Coix lacryma-jobi var. ma-yuen Stapf sprout extract induces cell cycle arrest and apoptosis in human cervical carcinoma cells

Abstract

BackgroundCervical cancer is the second-leading cause of cancer-related mortality in females. Coix lacryma-jobi L. var. ma-yuen (Rom.Caill.) Stapf ex Hook. f. is the most widely recognized medicinal herb for its remedial effects against inflammation, endocrine system dysfunctions, warts, chapped skin, rheumatism, and neuralgia and is also a nourishing food.MethodsTo investigate the activity of Coix lacryma-jobi sprout extract (CLSE) on cell proliferation in human cervical cancer HeLa cells, we conducted a Cell Counting Kit-8 (CCK-8) assay. Flow-cytometric analysis and western blot analysis were performed to verify the effect of CLSE on the regulation of the cell cycle and apoptosis in HeLa cells.ResultsWe observed that CLSE significantly inhibited cell proliferation. Furthermore, CLSE dose-dependently promoted cell cycle arrest at the sub-G1/ S phase in HeLa cells, as detected by bromodeoxyuridine (BrdU) staining. The cell-cycle-arrest effects of CLSE in HeLa cells were associated with downregulation of cyclin D1 and cyclin-dependent kinases (CDKs) 2, 4, and 6. Moreover, CLSE induced apoptosis, as determined by flow-cytometric analysis and nuclear DNA fragmentation with Annexin V/propidium iodide (PI) and 4′6′-diamidino-2-phenylindole (DAPI) staining. Induction of apoptosis by CLSE was involved in inhibition of the antiapoptotic protein B-cell lymphoma 2 (Bcl-2) and upregulation of the apoptotic proteins p53, cleaved poly (ADP-ribose) polymerase (PARP), cleaved caspase-3, and cleaved caspase-8. Finally, we observed that CLSE inactivated the phosphoinositide 3-kinase (PI3K) and protein kinase B (AKT) pathways.ConclusionsCLSE causes cell cycle arrest and apoptotic cell death through inactivation of the PI3K/AKT pathway in HeLa cells, suggesting it is a viable therapeutic agent for cervical cancer owing to its anticancer effects.

Coicis semen protects against focal cerebral ischemia-reperfusion injury by inhibiting oxidative stress and promoting angiogenesis via the TGFβ/ALK1/Smad1/5 signaling pathway

“…Stroke is a major cause of disability and death worldwide, but the agents currently used to treat stroke are not sufficient to effectively improve the recovery of stroke patients [ 25 , 26 ]. Coicis Semen, a traditional Chinese medicine, exerts antioxidant and anti-inflammatory effects in many diseases, including coronary heart disease [ 27 ], systemic inflammatory disease [ 28 ], and cancer [ 9 , 29 ]. In a previous study, Coicis Semen was shown to have an antioxidant effect, and oxidative stress is closely associated with the prognosis of ischemic stroke [ 28 , 30 ].…”

Enhancement of Anti-Proliferative Activity of the Extracts from Dehulled Adlay by Fermentation with Bacillus subtilis

“…With the increase in the treatment time and concentration of BDA-Nb, the proliferation inhibition level increased. Son et al [ 35 ] also observed that the cell proliferation inhibition in the cells treated with Coix lacryma-jobi sprout extract increased in a concentration- and time-dependent manner. Meanwhile, K562 and A549 cells showed abnormal morphological features, including low growth density, nuclear chromatin concentration, condensation, and margination ( Figure 3 ).…”

B Cell Lymphoma 2: A Potential Therapeutic Target for Cancer Therapy

“…Resistance in lymphoid cells for ABT-199 has been documented [ 189 ]. Some diseases are liable to be as dependent on one Bcl-2 protein as CLL; the majority of tumors will likely require combinations of these drugs to have a significant therapeutic impact; however, these combinations may show unacceptable toxicity [ 190 , 191 , 192 , 193 , 194 , 195 , 196 , 197 , 198 , 199 , 200 , 201 ].…”

“…Bcl-2 is a 26 kDa, 239 amino-acid protein that composes four domains, BH1, BH2, BH3, and BH4 [38,76]. The BH4 domain residues (10-30), BH3 domain residues (93-107), BH1 domain residues (136)(137)(138)(139)(140)(141)(142)(143)(144)(145)(146)(147)(148)(149)(150)(151)(152)(153)(154)(155), and BH2 domain residues (187)(188)(189)(190)(191)(192)(193)(194)(195)(196)(197)(198)(199)(200)(201)(202) [76] (https://www.uniprot.org/uniprot/P10415#structure; accessed on 15 August 2021) (Figure 3A) and the amino acid sequences of the BH1-4 domains of Bcl-2 [76] (Figure 3B) are provided. The structure of a Bcl-2 chimeric protein comprising a truncated loop obtained from Bcl-xL among the Hα1 as well as Hα2 was initially observed through NMR spectroscopy [77].…”