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aims: To investigate anticancer activity of sericin preparation from cocoons of A. proylei. background: In spite of much progress in understanding the biology of cancer disease, advancement in technology for early diagnosis, the expanding array of anticancer drugs and treatment modalities, the global cancer burden is still significant and increasing. It is estimated that the new cases of cancer in the year 2040 will be 29.4 million per year globally. Sericin, an adhesive protein of silk cocoons has been shown to be a potential protein in various biomedical applications including cancer therapeutics. The present study evaluates the anticancer property of sericin from cocoons of Antheraea proylei J (SAP) against human lung cancer (A549) and cervical cancer (HeLa) cell lines. This is the first report of anti-cancer activity of the non-mulberry silkworm A. proylei J. objective: 1. Establish antiproliferative potential of SAP. 2. Identify the molecular mechanism of cell death induced by SAP on two different cell lines. method: SAP was prepared from cocoons of A. proylei J. by the process of degumming method. The amino acid composition of SAP was determined by HPLC. Cytotoxicity activity was assessed by MTT assay and genotoxicity activity was assessed by comet assay. Cleavage of caspase and PARP proteins and phosphorylation of MAPK pathway members were analysed by Western blotting. Cell cycle analysis was done by flow cytometer. result: SAP causes cytotoxicity to A549 and HeLa cell lines with the IC50 values 3.8 and 3.9 µg/µl respectively. SAP induces apoptosis in a dose dependent manner through caspase-3 and p38, MAPK pathways in A549 and HeLa cells. Moreover, in A549 and HeLa cells SAP induces cell cycle arrest at S phase in a dose dependent manner. conclusion: The difference in the molecular mechanisms of apoptosis induced by SAP in A549 and HeLa cell lines may be due to the difference in the genotypes of the cancer cell lines. However, further investigation is warranted. The overall results of the present study envisage the possibility of using SAP as anti-tumorigenic agent. other: This is the first report of sericin preparation from A. proylei to show anticancer activity. Other reports were from domesticated silkworms.

The leaf crude extract of

Leaf crude extract (aqueous) of Oroxylum indicum (L.) Kurz induces genomic DNA fragmentation, comet formation, and inhibition of cell proliferation in prostate cancer cell line, PC3 as assessed by agarose gel electrophoresis, comet assay, and MTT assay respectively. The bioactive compound was purified through bioassay-guided fractionation using preparative HPLC and MTT as-say. The brown and water-soluble compound was characterized using 1H and 13C nuclear magnetic resonance (NMR), fourier transform infrared (FT-IR) and electrospray ionization (ESI) mass spectrometry, and the compound was iden-tified as a glycosylated hydroquinone derivative, 2-[p-(2-Carboxyhydrazino)phenoxy]-6-(hydroxymethyl) tetrahy-dro-2H-pyran-3,4,5-triol (molecular formula, C13H18N2O8; molecular mass = 330). The identified phytocompound has not been reported earlier elsewhere. Therefore, the common name of the novel anticancer phytocompound isolated from oroxylum indicum in this current study is named as oroxyquinone. The half-maximal inhibitory concentration (IC50) of oroxyquinone on PC3 cells was 19.44 µg/ml (95% CI = 17.97 to 21.04). Oroxyquinone induced cell cycle arrest at S phases and inhibition of cell migration on PC3 as assessed by flow cytome-try and wound healing assay respectively. On investigating the molecular mechanism of inducing apoptosis, the results indicated that the oroxyquinone induced apoptosis through the p38 pathway and cell cycle arrest, however, not through caspase-3 and PARP pathways. The present study identifies a novel an-ticancer molecule and provides scientific evidence supporting the therapeutic potency of OI for ethnomedicinal uses.

We have previously reported that ovarian cancer G protein-coupled receptor 1 (OGR1) is a new metastasis suppressor gene. We have also reported for the first time that a new intronless gene for casein kinase 2α (CSNK2A3) is expressed in human cells. The promoter of the well-known casein kinase 2α (CSNK2A1) displays characteristics of housekeeping gene whereas CSNK2A3 has a characteristic of a regulated promoter with two TATA boxes and a CAAT box. In this study, we found that OGR1 up-regulates expression of CSNK2A3 by about 3 folds in A549 cells but not CSNK2A1. OGR1 also up-regulates expression of neutral endopeptidase (NEP). The OGR1 induced inhibition of A549 cell migration is completely abrogated by inhibition of casein kinase 2α activity, whereas partial abrogation (~ 30%) was observed in the presence of NEP inhibition. The results also revealed that OGR1 regulates CSNK2A3 via activation of Rac1/cdc42 and MAPKs pathways. CK2 is ubiquitously expressed and in contrast it is believed to be a constitutively active enzyme and its regulation appears to be independent of known second messengers. There is no previous report on how expression of CK2α in cancer cells is regulated although many studies have report of aberrant expression of the kinase in cancer. In the current study, we are reporting for the first time the regulation of intronless casein kinase 2α gene, CSNK2A3 in cancer cells. Our findings suggest that the aberrantly casein kinase 2α expression found in various cancer cells may the due to CSNK2A3 expression which is potentially regulated by several master regulators of the developmental pathways rather than well-known casein kinase 2α gene, CSNK2A1.