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. Microbiol Res. 2022 May;258:126976. doi: 10.1016/j.micres.2022.126976. Epub 2022 Feb 8. Pythium oligandrum in plant protection and growth promotion: Secretion of hydrolytic enzymes, elicitors and tryptamine as auxin precursor. Bělonožníková K(1), Hýsková V(2), Chmelík J(3), Kavan D(4), Čeřovská N(5), Ryšlavá H(6). Author information: (1)Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030, 128 43 Praha 2, Czech Republic. Electronic address: katerina.belonoznikova@natur.cuni.cz. (2)Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030, 128 43 Praha 2, Czech Republic. Electronic address: veronika.hyskova@natur.cuni.cz. (3)Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030, 128 43 Praha 2, Czech Republic. Electronic address: josef.chmelik@natur.cuni.cz. (4)Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030, 128 43 Praha 2, Czech Republic. Electronic address: daniel.kavan@natur.cuni.cz. (5)Institute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 313, 165 00 Praha 6, Czech Republic. Electronic address: cerovska@ueb.cas.cz. (6)Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030, 128 43 Praha 2, Czech Republic. Electronic address: helena.ryslava@natur.cuni.cz. Pythium is a genus of parasitic oomycetes which target plants and both nonvertebrate and vertebrate animals, including fish and mammalian species. However, several Pythium spp., such as P. oligandrum, function as mycoparasites of pathogenic fungi, bacteria, and oomycetes in soil and thus as advantageous biocontrol agents. This review primarily focuses on biochemical processes underlying their positive effects. For example, P. oligandrum degrades host cell wall polysaccharides using chitinases, cellulases, endo-β-1,3-glucanases, and various exoglycosidases. Proteases from various classes also participate in the cell wall hydrolysis. All these processes can modify cell surface structures and help Pythium spp. compete for space and nutrition. Accordingly, enzyme secretion most likely plays a key role in plant root colonisation. Plant-P. oligandrum interactions, nevertheless, do not involve tissue injury but instead activate plant defence mechanisms, thereby strengthening future plant responses to pathogen attacks. Priming induces the phenylpropanoid and terpenoid pathways and thus synthesis of secondary metabolites, including lignin, for cell wall fortification and other metabolic adjustments. Such metabolic changes are mediated by elicitins, cell wall glycoproteins and oligandrins produced by P. oligandrum. As homologous proteins of β-cinnamomin from Phytophthora cinnamomi with similar essential amino acids for sterol binding, oligandrins stand out for their structure, which they share with cell wall glycoproteins, albeit without the Ser-Thr-rich O-glycosylated domain for cell wall attachment. P. oligandrum also provides plant with tryptamine used for auxin synthesis, promoting plant growth. Overall, in addition to discussing plant metabolic and phytohormonal changes after P. oligandrum inoculation, we review data on P. oligandrum applications as researchers increasingly search for effective and environmentally friendly ways to protect crops. In this context, P. oligandrum emerges as a highly suitable biotechnological solution. Copyright © 2022 Elsevier GmbH. All rights reserved. DOI: 10.1016/j.micres.2022.126976 PMID: 35158298 [Indexed for MEDLINE] 2. Am J Transl Res. 2017 Dec 15;9(12):5719-5742. eCollection 2017. Research on ribosome-inactivating proteins from angiospermae to gymnospermae and cryptogamia. Liu WY(1). Author information: (1)Institute of Biochemistry and Cell Biology, The Chinese Academy of Sciences 320 Yue-Yang RoadShanghai 200031, China. Ribosome-inactivating Proteins (RIPs) are a group of cytotoxin proteins that usually contain a RNA N-glycosidase domain, which irreversibly inactivates ribosome, thus inhibiting protein synthesis. During