Aim: To investigate anticancer activity of the DNA binding domain of SMAR1 (His 5) in vitro and in vivo.
Materials & Methods: His 5 was conjugated to hydrothermally synthesized carbon nanospheres (CNs). Anticancer activity of CNs-His 5 was evaluated in vitro and in vivo.
Results: CNs- His 5 significantly reduced cyclin D1 levels in MDA-MB-231 cells. Tumor bearing Balb/c mice injected with CNs-His 5 showed approximately 62% tumor regression and significantly reduced FDG uptake. Caspases assay and IHC staining confirmed tumor growth inhibition, which could be attributed to apoptotic, antiproliferative and antiangiogenic activities of His 5.
Conclusion: DNA binding domain of the SMAR1 protein (His 5) has potent anticancer activity and its CNs mediated delivery could control breast tumor in mice model.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.2217/nnm-2017-0298 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
MA -mediated lncRNA SCIRT stability promotes NSCLC progression through binding to SFPQ and activating the PI3K/Akt pathway.
Cell Mol Life Sci
January 2025
Department of Clinical Laboratory, Harbin Medical University Cancer Hospital, 150 Haping Road, Harbin, 150081, China.
Non-small cell lung cancer (NSCLC) has emerged as one of the most prevalent malignancies worldwide. N6-methyladenosine (mA) methylation, a pervasive epigenetic modification in long noncoding RNAs (lncRNAs), plays a crucial role in NSCLC progression. Here, we report that mA modification and the expression of the lncRNA stem cell inhibitory RNA transcript (SCIRT) was significantly upregulated in NSCLC tissues and cells.
View Article and Find Full Text PDFExploring Biophysical and Chemoinformatics Approaches for Interactions of Ionic Liquids with Hemoglobin, DNA, BSA, and HSA.
Chem Biodivers
January 2025
SRM Institute of Science and Technology - NCR Campus, chemistry, Department of Chemistry, SRM Institute of Science and Technology, Delhi NCR Camp, India, 241405, Modinagar, INDIA.
This review paper provides an inclusive overview of the intricate interactions amid ionic liquids (ILs) and essential biomacromolecules, mainly Hemoglobin (Hb), Bovine Serum Albumin (BSA), Human Serum Albumin (HSA), and Calf Thymus-DNA (CT-DNA). ILs have recently become a topic of great attention because of their inimitable physicochemical properties and potential uses in different fields. The review systematically explores the binding mechanisms, thermodynamics, and structural changes induced by ILs on Hb, BSA, HSA, and CT-DNA using spectroscopic, thermodynamic, and computational techniques.
View Article and Find Full Text PDFEctopic overexpression of DNA-/RNA-binding Alba proteins misregulates virulence gene homeostasis during asexual blood development.
Microbiol Spectr
January 2025
Institute of Bioinformatics and Applied Biotechnology, Bengaluru, Karnataka, India.
Alba domain-containing proteins are ubiquitously found in archaea and eukaryotes. By binding to either DNA, RNA, or DNA:RNA hybrids, these proteins function in genome stabilization, chromatin organization, gene regulation, and/or translational modulation. In the malaria parasite , six Alba domain proteins PfAlba1-6 have been described, of which PfAlba1 has emerged as a "master regulator" of translation during parasite intra-erythrocytic development (IED).
View Article and Find Full Text PDFChIP-mini: a low-input ChIP-exo protocol for elucidating DNA-binding protein dynamics in intracellular pathogens.
Nucleic Acids Res
January 2025
School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea.
Genome-wide identification of binding profiles for DNA-binding proteins from the limited number of intracellular pathogens in infection studies is crucial for understanding virulence and cellular processes but remains challenging, as the current ChIP-exo is designed for high-input bacterial cells (>1010). Here, we developed an optimized ChIP-mini method, a low-input ChIP-exo utilizing a 5,000-fold reduced number of initial bacterial cells and an analysis pipeline, to identify genome-wide binding dynamics of DNA-binding proteins in host-infected pathogens. Applying ChIP-mini to intracellular Salmonella Typhimurium, we identified 642 and 1,837 binding sites of H-NS and RpoD, respectively, elucidating changes in their binding position and binding intensity during infection.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!