Journal: Journal of the American Chemical Society

Article Title: Encapsulation of Gold-Based Anticancer Agents in Protease-Degradable Peptide Nanofilaments Enhances Their Potency

doi: 10.1021/jacs.2c09820

Figure Lengend Snippet: Cell Viability of gold anticancer agents, gold-loaded peptide nanofilaments ( PD+1 , PD+2 , AD+1 , AD+2 ), and peptides ( PD , AD ) in three human cell lines. Caki-1 (renal cancer), MDA-MB-231 (Triple Negative Breast Cancer), and IMR-90 (lung fibroblasts) incubated with drug-loaded peptide for 72 h. A) Compound 1 , B) Compound 2 . (* represents P <0.05, ** represents P <0.01, *** represents P <0.001).

Article Snippet: Human breast adenocarcinoma line MDA-MB-231 and human lung fibroblast line IMR-90 were obtained from the American Type Culture Collection (ATCC; Manassas, Virginia, USA) and cultured with Dulbecco’s modified Eagle’s medium (DMEM; Fisher Scientific) containing 10 % fetal bovine serum, certified, heat inactivated, US origin (FBS; Fisher Scientific), 1 % minimum essential media (MEM) nonessential amino acids (NEAA; Fisher Scientific), and 1 % penicillin–streptomycin (PenStrep; Fisher Scientific).

Techniques: Incubation

Journal: Breast Cancer Research : BCR

Article Title: Honokiol activates AMP-activated protein kinase in breast cancer cells via an LKB1-dependent pathway and inhibits breast carcinogenesis

doi: 10.1186/bcr3128

Figure Lengend Snippet: AMPK knockdown abrogates honokiol-mediated increased phosphorylation of ACC, inhibition of phosphorylation of S6K, and inhibition of migration . (a) Immunoblotting for AMPK protein by using lysates from untreated MEFs derived from AMPK-WT (WT) and AMPK-knockout mice (AMPK-null). The blot was stripped and reprobed with anti-actin antibody. (b) WT and AMPK-null MEFs were treated with honokiol (HNK, 2.5 μ M ) for indicated time intervals. U, untreated cell. Total protein was isolated, and equal amounts of proteins were resolved with SDS-PAGE and subjected to immunoblot analysis by using specific antibodies for phosphorylated ACC (p-ACC). Anti-actin antibody was used as control. (c) WT and AMPK-null MEFs were subjected to scratch-migration assay in the presence (HNK, 2.5 μ M ) or absence (U) of honokiol. The plates were photographed at the identical location of the initial image (0 hours) at 24 hours. The histogram shows the fold change in migration. * P < 0.001, compared with untreated controls. All the experiments were performed thrice in triplicate. (d) WT and AMPK-null MEFs were treated with honokiol (HNK, 2.5 μ M ) for indicated time intervals. U, untreated cell. Total protein was isolated, and equal amounts of proteins were resolved with SDS-PAGE and subjected to immunoblot analysis by using specific antibodies for phosphorylated pS6K (p-pS6K). The membranes were reblotted by using total pS6K and actin antibody as control. (e) WT and AMPK-null MEFs were subjected to XTT assay in the presence (HNK) or absence (U) of honokiol, as indicated. The results shown are representative of three independent experiments performed in triplicate. * P < 0.001, compared with untreated controls.

Article Snippet: AMPK-null and AMPK-WT immortalized MEFs were kindly provided by Dr. Keith R. Laderoute (SRI International, Menlo Park, CA, USA) [ ].

Techniques: Knockdown, Phospho-proteomics, Inhibition, Migration, Western Blot, Derivative Assay, Knock-Out, Isolation, SDS Page, Control, XTT Assay