the past 14 years (1990-2004), the studies conducted in our laboratory had been focusing on the structure and enzymatic mechanism of several PIPs. Herein, we briefly described a summary of the studies conducted mainly in our laboratory on RIPs from angiospermae to gymnospermae and cryptogamia as follows. (1) Cinnamomin is a novel type II RIP isolated from mature seeds of camphor tree. Like ricin, it specifically removes the adenine at A4324 in rat liver 28S rRNA. We systematically studied this low-toxic RIP in term of its enzymatic mechanism, the primary and crystal structure and the nucleotide sequence of its gene, the genetic expression, and its physiological role in the seed cell and the toxicity to human cancer cells and insect larvae. The cleavage of supercoiled double-stranded DNA was its intrinsic property of cinnamomin A-chain, its N- and C-terminal regions were found to be required for deadenylation of rRNA and also necessary for deadenylation of supercoiled double-stranded circular DNA. These results strongly excluded the possibility that cleavage of supercoiled DNA was due to nuclease contamination. (2) Trichosanthin, an abortifacient protein, was purified from the Chinese medicinal herb, Tian-hua-fen, obtained from root tubers of Chinese trichosanthes plant. We proved that trichosanthin was a RNA N-glycosidase, inactivating eukaryotic ribosome by hydrolyzing the N-C glycosidic bond of the adenose at site 4324 in rat 28S rRNA, and inhibited protein synthesis in vitro. (3) A unique Biota orientalis RNase (RNase Bo) was extracted from the mature seeds of the cypress cypress tree (Oriental arborvita), which was gymnospermae plant. It cleaved only a specific phosphodiester bond between C4453 and A4454 of 28S RNA in rat ribosomes, producing a small RNA-fragment (S-fragment), thus inhibiting protein synthesis and belonging to RNase-like RIP, similar to α-sarcin, a special RIP. (4) Lamjapin, the first RIP purified from kelp, the marine cryptogamia algal plant, was shown to be the first single-chained RNA N-glycosidase from marine plant to date. It hydrolyzed rat ribosomal 28S RNA to produce meanly a rather smaller RNA, shorter than the diagnostic R-fragment under the restricted condition. The significance of existence of type I RIP in the lower marine algal plant was briefly discussed. PMCID: PMC5752922 PMID: 29312524 3. PLoS One. 2014 Feb 18;9(2):e88422. doi: 10.1371/journal.pone.0088422. eCollection 2014. Eutirucallin, a RIP-2 type lectin from the latex of Euphorbia tirucalli L. presents proinflammatory properties. Santana SS(1), Gennari-Cardoso ML(1), Carvalho FC(2), Roque-Barreira MC(2), Santiago Ada S(1), Alvim FC(1), Pirovani CP(1). Author information: (1)Universidade Estadual de Santa Cruz, Centro de Biotecnologia e Genética, Ilhéus, Bahia, Brasil. (2)Medical School of Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo, Brasil. Lectins are carbohydrate-binding proteins that recognize and modulate physiological activities and have been used as a toll for detection and identification of biomolecules, and therapy of diseases. In this study we have isolated a lectin present in the latex of Euphorbia tirucalli, and named it Eutirucallin. The latex protein extract was subjected to ion exchange chromatography and showed two peaks with haemagglutinating activity. Polypeptides of 32 kDa protein extract strongly interacted with immobilized galactose (α-lactose > D-N-acetylgalactosamine). The Eutirucallin was obtained with a yield of 5.6% using the α-lactose column. The lectin domain has 32 kDa subunits and at least two of which are joined by disulfide bridges. The agglutinating capacity for human erythrocytes A(+), B(+) and O(+) is inhibited by D-galactose. The haemagglutinating activity of Eutirucallin was independent of Ca(2+) and maintained until the temperature of 55°C. Eutirucallin presented biological activities such as neutrophils recruitment and cytokine prodution