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Anti-Cancer Agents from Natural Sources
Published in Rohit Dutt, Anil K. Sharma, Raj K. Keservani, Vandana Garg, Promising Drug Molecules of Natural Origin, 2020
Debasish Bandyopadhyay, Felipe Gonzalez
L-glutaminase is another vital enzyme that is primarily produced by bacillus and pseudomonas sp., while also be found in some fungi (Bind et al., 2017). It is extensively used in food industries, but recent research has determined that L-glutaminase has the potential to be a very powerful anti-cancer enzyme. The amino acid L-glutamine is essential for cellular function, especially for protein biosynthesis. The enzyme works by starving cancer cells through a conversion of L-glutamine to glutamic acid and ammonia. This catalytic reaction induced apoptosis because cancerous cells lack the glutamine biosynthesis enzyme, L-glutamine synthase (Unissa et al., 2015). A study conducted in 1966 by El-Asmar et al. (1966) revealed that normal cells were not affected by L-glutaminase because of the transformation of L-glutamine into glutamic acid. A study (Wise et al., 2010) determined that cancerous cells have an addiction to glutamine, as an important mitochondrial substrate, it takes part in NADPH production. For instance, pancreatic carcinoma MIA PaCa-2 and PANC-1 cells, showed dependence on L-glutamine in a study conducted in 1978 (Wu et al., 1978).
Role of Growth Factors in Neoplastic Processes
Published in Enrique Pimentel, Handbook of Growth Factors, 2017
The proliferation of tumor cells frequently depends on the operation of autocrine mechanisms. Two or more independent autocrine loops may arise in clones derived from a single tumor cell.78 The human pancreatic carcinoma cell line MIA-PaCa 2, for example, expresses both IGF-I and TGF-α and their receptors, which would constitute a double autocrine loop in these cells.79 Coexpression of two or more growth factors and their receptors may occur frequently in malignant tumors,80 but a similar coexpression is observed in various benign tumors.81,82 Higher levels of growth factor expression may be observed in malignant cells as compared with cells from benign tumors, but there are no definite correlations between growth factor overexpression and tumor progression. Moreover, normal cells such as placental cytotrophoblasts, may coexpress growth factors and their receptors.83
Hormonal Effects on Gastrointestinal Cancer Growth
Published in Jean Morisset, Travis E. Solomon, Growth of the Gastrointestinal Tract: Gastrointestinal Hormones and Growth Factors, 2017
Courtney M. Townsend, Singh Pomila, James C. Thompson
EGF mildly increased the number of PANC-I cells after 6 d in cultures in which the serum concentration was 0.1%.106 Pancreatic carcinoma cell lines (ASPC-I, T3M4, PANC-I, COLO 357, and MIA PaCa-2) produce transforming growth factor alpha (TGF-α) and express TGF-α mRNA.108 The amount of TGF-α protein found in the supernatant of these cells did not correlate with the amount of TGF-α mRNA. Differential growth effects of TGF-α and EGF on colony formation of PANC-I cells in soft agar were noted. The role of TGF-α as an autocrine growth factor for pancreatic cancer has not been conclusively demonstrated.
A Marine Carotenoid of Fucoxanthinol Accelerates the Growth of Human Pancreatic Cancer PANC-1 Cells
Published in Nutrition and Cancer, 2022
Masaru Terasaki, Shouta Takahashi, Ryuta Nishimura, Atsuhito Kubota, Hiroyuki Kojima, Tohru Ohta, Junichi Hamada, Yasuhiro Kuramitsu, Hayato Maeda, Kazuo Miyashita, Mami Takahashi, Michihiro Mutoh
All-trans-FxOH (purity, ≥98%) was purified from a brown alga by Dr. Hayato Maeda (Hirosaki University, Japan) (Figure 1A). Dulbecco’s modified Eagle’s medium (DMEM) was obtained from Wako Pure Chemicals (Osaka, Japan). Human pancreatic cancer PANC-1 and colorectal cancer DLD-1 cells were purchased from the American Type Culture Collection (Manassas, VA, USA). Human pancreatic cancer BxPC-3 cells and MIA PaCa-2 were from Dainippon Pharmaceuticals (Osaka, Japan) and Health Science Research Resources Bank (Osaka, Japan), respectively. These cells were maintained in DMEM mixed with 10 v/v% FBS, L-glutamine (final, 4 mM), penicillin (final, 40,000 U/L), and streptomycin (final, 40 mg/l). β-Actin, Akt (pan), cyclin B1, phosphorylated FAK (pFAK (Tyr397)), FYN, integrin α5, integrin β1, NRF2, and phosphorylated Smad2 (pSmad2 (Ser465/467)) antibodies were purchased from GeneTex (Irvine, CA, USA). Cyclin D1, phosphorylated C-Raf (pC-Raf (Ser338)), phosphorylated MEK1/2 (pMEK1/2 (Ser217/221)), phosphorylated ERK1/2 (pERK1/2 (Thr202/Tyr204)), and PPARγ antibodies were obtained from Cell Signaling Technology (Danvers, MA, USA). Cyclin D2 and phosphorylated Akt (pAkt (Ser473)) antibodies were purchased from Bioss Antibodies (Beijing, China) and GenScript (Piscataway, NJ, USA), respectively. Phosphorylated paxillin (pPaxillin (Tyr31)) antibody was from Novex (San Diego, CA, USA). All other reagents were of analytical grade.
