{"title":"-巯基增加溶组织内阿米巴的丝状肌动蛋白","authors":"Mayra Herrera-Martínez , Verónica Ivonne Hernández-Ramírez , Sarita Montaño , Bibiana Chávez-Munguía , Beatriz Hernández-Carlos , Patricia Talamás-Rohana","doi":"10.1016/j.molbiopara.2022.111512","DOIUrl":null,"url":null,"abstract":"<div><p>This study aimed to know if alpha terthienyl (α-T) affects <span><em>E. histolytica</em></span><span> viability and to analyze its effect on the actin cytoskeleton. Trophozoites of </span><em>E. histolytica</em><span> HM1-IMSS were treated with α-T, then, cell viability<span><span> and morphology were evaluated using tetrazolium salts and scanning electron microscopy, respectively; while actin filaments (F-actin) were stained with rhodamine-phalloidin, observed by </span>confocal microscopy and quantified by fluorometry. Data showed that α-T inhibited cell viability of trophozoites (IC</span></span><sub>50</sub><span><span>, 19.43 µg / mL), affected the cell morphology, and increased the F-actin in a dose-dependent manner. Production of reactive oxygen species and RhoA-GTP levels remained normal in α-T-treated amebas. Two inhibitors that affect the organization of the trophozoites cytoskeleton, one that interacts directly with actin, Cytochalasin D (CD), and one that affects the Rho </span>signaling pathway by inhibiting the downstream effector Rock, Y27632, were tested. Y27632 did not affect the increase of polymerized actin observed with α-T, this compound partially ameliorates the potent disrupting effects of CD on actin filaments. Docking results suggest that α-T could be an antagonist of CD for the same interaction zone in actin, however, more studies are needed to define the action mechanism of this compound.</span></p></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":null,"pages":null},"PeriodicalIF":1.4000,"publicationDate":"2022-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Alpha-terthienyl increases filamentous actin of Entamoeba histolytica\",\"authors\":\"Mayra Herrera-Martínez , Verónica Ivonne Hernández-Ramírez , Sarita Montaño , Bibiana Chávez-Munguía , Beatriz Hernández-Carlos , Patricia Talamás-Rohana\",\"doi\":\"10.1016/j.molbiopara.2022.111512\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>This study aimed to know if alpha terthienyl (α-T) affects <span><em>E. histolytica</em></span><span> viability and to analyze its effect on the actin cytoskeleton. Trophozoites of </span><em>E. histolytica</em><span> HM1-IMSS were treated with α-T, then, cell viability<span><span> and morphology were evaluated using tetrazolium salts and scanning electron microscopy, respectively; while actin filaments (F-actin) were stained with rhodamine-phalloidin, observed by </span>confocal microscopy and quantified by fluorometry. Data showed that α-T inhibited cell viability of trophozoites (IC</span></span><sub>50</sub><span><span>, 19.43 µg / mL), affected the cell morphology, and increased the F-actin in a dose-dependent manner. Production of reactive oxygen species and RhoA-GTP levels remained normal in α-T-treated amebas. Two inhibitors that affect the organization of the trophozoites cytoskeleton, one that interacts directly with actin, Cytochalasin D (CD), and one that affects the Rho </span>signaling pathway by inhibiting the downstream effector Rock, Y27632, were tested. Y27632 did not affect the increase of polymerized actin observed with α-T, this compound partially ameliorates the potent disrupting effects of CD on actin filaments. Docking results suggest that α-T could be an antagonist of CD for the same interaction zone in actin, however, more studies are needed to define the action mechanism of this compound.</span></p></div>\",\"PeriodicalId\":18721,\"journal\":{\"name\":\"Molecular and biochemical parasitology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.4000,\"publicationDate\":\"2022-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular and biochemical parasitology\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0166685122000664\",\"RegionNum\":4,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular and biochemical parasitology","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0166685122000664","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Alpha-terthienyl increases filamentous actin of Entamoeba histolytica
This study aimed to know if alpha terthienyl (α-T) affects E. histolytica viability and to analyze its effect on the actin cytoskeleton. Trophozoites of E. histolytica HM1-IMSS were treated with α-T, then, cell viability and morphology were evaluated using tetrazolium salts and scanning electron microscopy, respectively; while actin filaments (F-actin) were stained with rhodamine-phalloidin, observed by confocal microscopy and quantified by fluorometry. Data showed that α-T inhibited cell viability of trophozoites (IC50, 19.43 µg / mL), affected the cell morphology, and increased the F-actin in a dose-dependent manner. Production of reactive oxygen species and RhoA-GTP levels remained normal in α-T-treated amebas. Two inhibitors that affect the organization of the trophozoites cytoskeleton, one that interacts directly with actin, Cytochalasin D (CD), and one that affects the Rho signaling pathway by inhibiting the downstream effector Rock, Y27632, were tested. Y27632 did not affect the increase of polymerized actin observed with α-T, this compound partially ameliorates the potent disrupting effects of CD on actin filaments. Docking results suggest that α-T could be an antagonist of CD for the same interaction zone in actin, however, more studies are needed to define the action mechanism of this compound.
期刊介绍:
The journal provides a medium for rapid publication of investigations of the molecular biology and biochemistry of parasitic protozoa and helminths and their interactions with both the definitive and intermediate host. The main subject areas covered are:
• the structure, biosynthesis, degradation, properties and function of DNA, RNA, proteins, lipids, carbohydrates and small molecular-weight substances
• intermediary metabolism and bioenergetics
• drug target characterization and the mode of action of antiparasitic drugs
• molecular and biochemical aspects of membrane structure and function
• host-parasite relationships that focus on the parasite, particularly as related to specific parasite molecules.
• analysis of genes and genome structure, function and expression
• analysis of variation in parasite populations relevant to genetic exchange, pathogenesis, drug and vaccine target characterization, and drug resistance.
• parasite protein trafficking, organelle biogenesis, and cellular structure especially with reference to the roles of specific molecules
• parasite programmed cell death, development, and cell division at the molecular level.