Relevant bibliographies by topics / Cancer, Cancer cells, DU145, Cytochalasin D

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Academic literature on the topic 'Cancer, Cancer cells, DU145, Cytochalasin D'

Author: Grafiati
Published: 14 March 2023

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Journal articles on the topic "Cancer, Cancer cells, DU145, Cytochalasin D"

1

Dondi, D., R. Maggi, E. Scaccianoce, L. Martini, M. Motta, and A. Poletti. "Expression and role of functional glucocorticoid receptors in the human androgen-independent prostate cancer cell line, DU145." Journal of Molecular Endocrinology 26, no. 3 (June 1, 2001): 185–91. http://dx.doi.org/10.1677/jme.0.0260185.

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We investigated the presence of glucocorticoid receptors (GR) as well as the role of glucocorticoids (Gc) in the control of proliferation of the androgen-independent prostate cancer cell line, DU145. We detected the presence of a specific high affinity binding site (K(d) 2.3 nM) for [(3)H]dexamethasone ([(3)H]Dex) in the cytosolic preparations of DU145 cells; the density of these binding sites is significantly higher than that detected in HA22T/VGH and in HepG2, two hepatoma cell lines classically considered models for the study of GR. Immunocytochemistry studies confirmed the presence of GR in the cytosolic compartment of DU145 cells; GR undergo translocation to the nucleus following exposure to dexamethasone (Dex). The functional activity of GR present in DU145 cells was also studied by analyzing the potency of Dex in inducing chloramphenicol acyltransferase (CAT) activity in DU145 cells transfected with a glucocorticoid/progesterone response element (GRE/PRE) tkCAT plasmid (GRE/PREtkCAT plasmid). The results have shown that Dex stimulates the transcriptional activity of GR in transfected DU145 cells with an EC(50) of 9.65 nM and a maximal induction of sevenfold above basal levels. Finally, a dose-dependent (IC(50) 3.14 nM) decrease of DU145 cell numbers was observed after their exposure to Dex for 4 days; this effect was counteracted by the presence of the steroid antagonist, RU486. In conclusion, the present data suggest a possible role of corticoids in the control of the growth of androgen-independent prostate cancer.
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Wanyan, Yangke, Xixi Xu, Kehang Liu, Huidan Zhang, Junai Zhen, Rong Zhang, Jumei Wen, Ping Liu, and Yuqing Chen. "2-Deoxy-d-glucose Promotes Buforin IIb-Induced Cytotoxicity in Prostate Cancer DU145 Cells and Xenograft Tumors." Molecules 25, no. 23 (December 7, 2020): 5778. http://dx.doi.org/10.3390/molecules25235778.

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Inhibition of the glycolytic pathway is a critical strategy in anticancer therapy because of the role of aerobic glycolysis in cancer cells. The glycolytic inhibitor 2-Deoxy-d-glucose (2-DG) has shown potential in combination with other anticancer agents. Buforin IIb is an effective antimicrobial peptide (AMP) with broad-spectrum anticancer activity and selectivity. The efficacy of combination treatment with 2-DG and buforin IIb in prostate cancer remains unknown. Here, we tested the efficacy of buforin IIb as a mitochondria-targeting AMP in the androgen-independent human prostate cancer cell line DU145. Combining 2-DG with buforin IIb had a synergistic toxic effect on DU145 cells and mouse xenograft tumors. Combination treatment with 2-DG and buforin IIb caused stronger proliferation inhibition, greater G1 cell cycle arrest, and higher apoptosis than either treatment alone. Combination treatment dramatically decreased L-lactate production and intracellular ATP levels, indicating severe inhibition of glycolysis and ATP production. Flow cytometry and confocal laser scanning microscopy results indicate that 2-DG may increase buforin IIb uptake by DU145 cells, thereby increasing the mitochondria-targeting capacity of buforin IIb. This may partly explain the effect of combination treatment on enhancing buforin IIb-induced apoptosis. Consistently, 2-DG increased mitochondrial dysfunction and upregulated Bax/Bcl-2, promoting cytochrome c release to initiate procaspase 3 cleavage induced by buforin IIb. These results suggest that 2-DG sensitizes prostate cancer DU145 cells to buforin IIb. Moreover, combination treatment caused minimal hemolysis and cytotoxicity to normal WPMY-1 cells. Collectively, the current study demonstrates that dual targeting of glycolysis and mitochondria by 2-DG and buforin IIb may be an effective anticancer strategy for the treatment of some advanced prostate cancer.
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Melzer, Catharina, Juliane von der Ohe, and Ralf Hass. "Involvement of Actin Cytoskeletal Components in Breast Cancer Cell Fusion with Human Mesenchymal Stroma/Stem-Like Cells." International Journal of Molecular Sciences 20, no. 4 (February 18, 2019): 876. http://dx.doi.org/10.3390/ijms20040876.

