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Journal articles on the topic 'Pancreatic cancer Sp proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Abdelrahim, Maen, Shengxi Liu, and Stephen Safe. "Induction of Endoplasmic Reticulum-induced Stress Genes in Panc-1 Pancreatic Cancer Cells Is Dependent on Sp Proteins." Journal of Biological Chemistry 280, no. 16 (March 8, 2005): 16508–13. http://dx.doi.org/10.1074/jbc.c500030200.

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Endoplasmic reticulum (ER) stress plays a critical role in multiple diseases, and pharmacologically active drugs can induce cell death through ER stress pathways. Stress-induced genes are activated through assembly of transcription factors on ER stress response elements (ERSEs) in target gene promoters. Gel mobility shift and chromatin immunoprecipitation assays have confirmed interactions of NF-Y and YY1 with the distal motifs of the tripartite ERSE from the glucose-related protein 78 (GRP78) gene promoter. The GC-rich nonanucleotide (N9) sequence, which forms the ER stress response binding factor (ERSF) complex binds TFII-I and ATF6; however, we have now shown that in Panc-1 pancreatic cancer cells, this complex also binds Sp1, Sp3, and Sp4 proteins. Sp proteins are constitutively bound to the ERSE; however, activation of GRP78 protein (or reporter gene) by thapsigargin or tunicamycin is inhibited after cotransfection with small inhibitory RNAs for Sp1, Sp3, and Sp4. This study demonstrates that Sp transcription factors are important for stress-induced responses through their binding to ERSEs.

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2

Oberoi, Shilpa, Rajesambhaji Borade, Neal McCollum, Santhi D. Konduri, Jimmie F. Colon, Cheryl H. Baker, and Maen Abdelrahim. "M2025 Inhibiting Pancreatic Cancer Growth and Sensitizing the Tumor to Radiotherapy Through Downregulation of SP Proteins." Gastroenterology 134, no. 4 (April 2008): A—453. http://dx.doi.org/10.1016/s0016-5085(08)62118-6.

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3

Higgins, Kelly J., Maen Abdelrahim, Shengxi Liu, Kyungsil Yoon, and Stephen Safe. "Regulation of vascular endothelial growth factor receptor-2 expression in pancreatic cancer cells by Sp proteins." Biochemical and Biophysical Research Communications 345, no. 1 (June 2006): 292–301. http://dx.doi.org/10.1016/j.bbrc.2006.04.111.

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4

Fernandez-Zapico, M. E., S. Tsuji, and R. Urrutia. "GLOBAL FUNCTIONAL ANALYSIS OF SP/KLF PROTEINS IDENTIFY KLF11 AS NOVEL TUMOR SUPPRESSOR CANDIDATE FOR PANCREATIC CANCER." Pancreas 31, no. 4 (November 2005): 441. http://dx.doi.org/10.1097/01.mpa.0000193667.32396.85.

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5

Abdelrahim, Maen, Roger Smith, Robert Burghardt, and Stephen Safe. "Role of Sp Proteins in Regulation of Vascular Endothelial Growth Factor Expression and Proliferation of Pancreatic Cancer Cells." Cancer Research 64, no. 18 (September 15, 2004): 6740–49. http://dx.doi.org/10.1158/0008-5472.can-04-0713.

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6

Safe, Stephen, Vijayalekshmi Nair, and Keshav Karki. "Metformin-induced anticancer activities: recent insights." Biological Chemistry 399, no. 4 (March 28, 2018): 321–35. http://dx.doi.org/10.1515/hsz-2017-0271.

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AbstractMetformin is a widely used antidiabetic drug, and there is evidence among diabetic patients that metformin is a chemopreventive agent against multiple cancers. There is also evidence in human studies that metformin is a cancer chemotherapeutic agent, and several clinical trials that use metformin alone or in combination with other drugs are ongoing.In vivoandin vitrocancer cell culture studies demonstrate that metformin induces both AMPK-dependent and AMPK-independent genes/pathways that result in inhibition of cancer cell growth and migration and induction of apoptosis. The effects of metformin in cancer cells resemble the patterns observed after treatment with drugs that downregulate specificity protein 1 (Sp1), Sp3 and Sp4 or by knockdown of Sp1, Sp3 and Sp4 by RNA interference. Studies in pancreatic cancer cells clearly demonstrate that metformin decreases expression of Sp1, Sp3, Sp4 and pro-oncogenic Sp-regulated genes, demonstrating that one of the underlying mechanisms of action of metformin as an anticancer agent involves targeting of Sp transcription factors. These observations are consistent with metformin-mediated effects on genes/pathways in many other tumor types.

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7

Hurtado, Myrna, Umesh T. Sankpal, Aboubacar Kaba, Shahela Mahammad, Jaya Chhabra, Deondra T. Brown, Raj K. Gurung, Alvin A. Holder, Jamboor K. Vishwanatha, and Riyaz Basha. "Novel Survivin Inhibitor for Suppressing Pancreatic Cancer Cells Growth via Downregulating Sp1 and Sp3 Transcription Factors." Cellular Physiology and Biochemistry 51, no. 4 (2018): 1894–907. http://dx.doi.org/10.1159/000495715.

