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Terpenoids: The Biological Key Molecules
Published in Dijendra Nath Roy, Terpenoids Against Human Diseases, 2019
Moumita Majumdar, Dijendra Nath Roy
Prenylation of proteins is one of the principle signalling pathways. The prenylated proteins are attached to the cell membrane and transport a signal to the next receptor through conformational changes. Protein prenylation was first identified in fungi in 1978 (Kamiya et al. 1978), and the first prenylated protein, farnesylated lamin B, was discovered in mammalian cells (Wolda and Glomset 1988; Farnsworth et al. 1989). Protein prenylation is accompanied mainly by farnesylation and by geranylgeranylation, which is an irreversible covalent post-translational modification found in all eukaryotic cells. Three prenyltransferase enzymes catalyse the associated reactions. Attachment of a single farnesyl (C15) or geranylgeranyl (C20) isoprenoid group is catalyzed by farnesyltransferase (FTase) and geranylgeranyltransferase type 1 (GGTase-I), respectively, to a cysteine residue located in a C-terminal consensus sequence commonly known as the CaaX box (Figure 3.1), where ‘C’ is cysteine, ‘a’ generally signifies an aliphatic amino acid and the ‘X’ residue defines which isoprenoid group is attached to the target protein (Bueno et al. 2015). Geranylgeranyltransferase type 2 (GGTase-II or Rab geranylgeranyltransferase) catalyses the addition of two geranylgeranyl groups at two cysteine residues in sequences such as CXC or CCXX close to the C terminus of Rab proteins.
Toxicological and pharmacokinetic properties of sucralose-6-acetate and its parent sucralose: in vitro screening assays
Published in Journal of Toxicology and Environmental Health, Part B, 2023
Susan S. Schiffman, Elizabeth H. Scholl, Terrence S. Furey, H. Troy Nagle
Within the current study, results of the sucralose vs sucralose-6-acetate comparison of gene expression are consistent with the sucralose-6-acetate vs control comparison that indicate sucralose-6-acetate impaired normal cellular functioning. The expression of genes for essential and fundamental cellular functions were lower in sucralose-6-acetate relative to sucralose. The Farnesyl-diphosphate farnesyltransferase (FDFT1) gene that encodes the first specific enzyme in cholesterol biosynthesis was markedly expressed by sucralose relative to sucralose-6-acetate with a fold change of 30.93. Cholesterol is not only essential for stability of cell membranes but also for tight junction formation (Shigetomi et al. 2023). Taken together data obtained from the sucralose vs sucralose-6-acetate comparison along with increased expression of MT1G, SHMT2, ATF3, and CHST3 in the sucralose-6-acetate vs control comparison indicated that exposure of human intestinal epithelium to sucralose-6-acetate disrupts essential cellular processes.
Current developments in chemistry, coordination, structure and biological aspects of 1-(acyl/aroyl)-3- (substituted)thioureas: advances Continue …
Published in Journal of Sulfur Chemistry, 2019
Aamer Saeed, Muhammad Naeem Mustafa, Muhammad Zain-ul-Abideen, Ghulam Shabir, Mauricio F. Erben, Ulrich Flörke
Okpareke employed docking simulation to investigate the anticancer properties of N,N-diethyl-Ń-palmitoylthiourea 41. Ten validated anticancer drug targets have been used for this purpose; androgen receptor (AR), mitotic regulator (MTR), protein farnesyltransferase (FST), signaling protein (SP), RASRAF- mitogen-activated protein kinase (RRMAPK), human protein kinase (HPK), cell cycle regulator (CCR), glycogen synthase kinase (GSK), retinoid X nuclear receptor (RXNR), oncogene protein (OGP). Studies showed that compound exhibited favorable interactions towards selected anticancer drug targets, which is an indication that compound 27 could be further manipulated as potent anticancer agent [115] (Figure 22).