Baicalin mediated regulation of key signaling pathways in cancer. (February 2021)

• Record Type: Journal Article
• Authors: Singh, Shilpi; Meena, Abha; Luqman, Suaib
• Is Part Of: Pharmacological research. Volume 164(2021)
• Publication Date: 2021-02
• Subjects: ADM adriamycin -- Akt/PKB protein kinase-B -- ALDH1A1 aldehyde dehydrogenase 1 family, member A1 -- AMPK 5′AMP activated protein kinase -- Apaf-1 apoptotic protease activating factor 1 -- AR androgen receptor -- α7nAChR α7 nicotinic acetylcholine receptor -- Atg5 autophagy related 5 -- Atg7 autophagy related 7 -- Atg12 autophagy related 12 -- AFP alpha-fetoprotein -- ALP alkaline phosphatase -- ABCG2 ATP-binding cassette super-family G member 2 -- ATF6 activating transcription factor 6 -- Bax Bcl-2-associated X protein -- Bcl-xL B-cell lymphoma-extra-large -- bFGF basic fibroblast growth factor -- Bcl-2 β cell lymphoma-2 -- Bad Bcl-2-associated death promoter (BAD) protein -- BIM Bcl-2-like protein 11 -- CCL2 MCP-1/chemokine (C-C motif) ligand 2 -- CDKs cyclin dependent kinases -- Cyt-c cytochrome-C -- CD133 prominin-1 -- CD44 non-kinase transmembrane glycoprotein -- CHOP C/EBP homologous protein -- CI combination index -- DKK1 dickkopf-1 -- EGFR epidermal growth factor receptor -- EMT epithelial–mesenchymal transition -- ENO1 enolase 1 -- ERK extracellular-signal-regulated kinase -- 4E-BP1 eukaryotic translation initiation factor 4E-binding protein 1 -- EIF4E eukaryotic translation initiation factor 4E -- FADD fas-associated death domain -- FasL fatty acid synthase ligand -- FOXO1 forkhead box protein O1 -- 5FU 5-fluorouracil -- GADD45b growth arrest and DNA-damage-inducible b -- Glut1 and Glut3 glucose transporters 1 and 3 -- GPI glucose-6-phosphate isomerise -- GSK-3b glycogen synthase kinase 3b -- GST-π glutathione S-transferase pi -- H3K9me3 histone 3 lysine 9 trimethylation -- GRP78 78-kDa glucose-regulated protein -- HK2 hexokinase 2 -- Hes-1 hairy and enhancer of split-1 -- HIF-1α hypoxia-inducible factor-1α -- ICAM-1 intercellular adhesion molecule 1 -- IKKb IkB kinase b -- ID1 inhibitor of DNA binding 1, HLH protein -- JNK C-jun N-terminal kinase -- LC3 microtubule-associated protein 1A/1B-light chain 3 -- LSH lymphocyte-specific helicase -- LSD1 lysine methyltransferases and demethylases 1 -- Msk-1 mitogen- and stress-activated kinase-1 -- MCL-1 myeloid cell leukemia 1 -- MMP-10 matrix metalloproteinase-10 -- MMP-9 matrix metalloproteinase-9 -- MMP-2 matrix metalloproteinase-2 -- MDR multi drug resistance -- mTOR mammalian target of rapamycin -- miRNA microRNA -- NK natural killer cells -- NFκB nuclear factor kappa B -- Notch1 notch homolog 1, translocation-associated -- PBK/TOPK PDZ-binding kinase/T-LAK cell-originated protein kinase -- PARP poly (ADP-ribose) polymerase -- PCNA proliferating cell nuclear antigen -- PLC phospholipase C -- p53 inducible gene 3 -- PI3K phosphatidylinositol-3 kinase -- P38MAPK P38 mitogen-activated protein kinase -- PD-L1 programmed death-ligand 1 -- PFK1 phosphofructokinase 1 -- p-S6 phospho-S6 ribosomal protein -- p70S6K ribosomal protein S6 kinase beta-1 (S6K1) -- PTEN phosphatase and tensin homolog -- PKM2 pyruvate kinase muscle 2 -- QHMF quercetin–dithiodipropionic acid–oligomeric hyaluronic acid–mannose–ferulic acid (Que–S–S–oHA–Man–FA) -- RASSF6 ras association domain family member 6 -- Rb retinoblastoma -- ROS reactive oxygen species -- Raf proto-oncogene c-RAF -- STAT-3 signal transducer and activator of transcription-3 -- SIRT1 NAD-dependent deacetylase sirtuin-1 -- Slug zinc finger protein SNAI2 -- Suv39H1 suppressor of variegation 3-9 homolog 1 -- TPA 12-O-tetradecanoylphorbol-13-acetate -- TGF-β-1 transforming growth factor beta 1 -- TRAIL tumor necrosis factor (TNF)-related apoptosis-inducing ligand -- TOPO-α topoisomerase enzyme α -- TPI1 triosephosphate isomerase 1 -- uPA urokinase-type plasminogen activator -- uPAR urokinase-type plasminogen activator receptor -- VEGF vascular endothelial growth factor -- xIAP X-linked inhibitor of apoptosis protein -- YAP yes-associated protein; Baicalin -- Angiogenesis -- Anticancer -- Antiproliferative -- Apoptosis -- Pharmacokinetics; Pharmacology -- Periodicals; Pharmacology -- Periodicals; Research -- Periodicals; Médicaments -- Recherche -- Périodiques; Pharmacologie -- Périodiques; 615.105
• DOI: 10.1016/j.phrs.2020.105387
• Languages: English
• ISSNs: 1043-6618

Abstract

Graphical abstract: Highlights: Baicalin reduces cell proliferation by affecting apoptotic pathways. Baicalin targets PI3K/Akt/mTOR, NFκB, MAPK/ERK, Wnt/β-catenin signaling. Baicalin arrests cell proliferation by regulating the cyclins and CDKs. Baicalin-loaded nanoformulations reduces cell proliferation and tumor growth. Abstract: Baicalin has been widely investigated against different types of malignancies both at the cellular and molecular levels over the past few years. Due to its remarkable anti-proliferative potential in numerous cancer cell lines, it has created immense interest as a potential chemotherapeutic modality compared to other flavonoids. Thus, this review focuses on the recent accomplishments of baicalin and its limitations in cancer prevention and treatment. Further, combination studies and nanoformulations using baicalin to treat cancer along with the metabolism, bioavailability, toxicity, and pharmacokinetics have been discussed. The present review explains biological source, and anti-proliferative potential of baicalin against cancers including breast, colon, hepatic, leukemia, lung, and skin, as well as the relevant mechanism of action to modulate diverse signaling pathways including apoptosis, cell cycle, invasion, and migration, angiogenesis, and autophagy. The anticancer mechanism of baicalin in orthotropic and xenograft mice models have been deliberated. The combination studies of baicalin in novel therapies as chemotherapeutic adjuvants have also been summarized. The low bioavailability, fast metabolism, and poor solubility, and other significant factors that limit the clinical use of baicalin have been examined as a challenge. The improvement in the pharmacokinetics and pharmacodynamics of baicalin with newer approaches and the gaps are highlighted, which could establish baicalin as an effective and safe compound for cancer treatment as well as help to translate its potential from bench to bedside.