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Targeting GRP78 suppresses oncogenic KRAS protein expression and reduces viability of cancer cells bearing various KRAS mutations
Neoplasia. 2022 Nov;33:100837. doi: 10.1016/j.neo.2022.100837. Epub 2022 Sep 24.ABSTRACTKRAS is the most commonly mutated oncogene in human cancers with limited therapeutic options, thus there is a critical need to identify novel targets and inhibiting agents. The 78-kDa glucose-regulated protein GRP78, which is upregulated in KRAS cancers, is an essential chaperone and the master regulator of the unfolded protein response (UPR). Following up on our recent discoveries that GRP78 haploinsufficiency suppresses both KRASG12D-driven pancreatic and lung tumorigenesis, we seek to determine the underlying mechanisms. Here, we rep...
Source: Neoplasia - September 26, 2022 Category: Cancer & Oncology Authors: Dat P Ha Bo Huang Han Wang Daisy Flores Rangel Richard Van Krieken Ze Liu Soma Samanta Nouri Neamati Amy S Lee Source Type: research

Cancers, Vol. 14, Pages 566: Successful Incorporation of Exosome-Capturing Antibody-siRNA Complexes into Multiple Myeloma Cells and Suppression of Targeted mRNA Transcripts
In conclusion, exosome-capturing Ab-conjugated siRNAs with branched Arg linkers can be effectively delivered into MM cells via uptake of exosomes by parental cells. This technology has the potential to lead to a breakthrough in drug delivery systems for hematologic cancers.
Source: Cancers - January 23, 2022 Category: Cancer & Oncology Authors: Emi Soma Asako Yamayoshi Yuki Toda Yuji Mishima Shigekuni Hosogi Eishi Ashihara Tags: Article Source Type: research

Cancers, Vol. 13, Pages 82: STAT3 Stabilizes IKK α Protein through Direct Interaction in Transformed and Cancerous Human Breast Epithelial Cells
In this study, we observed overexpression and co-localization of IKKα and STAT3 in human breast cancer tissues as well as in H-Ras transformed human breast epithelial (H-Ras MCF-10A) and breast cancer (MDA-MB-231) cells. By utilizing small interfering RNA (siRNA) technology, we were able to demonstrate that STAT3 up-regulated IKKα, but not IKKβ or IKKγ, in these cells. This was attributable to direct binding to and subsequent stabilization of IKKα protein by blocking the ubiquitin-proteasome system. Notably, we identified the lysine 44 residue of IKK&...
Source: Cancers - December 30, 2020 Category: Cancer & Oncology Authors: Young-Il Hahn Soma Saeidi Su-Jung Kim Se-Young Park Na-Young Song Jie Zheng Do-Hee Kim Han-Byoel Lee Wonshik Han Dong-Young Noh Hye-Kyung Na Young-Joon Surh Tags: Article Source Type: research