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Background/Aims: Targeting survivin, an anti-apoptotic protein and mitotic regulator, is considered as an effective therapeutic option for pancreatic cancer (PaCa). Tolfenamic acid (TA) showed anti-cancer activity in pre-clinical studies. A recent discovery demonstrated a copper(II) complex of TA (Cu-TA) can result in higher activity. In this study, the ability of Cu-TA to inhibit survivin and its transcription factors, Specificity protein (Sp) 1 and 3 in PaCa cell lines and tumor growth in mouse xenograft model were evaluated. Methods: Cell growth inhibition was measured in MIA PaCa-2 and Panc1 cells for 2 days using CellTiter-Glo kit. Sp1, Sp3 and survivin expression (by Western blot and qPCR), apoptotic cells and cell cycle phase distribution (by flow cytometry) were evaluated. A pilot study was performed using athymic nude mice [treated with vehicle/Cu-TA (25 or 50 mg/kg) 3 times/week for 4 weeks. Results: The IC50 value for Cu-TA was about half than TA.Both agents repressed the protein expression of Sp1/Sp3/survivin, Cu-TA was more effective than TA. Especially effect on survivin inhibition was 5.2 (MIA PaCa-2) or 6.4 (Panc1) fold higher and mRNA expression of only survivin was decreased. Apoptotic cells increased with Cu-TA treatment in both cell lines, while Panc1 showed both effect on apoptosis and cell cycle (G2/M) arrest. Cu-TA decreased the tumor growth in mouse xenografts (25 mg/kg: 48%; 50 mg/kg: 68%). Additionally, there was no change observed in mice body weights, indicating no overt toxicity was occurring. Conclusion: These results show that Cu-TA can serve as an effective survivin inhibitor for inhibiting PaCa cell growth.

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8

Zheng, Lanhong, Xiangjie Zhu, Kangli Yang, Meihong Zhu, Ammad Farooqi, Daole Kang, Mi Sun, et al. "PBN11-8, a Cytotoxic Polypeptide Purified from Marine Bacillus, Suppresses Invasion and Migration of Human Hepatocellular Carcinoma Cells by Targeting Focal Adhesion Kinase Pathways." Polymers 10, no. 9 (September 19, 2018): 1043. http://dx.doi.org/10.3390/polym10091043.

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The development of antitumor drugs has attracted cancer researchers and the identification of novel antitumor lead compounds is certainly of great interest. The fermentation broth of Bacillus sp. N11-8, which was isolated from the Antarctic waters, showed cytotoxicity towards different cells. A cytotoxic polypeptide, PBN11-8, was purified from the fermentation broth of Bacillus sp. N11-8 using ultrafiltration, ammonium sulfate precipitation, anion exchange liquid chromatography and high performance liquid chromatography (HPLC). Cloning and sequence analysis showed that PBN11-8 polypeptide (MW: ~19 kDa by the electrospray-ionization (ESI)) displayed high similarity with peptidase M84 from Bacillus pumilus. PBN11-8 possessed moderate cytotoxicity towards several cancer cell lines with IC50 values of 1.56, 1.80, 1.57, and 1.73 µg/mL against human hepatocellular carcinoma cell line BEL-7402, human renal clear cell adenocarcinoma cell line 786-0, human hepatocellular carcinoma cell line HepG2, and human pancreatic cancer cell line Panc-28, respectively. Moreover, the polypeptide displayed weak cytotoxicity towards normal cell line renal tubular epithelial cell line HK2 and human normal liver cell line L02 cells. Wound healing migration and Transwell experiments demonstrate that PBN11-8 could inhibit the migration and invasion of BEL-7402. Further investigation revealed that PBN11-8 suppresses focal adhesion kinase (FAK)-mediated adhesion, migration, and invasion by disturbing FAK/extracellular regulated protein kinases (ERK) signaling and matrix metalloproteinase-2(MMP-2) and matrix metalloproteinase-9 (MMP-9) in BEL-7402 cells. Thus, PBN11-8 represents a potential novel anti-cancer lead compound.

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9

Patel, Asish, Sukhwinder Kaur, Lynette Smith, Chandrakanth Are, and Surinder Batra. "Diagnostic potential of mucins in pancreatic juice for pancreatic cancer." Journal of Clinical Oncology 34, no. 4_suppl (February 1, 2016): 222. http://dx.doi.org/10.1200/jco.2016.34.4_suppl.222.

