Xanthone from &lt;i&gt;Swertia chirata&lt;/i&gt; Exerts Chemotherapeutic Potential Against Colon Carcinoma

Barua, Atish; Choudhury, Pritha; Nag, Niraj; Nath, Anirban; Kundagrami, Sabyasachi; Pal, Amit; Panda, Chinmay Kumar; Saha, Prosenjit

doi:10.18520/cs/v122/i1/47-55

Cited by 4 publications

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“…In this regard, the anticancer potentials of natural products have been extensively explored for their differential effects as 'cytoprotectors' to normal cells and 'cytotoxics' to cancer cells. Predominantly, natural products exhibit this dual role by targeting several key molecules which in many instances impart resistance to conventional chemotherapy [4][5][6]. Herein, microorganisms supply structurally diverse natural products in abundance, serving the purpose of drug discovery.…”

Section: Introductionmentioning

confidence: 99%

Metallo-protease Peptidase M84 fromBacillus altitudinisinduces ROS dependent apoptosis in ovarian cancer cells by targeting PAR-1

Nag,

Ray,

Tapader

et al. 2023

Preprint

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In pursuit of isolating novel anticancer proteases from environmental microbial isolates, we have purified and identified an extracellular metallo-protease from Bacillus altitudinis named Peptidase M84. This protease selectively triggered apoptosis in human ovarian adenocarcinoma cells (PA-1, SKOV3) and mouse ovarian carcinoma cells (ID8), in addition to exhibiting no significant effect on normal human epithelial ovarian cell (IOSE) and mouse peritoneal macrophage (PEMΦ) cell viabilities. Protease activated receptor-1 (PAR-1); a GPCR which is reported to be overexpressed in ovarian cancer cells was identified as a novel target of Peptidase M84. We observed that Peptidase M84 induced PAR-1 overexpression along with activating its downstream signalling effectors NFκB and MAPK to promote excessive reactive oxygen species (ROS) generation in ovarian cancer cells. This disrupted mitochondrial membrane potential, allowed cytosolic release of mitochondrial cytochrome c, increased the Bax (pro-apoptotic) to Bcl-2 (anti-apoptotic) ratio and promoted DNA damage to evoke apoptotic death of the ovarian cancer cells. Peptidase M84 also reduced nuclear ki-67 expression in these malignant cells to render an anti-proliferative role. In in vivo set-up, weekly intraperitoneal administration of Peptidase M84 (12 ug/kg body-weight) in the ID8 mice model significantly diminished ascitic fluid accumulation through induction of oxidative stress, increasing murine survival rates by 60%. Collectively, our in vitro and in vivo findings suggested that Peptidase M84 triggered PAR-1 mediated oxidative stress to act as an apoptosis inducer in ovarian cancer cells. This established Peptidase M84 as a promising drug candidate for receptor mediated targeted-therapy of ovarian cancer.

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Section: Introductionmentioning

confidence: 99%

Metallo-protease Peptidase M84 fromBacillus altitudinisinduces ROS dependent apoptosis in ovarian cancer cells by targeting PAR-1

Nag,

Ray,

Tapader

et al. 2023

Preprint

Self Cite

View full text Add to dashboard Cite

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Metallo-protease Peptidase M84 from Bacillus altitudinis induces ROS-dependent apoptosis in ovarian cancer cells by targeting PAR-1

Nag,

Ray,

Tapader

et al. 2024

iScience

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Cetuximab-conjugated PLGA nanoparticles as a prospective targeting therapeutics for non-small cell lung cancer

Kumari

Ehsan

Mondal

et al. 2023

Journal of Drug Targeting

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The initial emulsion thus produced was subsequently emulsified with 75 ml of 1.5% aqueous PVA solution using the same apparatus by homogenizing for around 8 min at 16,000 rpm. Subsequently, a bath sonicator was used to sonicate the double emulsion (w/o/w) for 30 min in order to reduce the size of the emulsion droplets. To get rid of any leftover organic solvents, the final double emulsion was then agitated overnight at room temperature using a magnetic stirrer.The evaporation of organic solvents and subsequent solidification of polymers produced the nanoparticles. The nanoparticles were then sorted in two subsequent centrifugation cycles in a cooling centrifuge (Hermle refrigerated centrifuge, Siemensstr, Wehingen, Germany) at 5,000 rpm for 10 min, and then at 16,000 rpm for 45 min. By washing the nanoparticles with doubledistilled water twice and centrifuging at 16,000 rpm, excess PVA that was attached to the surface of the nanoparticles was removed. The ultimate pellet of nanoparticles was produced, redispersed in 2 ml of double-distilled water, frozen in a refrigerator (So-Low, Environmental Equipment, Ohio, USA), and lyophilized in a Freeze dryer (Laboratory Freeze Dryer, Instrumentation India, Kolkata, India) to produce a dried nanoparticles. In order to prepare FITC loaded nanoaprticles, at the time of preparation of primary emulsion, 100 µL of a 0.4% (w/v) ethanolic FITC solution were added to the initial organic phase [11,12]. Preparation of antibody conjugated nanoparticlesThe Cet antibody was tagged onto the nanoparticles surface by implementing EDC/NHS coupling chemistry as mentioned in the previous studies [13,14]. In brief, the carboxyl group of DTX-loaded PLGA nanoparticles will be activated by using 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride (EDC) and N-hydroxysuccinimide (NHS). Subsequently, a weighed quantity of lyophilized nanoparticles (DTX NP) was suspended in PBS (1 mg/1 mL). The prepared solution received 1 µL of antibody (from the primary stock). The resulting solution was

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Xanthone from <i>Swertia chirata</i> Exerts Chemotherapeutic Potential Against Colon Carcinoma

Cited by 4 publications

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Metallo-protease Peptidase M84 fromBacillus altitudinisinduces ROS dependent apoptosis in ovarian cancer cells by targeting PAR-1

Metallo-protease Peptidase M84 fromBacillus altitudinisinduces ROS dependent apoptosis in ovarian cancer cells by targeting PAR-1

Metallo-protease Peptidase M84 from Bacillus altitudinis induces ROS-dependent apoptosis in ovarian cancer cells by targeting PAR-1

Cetuximab-conjugated PLGA nanoparticles as a prospective targeting therapeutics for non-small cell lung cancer

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