Bioactivity and pharmacological properties of α-mangostin from the mangosteen fruit: a review
Published in Expert Opinion on Therapeutic Patents, 2018
Guoqing Chen, Yong Li, Wei Wang, Liping Deng
The researches on the treatment and/or prevention of pancreatic cancer have never stopped. They recently cultured the human pancreatic cancer TMIA PaCa-2 and PANC-1 cells and treated with α-MG or γ-MG at varying concentrations. After 48 or 72 h, they were then subjected to TUNEL assay, Western blotting, and miRNA assay to determine the anticancer effect of α-MG and γ-MG. The results indicated that α-MG and γ-MG could reduce the viability of MIA PaCa-2 and PANC-1, induce apoptosis of MIA PaCa-2 and PANC-1, and induce autophagy in pancreatic cancer. Furthermore, treatment of MIA PaCa-2 or PANC-1 with gemcitabine alone or combined with α-MG or γ-MG at IC50 for 72 h measured the cells viability. They found that α-MG and γ-MG showed synergistic effects for gemcitabine on cell viability of MIA PaCa-2 compared to treatment of gemcitabine alone [26].
Broad reactivity and enhanced potency of recombinant anti-EGFR × anti-CD3 bispecific antibody-armed activated T cells against solid tumours
Published in Annals of Medicine, 2022
Manley T. F. Huang, Vikram Sharma, Andrew Mendelsohn, Qisheng Wei, Jinjing Li, Bo Yu, James W. Larrick, Lawrence G. Lum
Normal donor ATC were armed with rEGFRBi with 1, 10, 25, 50, 100, 200 or 400 ng of rEGFRBi/106 cells and tested against MDA-MB-231, SK-BR-3 and U87 cells in an 18 h 51Cr-release assay at 10:1 E:T. For U87 cells there was no significant difference in cytotoxicity among the different rEGFRBi arming conditions nor between any of the rEGFR-BATs conditions and EGFRBi-BATs armed at 50 ng of EGFRBi/106cells (Figure 2(e)). And, as demonstrated earlier by Zitron et al. [16], HER2-BATs did not kill U87 cells. With SK-BR-3 targets, there was no significant difference among rEGFR-BATs armed at 400 to 10 ng of rEGFRBi, nor any of those rEGFR-BATs conditions and HER2-BATs. However, rEGFR-BATs armed between 10 and 200 ng were significantly higher than EGFR-BATs. For MDA-MB-231, there was no significant difference among rEGFR-BATs between 10 and 100 ng, although all of those were significantly greater than rEGFRBi at 200 and 400 ng. rEGFR-BATs at 25, 50 and 100 ng were significantly higher than at 1 ng, while those at 10, 200 and 400 were not different than 1 ng. However, rEGFRBi-BATs armed from 10 to 400 ng were significantly higher than for EGFR-BATs, while rEGFR-BATS from 1 to 400 were significantly higher than for HER2-BATs (Figure 2(e)). When 2 normal donors were armed over a narrower range of 50, 5 and 0.5 ng and tested against BXPC-3 and MDA-MB-231 cells, rEGFR-BATs maintained the same level of killing across all three concentrations, while EGFR- and HER2-BATs dropped off at 0.5 ng (Figure 2(f)). The same pattern was seen with a normal donor against MIA PaCa-2 cells (pancreatic cancer, data not shown).