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222 Background: Pancreatic juice remains an underutilized resource for diagnosing pancreatic cancer. Mucins are high molecular weight glycoproteins differentially upregulated in pancreatic cancer, and we hypothesize that their profile in pancreatic juice may have diagnostic potential. Methods: Pancreatic juice was obtained during endoscopy from non-healthy non-pancreatic control (NHPC, n = 57), chronic pancreatitis (CP, n = 23), and pancreatic cancer (PC, n = 23) patients. Sandwich ELISA was used to detect MUC1, MUC4, MUC5AC, CA125, and CA19-9. Kruskal-Wallis test and Wilcoxon rank sum test for group and pairwise comparison was done with p < 0.05 as significant. Logistic regression with ROC curve modeling of log transformed data was done for each biomarker individually and in combination to determine odds ratio (OR), sensitivity (SN), and specificity (SP) for PC. Results: PC vs NHPC: MUC5AC had the best individual performance for diagnosing PC with an OR = 2.78 (95% CI = 1.51-5.13), AUC = 0.81, and optimal SN/SP of 0.83 and 0.67, respectively. CA125 was increased in PC with an OR = 2.31 (95% CI = 1.4-4.0), AUC = 0.73, and optimal SN/SP of 0.88 and 0.67. CA19-9 was increased in PC with an OR = 1.5 (95% CI = 1.2-1.8), AUC = 0.76, and optimal SN/SP of 0.73 and 0.70. A combination of MUC1, MUC5AC, CA125, and CA19-9 outperformed all individual markers and had the largest AUC (0.89) with optimal SN/SP of 0.84 and 0.79. PC vs CP: MUC1 concentration in PC was significantly less than CP with an OR = 0.21 (95%CI = 0.088-0.49), AUC = 0.82, and optimal SN/SP of 0.87 and 0.78. PC vs NHPC+CP: MUC1 was decreased significantly in PC with an OR = 0.65 (95% CI = 0.44-0.96), AUC = 0.69, and optimal SN/SP of 0.87 and 0.63. CA125 was increased in PC with an OR = 1.64 (95%CI = 1.1-2.4), AUC = 0.66, and optimal SN/SP of 0.67 and 0.64. CA19-9 was increased in PC with an OR = 1.32 (95%CI = 1.1-1.6), AUC = 0.68, and optimal SN/SP of 0.63 and 0.67. A combination of MUC1, MUC5AC, CA125, and CA19-9 had an AUC = 0.86 with optimal SN/SP of 0.87 and 0.77 for PC. Conclusions: MUC1, MUC5AC, CA125, and CA19-9 combination provides a significantly improved diagnostic panel compared to any individual marker in pancreatic juice for detecting malignancy.

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10

Mann, Karen M., Haoqiang Ying, Joseph Juan, Nancy A. Jenkins, and Neal G. Copeland. "KRAS-related proteins in pancreatic cancer." Pharmacology & Therapeutics 168 (December 2016): 29–42. http://dx.doi.org/10.1016/j.pharmthera.2016.09.003.

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11

Cano, Carla E., and Juan L. Iovanna. "Stress Proteins and Pancreatic Cancer Metastasis." Scientific World JOURNAL 10 (2010): 1958–66. http://dx.doi.org/10.1100/tsw.2010.186.

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Tumor metastasis is challenged by its resistance to microenvironmental stress infringed during escape from the primary tumor and the colonization of a foreign secondary tissue. Because of its great metastatic potential and its strong resistance to anticancer drugs, pancreatic cancer is regarded as a paradigm of the adaptation of cancer cells to microenvironmental stress. Thus, to understand how pancreatic cancer cells adapt to the different endogenous and therapy-related stresses is crucial for understanding their etiology and for the development of new efficient anticancer strategies. This review summarizes the multiple functions accomplished by one major factor of pancreatic cancer cell stress response, the stress protein p8.

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12

Brunner, T. B., E. Hill, J. Wilson, T. Maughan, C. Eccles, and W. G. McKenna. "SP-28: Nelfinavir and RT in Pancreatic Cancer." Radiotherapy and Oncology 104 (September 2012): 29. http://dx.doi.org/10.1016/s0167-8140(15)34582-5.

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13

Bohoudi, O. "SP-0681 Online adaptive planning in pancreatic cancer." Radiotherapy and Oncology 133 (April 2019): S357. http://dx.doi.org/10.1016/s0167-8140(19)31101-6.

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14

Brunner, T. "SP-0656 For the motion: resectable pancreatic cancer." Radiotherapy and Oncology 133 (April 2019): S346. http://dx.doi.org/10.1016/s0167-8140(19)31076-x.

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15

Falconi, M. "SP-0657 Against the motion: resectable pancreatic cancer." Radiotherapy and Oncology 133 (April 2019): S346. http://dx.doi.org/10.1016/s0167-8140(19)31077-1.

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16

Jiang, Weihua, Jiujie Cui, Dacheng Xie, and Liwei Wang. "Sp/KLF Family and Tumor Angiogenesis in Pancreatic Cancer." Current Pharmaceutical Design 18, no. 17 (April 1, 2012): 2420–31. http://dx.doi.org/10.2174/13816128112092420.

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17

Cornelissen, B. "SP-0570: Radiopharmaceuticals in pancreatic cancer: imaging and therapy." Radiotherapy and Oncology 123 (May 2017): S304. http://dx.doi.org/10.1016/s0167-8140(17)31010-1.

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18

Van Cutsem, E. "SP-0659 Against the motion: locally advanced pancreatic cancer." Radiotherapy and Oncology 133 (April 2019): S346. http://dx.doi.org/10.1016/s0167-8140(19)31079-5.

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19

Huguet, F. "SP-0658 For the motion: locally advanced pancreatic cancer." Radiotherapy and Oncology 133 (April 2019): S346. http://dx.doi.org/10.1016/s0167-8140(19)31078-3.

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20

Thomas, Hugh. "Targeting chromatin remodelling proteins to treat pancreatic cancer." Nature Reviews Gastroenterology & Hepatology 12, no. 11 (October 6, 2015): 608. http://dx.doi.org/10.1038/nrgastro.2015.171.

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21

Li, W., J. Martinez Useros, M. J. Fernández-Aceñero, N. García Carbonero, and J. García-Foncillas. "PIWI proteins play oncogenic functions in pancreatic cancer." Annals of Oncology 30 (February 2019): i1. http://dx.doi.org/10.1093/annonc/mdz025.

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22

Scarpa, A. "SP 129 International Cancer Genome Consortium: a promising story in pancreatic cancer." European Journal of Cancer 47 (October 2011): S4. http://dx.doi.org/10.1016/s0959-8049(11)72608-9.