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Cell fusion as a rare event was observed following the co-culture of human MDA-MB-231cherry breast cancer cells or benign neoplastic MCF10Acherry breast epithelial cells together with different mesenchymal stroma/stem-like cells (MSCGFP) cultures, respectively, resulting in the generation of double-fluorescing hybrid cells. Analysis of potential molecular mechanisms for the formation of cancer hybrid cells revealed cytoskeletal components, including F-actin. Thus, a sub-lethal concentration of cytochalasin D, which blocks elongation of actin filaments, was able to significantly reduce cancer hybrid cell formation. Simultaneously, cell cycle progression of the different co-cultures remained unaffected following treatment with cytochalasin D, indicating continued proliferation. Moreover, exposure to 50 nM cytochalasin D revealed little if any effect on the expression of various integrins and cell adhesion molecules in the different co-cultures. However, LC-MS proteome analysis of the different control co-cultures compared to corresponding cytochalasin-treated co-cultures demonstrated predominant differences in the expression of actin-associated cytoskeletal proteins. In addition, the requirement of structured actin to provide an appropriate cytoskeletal network for enabling subsequent fusion processes was also substantiated by the actin filament disrupting latrunculin B, which inhibits the fusion process between the breast cancer populations and mesenchymal stroma/stem-like cells (MSC). Together, these findings suggest an important role of distinct actin structures and associated cytoskeletal components during cell fusion and the formation of breast cancer hybrid cells.
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4

Tanaudommongkon, Irin, Asama Tanaudommongkon, Priyanka Prathipati, Joey Trieu Nguyen, Evan T. Keller, and Xiaowei Dong. "Curcumin Nanoparticles and Their Cytotoxicity in Docetaxel-Resistant Castration-Resistant Prostate Cancer Cells." Biomedicines 8, no. 8 (July 30, 2020): 253. http://dx.doi.org/10.3390/biomedicines8080253.

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Most prostate cancer patients develop resistance to anti-androgen therapy. This is referred to as castration-resistant prostate cancer (CRPC). Docetaxel (DTX) is the mainstay treatment against CRPC. However, over time patients eventually develop DTX resistance, which is the cause of the cancer-related mortality. Curcumin (CUR) as a natural compound has been shown to have very broad pharmacological activities, e.g., anti-inflammatory and antioxidant properties. However, CUR is very hydrophobic. The objective of this study was to develop CUR nanoparticles (NPs) and evaluate their cytotoxicity in DTX-resistant CRPC cells for the treatment of DTX-resistant CRPC. We tested solubility of CUR in different lipids and surfactants. Finally, Miglyol 812 and D-alpha-tocopheryl poly (ethylene glycol) succinate 1000 (TPGS) were chosen to prepare lipid-based NPs for CUR. We fully characterized CUR NPs that had particle size < 150 nm, high drug loading (7.5%), and entrapment efficiency (90%). Moreover, the CUR NPs were successfully lyophilized without using cryoprotectants. We tested the cytotoxicity of blank NPs, free CUR, and CUR NPs in sensitive DU145 and PC3 cells as well as their matching docetaxel-resistant cells. Cytotoxicity studies showed that blank NPs were very safe for all tested prostate cancer cell lines. Free CUR overcame the resistance in PC3 cells, but not in DU145 cells. In contrast, CUR NPs significantly increased CUR potency in all tested cell lines. Importantly, CUR NPs completely restored CUR potency in both resistant DU145 and PC3 cells. These results demonstrate that the CUR NPs have potential to overcome DTX resistance in CRPC.
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Morrison, T. G., and L. J. McGmnes. "Cytochalasin D accelerates the release of Newcastle disease virus from infected cells." Virus Research 4, no. 1 (December 1985): 93–106. http://dx.doi.org/10.1016/0168-1702(85)90023-1.

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Park, Jee-Young, Jong-Wook Park, Seong-Il Suh, and Won-Ki Baek. "d-Glucosamine down-regulates HIF-1α through inhibition of protein translation in DU145 prostate cancer cells." Biochemical and Biophysical Research Communications 382, no. 1 (April 2009): 96–101. http://dx.doi.org/10.1016/j.bbrc.2009.02.129.

