three- to fourfold increase in the invasion index compared to either wt Cx43 or vector control cells. The increase in invasiveness was eliminated by migration towards media with charcoal-stripped serum, suggesting that migration may be directed towards a lipophilic compound(s). Our findings demonstrate that a dominant negative Cx43 mutant deficient in channel formation exhibits a dual pattern of regulation in metastatic melanoma cells with a decrease in anchorage-independent growth and an increase in invasive potential. J. Cell. Physiol. 228: 853-859, 2013. © 2012 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]

Published
2013
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27. Mutation of a conserved threonine in the third transmembrane helix of alpha- and beta-connexins creates a dominant-negative closed gap junction channel.

Author

Beahm DL, Oshima A, Gaietta GM, Hand GM, Smock AE, Zucker SN, Toloue MM, Chandrasekhar A, Nicholson BJ, and Sosinsky GE

Subjects
Amino Acid Sequence, Animals, Baculoviridae metabolism, Cell Line, Connexin 26, Connexin 43 genetics, Cryoelectron Microscopy, Cysteine chemistry, Cytoplasm metabolism, DNA, Complementary metabolism, Electrophysiology, Fluorescent Dyes pharmacology, Gap Junctions, Genes, Dominant, HeLa Cells, Humans, Image Processing, Computer-Assisted, Insecta, Keratinocytes metabolism, Light, Microscopy, Electron, Microscopy, Fluorescence, Molecular Sequence Data, Mutagenesis, Site-Directed, Oocytes metabolism, Oxygen metabolism, Phylogeny, Point Mutation, RNA, Complementary metabolism, Rats, Time Factors, Transfection, Xenopus, Cell Membrane metabolism, Connexins chemistry, Connexins genetics, Mutation, Threonine chemistry
Abstract

Single site mutations in connexins have provided insights about the influence specific amino acids have on gap junction synthesis, assembly, trafficking, and functionality. We have discovered a single point mutation that eliminates functionality without interfering with gap junction formation. The mutation occurs at a threonine residue located near the cytoplasmic end of the third transmembrane helix. This threonine is strictly conserved among members of the alpha- and beta-connexin subgroups but not the gamma-subgroup. In HeLa cells, connexin43 and connexin26 mutants are synthesized, traffic to the plasma membrane, and make gap junctions with the same overall appearance as wild type. We have isolated connexin26T135A gap junctions both from HeLa cells and baculovirus-infected insect Sf9 cells. By using cryoelectron microscopy and correlation averaging, difference images revealed a small but significant size change within the pore region and a slight rearrangement of the subunits between mutant and wild-type connexons expressed in Sf9 cells. Purified, detergent-solubilized mutant connexons contain both hexameric and partially disassembled structures, although wild-type connexons are almost all hexameric, suggesting that the three-dimensional mutant connexon is unstable. Mammalian cells expressing gap junction plaques composed of either connexin43T154A or connexin26T135A showed an absence of dye coupling. When expressed in Xenopus oocytes, these mutants, as well as a cysteine substitution mutant of connexin50 (connexin50T157C), failed to produce electrical coupling in homotypic and heteromeric pairings with wild type in a dominant-negative effect. This mutant may be useful as a tool for knocking down or knocking out connexin function in vitro or in vivo.

Published
2006
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