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23

Sunami, Yoshiaki, Johanna Häußler, and Jörg Kleeff. "Cellular Heterogeneity of Pancreatic Stellate Cells, Mesenchymal Stem Cells, and Cancer-Associated Fibroblasts in Pancreatic Cancer." Cancers 12, no. 12 (December 15, 2020): 3770. http://dx.doi.org/10.3390/cancers12123770.

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Pancreatic cancer is projected to become the second deadliest cancer by 2030 in the United States, and the overall five-year survival rate stands still at around 9%. The stroma compartment can make up more than 90% of the pancreatic tumor mass, contributing to the hypoxic tumor microenvironment. The dense stroma with extracellular matrix proteins can be a physical and metabolic barrier reducing therapeutic efficacy. Cancer-associated fibroblasts are a source of extracellular matrix proteins. Therefore, targeting these cells, or extracellular matrix proteins, have been considered as therapeutic strategies. However, several studies show that deletion of cancer-associated fibroblasts may have tumor-promoting effects. Cancer-associated fibroblasts are derived from a variety of different cell types, such as pancreatic stellate cells and mesenchymal stem cells, and constitute a diverse cell population consisting of several functionally heterogeneous subtypes. Several subtypes of cancer-associated fibroblasts exhibit a tumor-restraining function. This review article summarizes recent findings regarding origin and functional heterogeneity of tumor-promoting as well as tumor-restraining cancer-associated fibroblasts. A better understanding of cancer-associated fibroblast heterogeneity could provide more specific and personalized therapies for pancreatic cancer patients in the future.

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24

Brunner, T. "SP-0266: Scheduling radiotherapy and drug treatments for pancreatic cancer." Radiotherapy and Oncology 152 (November 2020): S134. http://dx.doi.org/10.1016/s0167-8140(21)00290-5.

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25

Simtniece, Z., I. Strumfa, A. Abolins, A. Vanags, M. Pavars, E. Vasko, and J. Gardovskis. "MC13-0081 Cell cycle regulatory proteins in pancreatic cancer." European Journal of Cancer 49 (November 2013): S34. http://dx.doi.org/10.1016/s0959-8049(13)70186-2.

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26

Felix, Klaus, Frederik Fakelman, Daniel Hartmann, Nathalia A. Giese, Matthias M. Gaida, Martina Schnölzer, Thomas Flad, Markus W. Büchler, and Jens Werner. "Identification of serum proteins involved in pancreatic cancer cachexia." Life Sciences 88, no. 5-6 (January 2011): 218–25. http://dx.doi.org/10.1016/j.lfs.2010.11.011.

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27

Vimalachandran, C. D., C. C. Thompson, J. P. Neoptolemos, and E. Costello. "IDENTIFICATION OF NOVEL PROTEINS IN THE PANCREATIC CANCER MICROENVIRONMENT." Pancreas 29, no. 4 (November 2004): 350. http://dx.doi.org/10.1097/00006676-200411000-00096.

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28

Chen, Ru, David W. Dawson, Sheng Pan, Niki A. Ottenhof, Roeland F. de Wilde, Christopher L. Wolfgang, Damon H. May, et al. "Proteins associated with pancreatic cancer survival in patients with resectable pancreatic ductal adenocarcinoma." Laboratory Investigation 95, no. 1 (October 27, 2014): 43–55. http://dx.doi.org/10.1038/labinvest.2014.128.

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29

Bonacci, Thomas, Julie Roignot, and Philippe Soubeyran. "Protein Ubiquitylation in Pancreatic Cancer." Scientific World JOURNAL 10 (2010): 1462–72. http://dx.doi.org/10.1100/tsw.2010.133.

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Pancreatic cancer is one of the worst, as almost 100% of patients will die within 5 years after diagnosis. The tumors are characterized by an early, invasive, and metastatic phenotype, and extreme resistance to all known anticancer therapies. Therefore, there is an urgent need to develop new investigative strategies in order to identify new molecular targets and, possibly, new drugs to fight this disease efficiently. Whereas it has been known for more than 3 decades now, ubiquitylation is a post-translational modification of protein that only recently emerged as a major regulator of many biological functions, dependent and independent on the proteasome, whose failure is involved in many human diseases, including cancer. Indeed, despite its role in promoting protein degradation through the proteasome, ubiquitylation is now known to regulate diverse cellular processes, such as membrane protein endocytosis and intracellular trafficking, assembly of protein complexes, gene transcription, and activation or inactivation of enzymes. Taking into account that ubiquitylation machinery is a three-step process involving hundreds of proteins, which is countered by numerous ubiquitin hydrolases, and that the function of ubiquitylation relies on the recognition of the ubiquitin signals by hundreds of proteins containing a ubiquitin binding domain (including the proteasome), the number of possible therapeutic targets is exceptionally vast and will need to be explored carefully for each disease. In the case of pancreatic cancer, the study and the identification of specific alteration(s) in protein ubiquitylation may help to explain its severity and may furnish more specific targets for more efficient therapies.

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30

Phillips, Phoebe, Lu Yang, Alain Vonlaufen, Zhihong Xu, Andrew V. Biankin, David Goldstein, Ron Pirola, Jeremy S. Wilson, and Minoti V. Apte. "S1820 Heat Shock Proteins Are Induced During Pancreatic Stellate Cell Activation in Pancreatic Cancer." Gastroenterology 136, no. 5 (May 2009): A—277. http://dx.doi.org/10.1016/s0016-5085(09)61262-2.