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7

Marchiani, Sara, Lorella Bonaccorsi, Pietro Ferruzzi, Clara Crescioli, Monica Muratori, Luciano Adorini, Gianni Forti, Mario Maggi, and Elisabetta Baldi. "The vitamin D analogue BXL-628 inhibits growth factor-stimulated proliferation and invasion of DU145 prostate cancer cells." Journal of Cancer Research and Clinical Oncology 132, no. 6 (February 17, 2006): 408–16. http://dx.doi.org/10.1007/s00432-006-0086-8.

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8

Gallegos-Martínez, Salvador, Itzel Montserrat Lara-Mayorga, Mohamadmahdi Samandari, Christian Mendoza-Buenrostro, Brenda Giselle Flores-Garza, Luisa María Reyes-Cortés, Juan Carlos Segoviano-Ramírez, Yu Shrike Zhang, Grissel Trujillo-de Santiago, and Mario Moisés Álvarez. "Culture of cancer spheroids and evaluation of anti-cancer drugs in 3D-printed miniaturized continuous stirred tank reactors (mCSTRs)." Biofabrication 14, no. 3 (April 21, 2022): 035007. http://dx.doi.org/10.1088/1758-5090/ac61a4.

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Abstract Cancer continues to be a leading cause of mortality in modern societies; therefore, improved and more reliable in vitro cancer models are needed to expedite fundamental research and anti-cancer drug development. Here, we describe the use of a miniaturized continuous stirred tank reactor (mCSTR) to first fabricate and mature cancer spheroids (i.e. derived from MCF7 cells, DU145 cells, and a mix of MCF7 cells and fibroblasts), and then to conduct anti-cancer drug assays under continuous perfusion. This 3 ml mCSTR features an off-center agitation system that enables homogeneous chaotic laminar mixing at low speeds to support cell aggregation. We incubated cell suspensions for 3 d in ultra-low-attachment plates to allow formation of discoid cell aggregates (∼600 µm in diameter). These cell aggregates were then transferred into mCSTRs and continuously fed with culture medium. We characterized the spheroid morphology and the expression of relevant tumor biomarkers at different maturation times for up to 4 weeks. The spheroids progressively increased in size during the first 5–6 d of culture to reach a steady diameter between 600 and 800 µm. In proof-of-principle experiments, we demonstrated the use of this mCSTR in anti-cancer drug testing. Three drugs commonly used in breast cancer treatment (doxorubicin, docetaxel, and paclitaxel) were probed at different concentrations in MCF7-derived spheroids. In these experiments, we evaluated cell viability, glucose consumption, spheroid morphology, lactate dehydrogenase activity, and the expression of genes associated with drug resistance (ABCB1 and ABCC1) and anti-apoptosis (Bcl2). We envision the use of this agitated system as a tumor-on-a-chip platform to expedite efficacy and safety testing of novel anti-cancer drugs and possibly in personalized medicine applications.
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Diaz Cruz, Maria Araceli, Sandra Karlsson, Ferenc Szekeres, Maria Faresjö, Dan Lund, and Dennis Larsson. "Differential expression of protein disulfide-isomerase A3 isoforms, PDIA3 and PDIA3N, in human prostate cancer cell lines representing different stages of prostate cancer." Molecular Biology Reports 48, no. 3 (March 2021): 2429–36. http://dx.doi.org/10.1007/s11033-021-06277-1.

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AbstractProstate cancer (PCa) is a highly heterogeneous and unpredictable progressive disease. Sensitivity of PCa cells to androgens play a central role in tumor aggressiveness but biomarkers with high sensitivity and specificity that follow the progression of the disease has not yet been verified. The vitamin D endocrine system and its receptors, the Vitamin D Receptor (VDR) and the Protein Disulfide-Isomerase A3 (PDIA3), are related to anti-tumoral effects as well as carcinogenesis and have therefore been suggested as potential candidates for the prevention and therapy of several cancer forms, including PCa. In this study, we evaluated the mRNA expression of VDR and PDIA3 involved in vitamin D signaling in cell lines representing different stages of PCa (PNT2, P4E6, LNCaP, DU145 and PC3). This study further aimed to evaluate vitamin D receptors and their isoforms as potential markers for clinical diagnosis of PCa. A novel transcript isoform of PDIA3 (PDIA3N) was identified and found to be expressed in all PCa cell lines analyzed. Androgen-independent cell lines showed a higher mRNA expression ratio between PDIA3N/PDIA3 contrary to androgen-dependent cell lines that showed a lower mRNA expression ratio between PDIA3N/PDIA3. The structure of PDIA3N differed from PDIA3. PDIA3N was found to be a N-truncated isoform of PDIA3 and differences in protein structure suggests an altered protein function i.e. cell location, thioredoxin activity and affinity for 1,25(OH)2D3. Collectively, PDIA3 transcript isoforms, the ratio between PDIA3N/PDIA3 and especially PDIA3N, are proposed as candidate markers for future studies with different stages of PCa progression.
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Karr, Joan F., Robert P. Apkarian, and John A. Petros. "Cationic Peptide Mediated Oligonucleotide Delivery to DU145 Prostate Cancer Cells - Cell Surface Binding Detected by High Resolution SEM." Microscopy and Microanalysis 5, S2 (August 1999): 392–93. http://dx.doi.org/10.1017/s1431927600015282.

