Worldwide, there are plants known as psychoactive plants that naturally contain psychedelic active components. They have a high concentration of neuroprotective substances that can interact with the nervous system to produce psychedelic effects. Despite these plants' hazardous potential, recreational use of them is on the rise because of their psychoactive properties. Early neuroscience studies relied heavily on psychoactive plants and plant natural products (NPs), and both recreational and hazardous NPs have contributed significantly to the understanding of almost all neurotransmitter systems. Worldwide, there are many plants that contain psychoactive properties, and people have been using them for ages. Psychoactive plant compounds may significantly alter how people perceive the world.
1. Adv Exp Med Biol. 2012;737:251-6. doi: 10.1007/978-1-4614-1566-4_37. Prenylated acylphloroglucinol derivatives: isoprenomics-based design, syntheses and antioxidative activities. Tanaka R(1), Uto Y, Ohnaka K, Ohta Y, Yazaki K, Umemoto N, Nakata E, Hori H. Author information: (1)Department of Life System, Institute of Technology and Science, Graduate School, The University of Tokushima, Minamijosanjimacho-2, Tokushima 770-8506, Japan. DOI: 10.1007/978-1-4614-1566-4_37 PMID: 22259110 [Indexed for MEDLINE] 2. J Pharmacol Exp Ther. 2008 Mar;324(3):985-91. doi: 10.1124/jpet.107.129825. Epub 2007 Dec 6. Inhibitor binding in the human renal low- and high-affinity Na+/glucose cotransporters. Pajor AM(1), Randolph KM, Kerner SA, Smith CD. Author information: (1)Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA. ampajor@utmb.edu The kidney contains two Na(+)/glucose cotransporters, called SGLT2 and SGLT1, arranged in series along the length of the proximal tubule. The low-affinity transporter, SGLT2, is responsible for the reabsorption of most of the glucose in the kidney. There is recent interest in SGLT2 as a target for the treatment of type II diabetes using selective inhibitors based on the structure of the phenylglucoside, phlorizin (phloretin-2'-beta-glucoside). In this study, we examined the inhibition of alpha-methyl-d-glucopyranose transport by phlorizin and a new candidate drug, sergliflozin-A [(2-[4-methoxyphenyl]methyl)phenyl beta-d-glucopyranoside], in COS-7 cells expressing hSGLT1 and hSGLT2. Inhibition by phlorizin was competitive, with K(i) values of 0.3 muM in hSGLT1 and 39 nM in hSGLT2. Inhibition by sergliflozin-A was also competitive, with K(i) values of 1 muM in hSGLT1 and 20 nM in hSGLT2. Phloretin [3-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)-1-propanone; the aglucone of phlorizin] was a less potent inhibitor, with IC(50) values of 142 muM in hSGLT1 and 25 muM in hSGLT2. Site-directed mutagenesis of residues believed to be in the phlorizin binding site showed that only Cys610 is involved in inhibitor binding in the human transporters. Mutation of Cys610 in hSGLT1 to lysine resulted in an increased IC(50) for all inhibitors. In contrast, mutagenesis of the analogous Cys615 in hSGLT2 produced the opposite effect, a decrease in IC(50) for phlorizin and sergliflozin-A. The differences in the effects of the mutations between hSGLT1 and hSGLT2 suggest that this cysteine holds key residues in place rather than participating directly in inhibitor binding. DOI: 10.1124/jpet.107.129825 PMID: 18063724 [Indexed for MEDLINE]