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31

Abdelrahim, Maen, Cheryl H. Baker, James L. Abbruzzese, and Stephen Safe. "Tolfenamic Acid and Pancreatic Cancer Growth, Angiogenesis, and Sp Protein Degradation." JNCI: Journal of the National Cancer Institute 98, no. 12 (June 21, 2006): 855–68. http://dx.doi.org/10.1093/jnci/djj232.

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32

Ideno, Noboru, Yasuhisa Mori, Masafumi Nakamura, and Takao Ohtsuka. "Early Detection of Pancreatic Cancer: Role of Biomarkers in Pancreatic Fluid Samples." Diagnostics 10, no. 12 (December 6, 2020): 1056. http://dx.doi.org/10.3390/diagnostics10121056.

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Pancreatic ductal adenocarcinoma (PDAC) is the fourth leading cause of cancer-related deaths worldwide. Most patients with PDAC present with symptomatic, surgically unresectable disease. Therefore, the establishment of strategies for the early detection is urgently needed. Molecular biomarkers might be useful in various phases of a strategy to identify high-risk individuals in the general population and to detect high-risk lesions during intense surveillance programs combined with imaging modalities. However, the low sensitivity and specificity of biomarkers currently available for PDAC, such as carbohydrate 19-9 (CA19-9), contribute to the late diagnosis of this deadly disease. Although almost all classes of biomarker assays have been studied, most of them are used in the context of symptomatic diseases. Compared to other body fluids, pancreatic juice and duodenal fluid are better sources of DNA, RNA, proteins, and exosomes derived from neoplastic cells and have the potential to increase the sensitivity/specificity of these biomarkers. The number of studies using duodenal fluid with or without secretin stimulation for DNA/protein marker tests have been increasing because of the less-invasiveness in comparison to pancreatic juice collection by endoscopic retrograde cholangiopancreatography (ERCP) and endoscopic ultrasound-guided fine needle aspiration (EUS-FNA). Genomic analyses have been very well-studied, and based on PDAC progression model, mutations detected in pancreatic juice/duodenal fluid seem to indicate the presence of microscopic precursors and high-grade dysplasia/invasive cancer. In addition to known proteins overexpressed both in precursors and PDACs, such as CEA and S100P, comprehensive proteomic analysis of pancreatic juice from patients with PDAC identified many proteins which were not previously described. A novel technique to isolate exosomes from pancreatic juice was recently invented and identification of exosomal microRNA’s 21 and 155 could be biomarkers for diagnosis of PDAC. Since many studies have explored biomarkers in fluid samples containing pancreatic juice and reported excellent diagnostic accuracy, we need to discuss how these biomarker assays can be validated and utilized in the strategy of early detection of PDAC.

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33

A. Ucar, Deniz, and Steven N. Hochwald. "FAK and Interacting Proteins as Therapeutic Targets in Pancreatic Cancer." Anti-Cancer Agents in Medicinal Chemistry 10, no. 10 (December 1, 2010): 742–46. http://dx.doi.org/10.2174/187152010794728675.

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34

Drabik, Anna, Anna Bodzon-Kulakowska, Piotr Suder, Jerzy Silberring, Jan Kulig, and Marek Sierzega. "Glycosylation Changes in Serum Proteins Identify Patients with Pancreatic Cancer." Journal of Proteome Research 16, no. 4 (March 20, 2017): 1436–44. http://dx.doi.org/10.1021/acs.jproteome.6b00775.

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35

Walsh, Naomi, Norma O'Donovan, Susan Kennedy, Michael Henry, Paula Meleady, Martin Clynes, and Paul Dowling. "Identification of pancreatic cancer invasion-related proteins by proteomic analysis." Proteome Science 7, no. 1 (2009): 3. http://dx.doi.org/10.1186/1477-5956-7-3.

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36

Won, Hye Sung, Yoon-Ho Ko, Young-Seok Cho, Eun Kyoung Jeon, and Myung Ah Lee. "Prognostic significance of autophagy-related proteins expression in resected pancreatic cancer." Journal of Clinical Oncology 30, no. 15_suppl (May 20, 2012): e14634-e14634. http://dx.doi.org/10.1200/jco.2012.30.15_suppl.e14634.

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e14634 Background: Autophagy is a critical intracellular pathway for removal of aggregated proteins and damaged organelles. The aim of this study was to explore the contribution of autophagy-related proteins on clinical outcomes of patients with resected pancreatic ductal adenocarcinoma (PDAC). Methods: The expression of five autophagy-related proteins in the PDCA tissues of 73 patients was evaluated by immunohistochemistry using a tissue array method. In addition, clinicopathological characteristics and survival were compared with the expression of autophagy-related proteins. Results: Of the 73 patients, autophagy-related proteins expression frequencies were 49.3% (36/73) for ATG5, 63.9% (46/72) for Ambra 1, 47.9% (35/73) for Beclin-1, 83.3% (60/72) for LC3B, and 69.9% (51/73) for Bif-1. The correlation between the expressions of autophagy-related proteins was statistically significant in all protein pairs. Advanced T stage was marginally associated with a higher number of protein changes (p = 0.059). Multivariate analysis revealed that Beclin 1 overexpression or increases in alteration of autophagy-related proteins were independently associated with poor prognosis (hazard ratio 5.365, p=0.001 and hazard ratio 5.270, p=0.022, respectively). Conclusions: The acquisition of autophagy-related proteins is associated with poor clinical outcome in PDCA. The awareness and inhibition of autophagy offer a potential therapeutic target for PDCA.