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Transfection of mammalian cells can be enhanced by forming complexes between exogenous DNA and cationic peptides which facilitate DNA transport through cell membranes. Although complexes of plasmid DNA and cationic peptides have been characterized by microscopy, little is known about the complexes formed between oligonucleotides (ODN) and cationic peptides or how the ultrastructure of these complexes affects the intracellular delivery via the cell membrane. Because ODN have potential as therapeutic reagents in the treatment of many diseases, there is a need to develop improved methods for effective delivery of these molecules. By analyzing molecular interactions between cationic peptides and ODN and their effects on cell membranes, cell viability, and DNA delivery, improved delivery compounds can be designed. In this paper, we compare the interactions of a 28 base ODN with three cationic peptides: a novel compound, MNLEK (H-Met-(Nle-Lys4)7-Nle-NH2), an established transfection reagent, poly(L-lysine) (∼ 54 kDa), and a recently described cationic peptide which delivers both plasmid DNA and antisense ODN to cells, KALA (WEAKLAKALAKALAKHLAKALAKALKACEA).For high resolution scanning electron microscopy (HRSEM), DU145 human prostate cancer cells were grown overnight on poly-(D-lysine) coated, UV irradiated silicon chips.
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Dissertations / Theses on the topic "Cancer, Cancer cells, DU145, Cytochalasin D"

1

D, Nolfi. "Studio morfologico e funzionale dell’apparato di Golgi in relazione ad una struttura LTL-positiva nelle cellule di carcinoma prostatico DU145." Doctoral thesis, Università di Siena, 2020. http://hdl.handle.net/11365/1095701.

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The Golgi apparatus is a complex structure present in all eukaryotic cells. This organelle, which was first observed in 1989, still represents a fascinating enigma for much of its structural and functional peculiarity. Generally, the Golgi apparatus is known as the heart of the secretory pathway and glycosylation, which is one of the major post-traductional modifications. Most of the reactions of the glycosylation pathway occur in the Golgi apparatus, where glycosyltransferases and glycosidases modify glucidic chains by adding or removing monosaccharides. All the steps follow a precise sequential order from the cis-Golgi to the trans-Golgi network, depending on the exclusive presence of peculiar enzymes in each Golgi compartment. The sequential order of all these reactions is guaranteed by the morphological stability of the Golgi apparatus, which appears as many staked cisternae fused together forming a unique ribbon structure in vertebrates’ cells. The integrity of the Golgi ribbon is the result of a perfect harmonization between Golgi matrix proteins and the cytoskeleton. Defect in glycosylation has been observed in many pathologies, such as in neurodegenerative disease and malignant transformation of cancer cells. Particularly, the Golgi apparatus of cancer cells loses its typical ribbon shape and splits in smaller vesicles scattered in the cytosol. This thesis focuses on the defects of glycosylation in cancer cells, with a particular regard to fucosylation, since we observed a novel Golgi-derived α 1,2 fucosylated tubular structure exclusive of high proliferative cells. This structure, which was highlighted thanks to the α 1,2 fucose binding Lotus tetragonolobus lectin (LTL), seems to be responsible for a peculiar uptake system that lets many molecules, including LTL itself, enter the cell. To better understand 1) the relation between the morphological scattering of the cisternae and the functionality of the Golgi apparatus and 2) the link between the Golgi disarrangement and the origin of the LTL-positive tubular system, we analysed cells from the human prostatic tumor cell line DU145 by confocal microscopy using the lectins LTL and AAA (Aleuria aurantia Agglutinin), both specific for fucose, and different antibodies able to mark the organelle. Microscopic observations were parallelly performed with SDS-PAGE on DU145 extracts to analyze the localization of the Golgi proteins and glycans in the nuclear, cytoplasmic, membrane, and cytoskeleton fractions obtained using the Qproteome Cell Compartment Kit. Furthermore, in order to evaluate the relationship between the Golgi apparatus/tubular system and the actin cytoskeleton, DU145 were left to grow in presence of Cytochalasin D, a fungal toxin capable to depolymerize the microfilaments. Finally, we performed an uptake experiment to test the functionality of the tubular system, both in the presence and absence of cytochalasin.
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