by macrophages. The analysis of the trypsin-digested Eutirucallin by ms/ms in ESI-Q-TOFF resulted in nine peptides similar to type 2 ribosome-inactivating protein (type-2 RIP). It's partial sequence showed a similarity of 67.4 - 83.1% for the lectin domain of type-2 RIP [Ricin and Abrin (83.1%), Viscumin, Ebulin, Pulchellin, Cinnamomin, Volkensin and type-2 RIP Iris hollandica]. Our data suggest that Eutirucallin is a new member of type 2 ribosome-inactivating protein and presents biotechnological potential. DOI: 10.1371/journal.pone.0088422 PMCID: PMC3928152 PMID: 24558388 [Indexed for MEDLINE] Conflict of interest statement: Competing Interests: The authors have declared that no competing interests exist. 4. Protein Expr Purif. 2013 Aug;90(2):117-23. doi: 10.1016/j.pep.2013.05.010. Epub 2013 Jun 4. Escherichia coli-based expression system for the heterologous expression and purification of the elicitin β-cinnamomin from Phytophthora cinnamomi. Hofzumahaus S(1), Schallmey A. Author information: (1)Institute of Biotechnology, RWTH Aachen University, Aachen, Germany. s.hofzumahaus@biotec.rwth-aachen.de Elicitins are sterol carrier proteins from the Oomycete genera Phytophthora and Phytium and elicit a hypersensitive response in many economically important plants, in some cases causing a systemic acquired resistance. Their recombinant expression in bacteria is complicated by the presence of three disulfide bonds in the elicitin structure. In consequence, elicitins have so far only been produced in soluble form by isolation from native Phytophthora or Phytium strains or by recombinant expression in the yeast Pichia pastoris. Here, for the first time, we report the soluble expression of the elicitin β-cinnamomin from Phytophthora cinnamomi in Escherichia coli by secretion of the protein into the periplasm. β-Cinnamomin yields have been significantly improved after careful selection of the optimum secretion signal sequence. In total, 17.6 mg β-cinnamomin per liter cell culture have been obtained in shake flasks with the secretion signal sequence of the maltose-binding protein MalE from E. coli. Furthermore, by making use of a C-terminal His-tag, β-cinnamomin purification has been significantly simplified with only one step of immobilized metal ion affinity chromatography yielding protein of high purity (>90%). The established protocol has further been successfully applied to the soluble expression of another elicitin. Copyright © 2013 Elsevier Inc. All rights reserved. DOI: 10.1016/j.pep.2013.05.010 PMID: 23747816 [Indexed for MEDLINE] 5. Am J Chin Med. 2011;39(5):867-78. doi: 10.1142/S0192415X11009263. Vasorelaxant effect of Cinnamomi ramulus ethanol extract via rho-kinase signaling pathway. Kang YH(1), Shin HM. Author information: (1)Department of Physiology, College of Oriental Medicine, Dongguk University, Gyeongju 780-714, Republic of Korea. The Rho-kinase (ROCK) signaling pathway is substantially involved in vascular contraction. This study investigated the vasodilatory effects and possible mechanisms of Cinnamomi ramulus ethanol extract (CRE), with the hypothesis that the CRE vasodilatory effect involves RhoA and the ROCK signaling pathway in rat aortic preparations. CRE (0.05-1 mg/ml) dose-dependently relaxed the vascular contraction induced by phenylephrine and calpeptin in an endothelium-independent manner. Measurement of the expression levels of ROCK-related signaling molecules in response to calpeptin revealed that CRE completely inhibited RhoA and ROCK2 protein expressions. Furthermore, CRE dephosphorylated the subsequent downstream targets myosin phosphatase targeting subunit 1 (MYPT-1), protein kinase C potentiated phosphatase inhibitor protein-17 kDa (CPI-17) and myosin light chain 20 kDa (MLC20). We conclude that the vasorelaxation effect of CRE occurs via downregulation of ROCK signal molecules. DOI: 10.1142/S0192415X11009263 PMID: 21905278 [Indexed for MEDLINE]