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37

Hessmann, Elisabeth, Soeren M. Buchholz, Ihsan Ekin Demir, Shiv K. Singh, Thomas M. Gress, Volker Ellenrieder, and Albrecht Neesse. "Microenvironmental Determinants of Pancreatic Cancer." Physiological Reviews 100, no. 4 (October 1, 2020): 1707–51. http://dx.doi.org/10.1152/physrev.00042.2019.

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Pancreatic ductal adenocarcinoma (PDAC) belongs to the most lethal solid tumors in humans. A histological hallmark feature of PDAC is the pronounced tumor microenvironment (TME) that dynamically evolves during tumor progression. The TME consists of different non-neoplastic cells such as cancer-associated fibroblasts, immune cells, endothelial cells, and neurons. Furthermore, abundant extracellular matrix components such as collagen and hyaluronic acid as well as matricellular proteins create a highly dynamic and hypovascular TME with multiple biochemical and physical interactions among the various cellular and acellular components that promote tumor progression and therapeutic resistance. In recent years, intensive research efforts have resulted in a significantly improved understanding of the biology and pathophysiology of the TME in PDAC, and novel stroma-targeted approaches are emerging that may help to improve the devastating prognosis of PDAC patients. However, none of anti-stromal therapies has been approved in patients so far, and there is still a large discrepancy between multiple successful preclinical results and subsequent failure in clinical trials. Furthermore, recent findings suggest that parts of the TME may also possess tumor-restraining properties rendering tailored therapies even more challenging.

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38

Takeda, Yu, Shogo Kobayashi, Masatoshi Kitakaze, Daisaku Yamada, Hirofumi Akita, Ayumu Asai, Masamitsu Konno, et al. "Immuno-Surgical Management of Pancreatic Cancer with Analysis of Cancer Exosomes." Cells 9, no. 7 (July 9, 2020): 1645. http://dx.doi.org/10.3390/cells9071645.

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Exosomes (EXs), a type of extracellular vesicles secreted from various cells and especially cancer cells, mesenchymal cells, macrophages and other cells in the tumor microenvironment (TME), are involved in biologically malignant behaviors of cancers. Recent studies have revealed that EXs contain microRNAs on their inside and express proteins and glycolipids on their outsides, every component of which plays a role in the transmission of genetic and/or epigenetic information in cell-to-cell communications. It is also known that miRNAs are involved in the signal transduction. Thus, EXs may be useful for monitoring the TME of tumor tissues and the invasion and metastasis, processes that are associated with patient survival. Because several solid tumors secrete immune checkpoint proteins, including programmed cell death-ligand 1, the EX-mediated mechanisms are suggested to be potent targets for monitoring patients. Therefore, a companion therapeutic approach against cancer metastasis to distant organs is proposed when surgical removal of the primary tumor is performed. However, EXs and immune checkpoint mechanisms in pancreatic cancer are not fully understood, we provide an update on the recent advances in this field and evidence that EXs will be useful for maximizing patient benefit in precision medicine.

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Schirmer, Markus A., Claudia M. Lüske, Sebastian Roppel, Alexander Schaudinn, Christian Zimmer, Ruben Pflüger, Martin Haubrock, et al. "Relevance of Sp Binding Site Polymorphism inWWOXfor Treatment Outcome in Pancreatic Cancer." Journal of the National Cancer Institute 108, no. 5 (February 8, 2016): djv387. http://dx.doi.org/10.1093/jnci/djv387.

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Abdel Hadi, Nadine, Gabriela Reyes-Castellanos, and Alice Carrier. "Targeting Redox Metabolism in Pancreatic Cancer." International Journal of Molecular Sciences 22, no. 4 (February 3, 2021): 1534. http://dx.doi.org/10.3390/ijms22041534.

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Cell metabolism is reprogrammed in cancer cells to meet their high bioenergetics and biosynthetic demands. This metabolic reprogramming is accompanied by alterations in redox metabolism, characterized by accumulation of reactive oxygen species (ROS). Elevated production of ROS, mostly by mitochondrial respiration, is counteracted by higher production of antioxidant defenses (mainly glutathione and antioxidant enzymes). Cancer cells are adapted to a high concentration of ROS, which contributes to tumorigenesis, metastasis formation, resistance to therapy and relapse. Frequent genetic alterations observed in pancreatic ductal adenocarcinoma (PDAC) affect KRAS and p53 proteins, which have a role in ROS production and control, respectively. These observations led to the proposal of the use of antioxidants to prevent PDAC development and relapse. In this review, we focus on the therapeutic strategies to further increase ROS level to induce PDAC cell death. Combining the promotion of ROS production and inhibition of antioxidant capacity is a promising avenue for pancreatic cancer therapy in the clinic.

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JI, YI-FEI, HUA HUANG, FENG JIANG, RUN-ZHOU NI, and MING-BING XIAO. "S100 family signaling network and related proteins in pancreatic cancer (Review)." International Journal of Molecular Medicine 33, no. 4 (January 24, 2014): 769–76. http://dx.doi.org/10.3892/ijmm.2014.1633.

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Tian, Chenxi, Daniel Öhlund, Steffen Rickelt, Tommy Lidström, Ying Huang, Liangliang Hao, Renee T. Zhao, et al. "Cancer Cell–Derived Matrisome Proteins Promote Metastasis in Pancreatic Ductal Adenocarcinoma." Cancer Research 80, no. 7 (February 6, 2020): 1461–74. http://dx.doi.org/10.1158/0008-5472.can-19-2578.

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Korc, Murray. "Sugar-Coated Proteins Pave the Way to Improving Pancreatic Cancer Diagnosis." Cellular and Molecular Gastroenterology and Hepatology 2, no. 2 (March 2016): 118–19. http://dx.doi.org/10.1016/j.jcmgh.2016.01.001.

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Cui, Lei, Fang Li, Qingchuan Zhao, and Zhili Li. "Screening and Verification of Differentially Expressed Proteins from Pancreatic Cancer Tissue." Chinese Journal of Chemistry 28, no. 6 (July 1, 2010): 884–90. http://dx.doi.org/10.1002/cjoc.201090166.

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Stasiewicz, Mark, Marek Kwaśniewski, and Tomasz M. Karpiński. "Microbial Associations with Pancreatic Cancer: A New Frontier in Biomarkers." Cancers 13, no. 15 (July 27, 2021): 3784. http://dx.doi.org/10.3390/cancers13153784.

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Pancreatic cancer (PC) remains a global health concern with high mortality and is expected to increase as a proportion of overall cancer cases in the coming years. Most patients are diagnosed at a late stage of disease progression, which contributes to the extremely low 5-year survival rates. Presently, screening for PC remains costly and time consuming, precluding the use of widespread testing. Biomarkers have been explored as an option by which to ameliorate this situation. The authors conducted a search of available literature on PubMed to present the current state of understanding as it pertains to the use of microbial biomarkers and their associations with PC. Carriage of certain bacteria in the oral cavity (e.g., Porphyromonas gingivalis, Aggregatibacter actinomycetemcomitans, Streptococcus sp.), gut (e.g., Helicobacter pylori, Synergistetes, Proteobacteria), and pancreas (e.g., Fusobacterium sp., Enterobacteriaceae, Pseudomonadaceae) has been associated with an increased risk of developing PC. Additionally, the fungal genus Malassezia has likewise been associated with PC development. This review further outlines potential oncogenic mechanisms involved in the microbial-associated development of PC.

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Patel, Kajal, Talha Shaikh, Lora S. Wang, John Parker Hoffman, Steven J. Cohen, and Joshua E. Meyer. "The association between sarcopenia and treatment outcomes in patients with pancreatic cancer undergoing chemoradiation." Journal of Clinical Oncology 34, no. 4_suppl (February 1, 2016): 415. http://dx.doi.org/10.1200/jco.2016.34.4_suppl.415.

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415 Background: Sarcopenia (Sp) or severe loss of muscle mass is a prognostic factor in cancer patients. We assessed the association between Sp and outcomes in borderline resectable or locally advanced/unresectable pancreatic cancer patients undergoing chemoradiation (CRT). Methods: We reviewed all patients who underwent CRT at an NCI-designated cancer center between 2007-2012. Patients with available pre-treatment imaging were included in the analysis. Sp was defined as a lumbar skeletal muscle area/height of < 55.4 cm2/m2 for males and < 38.9 cm2/m2for females. Sp was correlated to treatment toxicity, cause specific survival (CSS), and overall survival (OS). Analysis was performed using chi-square test for categorical variables and Mann-Whitney U test for continuous variables. Kaplan-Meier method and Cox regression was used for survival analysis. Results: A total of 86 patients met the inclusion criteria with 32 (37%) patients being sarcopenic. The median age was 70 (range 46-91) with a median follow-up of 14 months (3-68). The majority of patients were male (57%), had T3 disease (47%), or were borderline resectable (63%). Twenty nine (33.7%) patients underwent surgery. Sarcopenic patients were less likely to undergo surgery (p = 0.024) versus non-sarcopenic patients. Otherwise there was no difference in clinical or treatment factors. The 12-month actuarial OS for patients with and without Sp was 47.9% and 70.7%, respectively (p = 0.047). The 12-month actuarial CSS for patients with and without Sp was 48% and 76%, respectively (p = 0.007). On multivariable analysis, after controlling for T-stage, N-stage, resectability, gender, pre-treatment CA 19-9, and surgery, Sp was no longer associated with CSS (HR 0.284 95% CI 0.774-2.398) or OS (HR 1.077 95% CI 0.626-1.853). Surgery remained associated with CSS (HR 0.205 95% CI = 0.102-0.412) and OS (HR 0.187 95% CI 0.096-0.363). T-stage also remained associated with both CSS (HR 0.616 95% CI 0.410-0.925) and OS (HR 0.649 95% CI 0.440-0.957). Conclusions: The presence of Sp decreases the likelihood of undergoing curative surgery for pancreatic cancer. This may be another useful tool to identify poor prognosis patients.

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Schäfer, Claus, Hanna Steffen, Hartmut Printz, and Burkhard Göke. "Effects of synthetic cyclic AMP analogs on amylase exocytosis from rat pancreatic acini." Canadian Journal of Physiology and Pharmacology 72, no. 10 (October 1, 1994): 1138–47. http://dx.doi.org/10.1139/y94-161.

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Diastereomers of adenosine 3′,5′-phosphorothioate activate cAMP-dependent protein kinases (cAMP-PK) in vitro. We found that these compounds are highly selective tools to monitor cAMP-dependent PKA activation and its effect on amylase exocytosis from pancreatic acini. In permeabilized rat acinar cells, (Sp)-cAMPS dose-dependently stimulated amylase secretion, while (Rp)-cAMPS inhibited (Sp)-cAMPS-induced amylase release. In intact rat acini, 8-Br-(Sp)-cAMPS reduced the secretory responses to secretin, vasoactive intestinal polypeptide (VIP), 8-Br-cAMP, and 8-Br-(Sp)-cAMPS, but not to cerulein. Another derivative, dibutyryl-(Rp)-cAMPS, induced a small inhibitory effect against 8-Br-(Sp)-cAMPS and VIP, which was overlapped by an unspecific stimulatory effect on amylase exocytosis induced by the degradation product butyrate. Furthermore, (Sp)-5,6-dichloro-1-β-D-ribofuranosylbenzimidazole-3′,5′-monophosphorothioate ((Sp)-5,6-DCl-cBIMPS), a specific cAMP-PK activator, induced a maximal induction of cAMP-PK activity, but its stimulation of amylase secretion was less than that by secretin. (Sp)-5,6-DCl-cBIMPS regulated the phosphorylation of several proteins, which were also affected by secretin. However, secretin had additional effects. Its action was most likely mediated by a dual effect on the cAMP and the calcium pathway. Our results indicate that the cAMP-dependent pathway is involved in amylase exocytosis from rat pancreatic acini.Key words: secretin, vasoactive intestinal polypeptide, (Rp)-cAMPS, (Sp)-cAMPS, 8-Br-(Rp)-cAMPS, 8-Br-(Sp)-cAMPS, dibutyryl-(Rp)-cAMPS, (Sp)-5,6-DCl-cBIMPS, cAMP-dependent protein kinases, pancreatic acini, amylase secretion.

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Satoh, Juichi, Victor M. Darley-Usmar, Hiromasa Kashimura, Hisayuki Fukutomi, Kouichi Anan, and Toshiaki Ohsuga. "Analysis of pure pancreatic juice proteins by two-dimensional gel electrophoresis in cases of pancreatic cancer." Gastroenterologia Japonica 21, no. 6 (December 1986): 623–29. http://dx.doi.org/10.1007/bf02774491.

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Han, Liang, Jie Jiang, Mengwen Xue, Tao Qin, Ying Xiao, Erxi Wu, Xin Shen, Qingyong Ma, and Jiguang Ma. "Sonic hedgehog signaling pathway promotes pancreatic cancer pain via nerve growth factor." Regional Anesthesia & Pain Medicine 45, no. 2 (December 1, 2019): 137–44. http://dx.doi.org/10.1136/rapm-2019-100991.

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Background Many patients with pancreatic cancer (PC) suffer from abdominal pain and back pain. However, the cause of pain associated with PC is largely unclear. In this study, we tested the potential influence of the sonic hedgehog (sHH) signaling pathway on PC pain. Methods Substance P (SP) and calcitonin gene-related peptide (CGRP) expression was measured in cultured PC cells and dorsal root ganglions (DRG) by real-time PCR, western blotting analysis and ELISA. Small interfering RNA transfection and plasmid constructs were used to regulate the expression of sHH in the AsPc-1 and Panc-1 cell lines. Pain-related behavior was observed in an orthotopic tumor model in nude mice. Results In this study, the results show that sHH increased the expression of SP and CGRP in DRGs in a concentration and time-dependent manner. Additionally, sHH secretion from PC cells could activate the sHH signaling pathway and, in turn, increase the expression of nerve growth factor (NGF), P75, and TrkA in DRGs. Furthermore, the sHH signaling pathway and NGF/NGF receptor contributed to pain sensitivity in a nude mouse model. Conclusion Our results demonstrate that PC pain originates from the sHH signaling pathway, and NGF mediates the pain mechanism via regulating SP and CGRP.

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Wulanawati, Armi, Harry Noviardi, and Muhamad Sholehuddin Malik Ibrohim. "Finding a Potential Bruceine D Inhibitor for Apoptotic Resistance Protein Pancreatic Cancer Based on Molecular Docking." Indonesian Journal of Chemistry 18, no. 3 (August 30, 2018): 566. http://dx.doi.org/10.22146/ijc.25220.

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Pancreatic cancer arises when cells in the pancreas begin to multiply out of control. In pancreatic cancer, over expression of heat proteins (Hsp70, Hsp 90), constitutive activation of NFĸB, and Bcl-2 family are closely linked with resistance to apoptosis. Apoptotic resistance has been attributed to defects in apoptotic signaling pathways. Bruceine D, which found in abundance Brucea javanica, possesses potent anti-pancreatic cancer activity. In vitro result, bruceine D could induce apoptosis of pancreatic cancer cell. The aim of this study was to find the potential effect of bruceine D inhibitor on apoptotic resistance proteins in pancreatic cancer based on molecular docking. Docking showed a binding affinity between bruceine D with proteins involved in apoptosis using AutoDock. The results showed that free binding energy of Hsp70 is -5.19; Hsp90 -7.26; NFĸB1 -5.49; NFĸB2 -6.14; Bcl-W -6.02; Bcl-xL -5.45 kcal/mol. Based on the result, we conclude that bruceine D with Hsp90 protein has potential the best binding affinity than other proteins.

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