Topic
Lanosterol
About: Lanosterol is a research topic. Over the lifetime, 1239 publications have been published within this topic receiving 36737 citations. The topic is also known as: (3β)-lanosta-8,24-dien-3-ol & (3β,20R)-lanosta-8,24-dien-3-ol.
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TL;DR: This validated method by ultra performance liquid chromatography-tandem mass spectrometry with the electrospray ionization mode for quantitation of lanosterol in the vitreous humor of rabbits after ocular administration provided useful information on pharmacological action mechanism of Lanosterol and were meaningful for cataract treatment among the elderly population.
5 citations
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TL;DR: Results eliminate an azole-like MOA for the bengazoles, and suggest that another as-yet unidentified mechanism is operative, which is likely to be dose-dependent synergistic antifungal activity.
Abstract: Bengazoles A–G from the marine sponge Jaspis sp. exhibit potent in vitro antifungal activity against Candida spp. and other pathogenic fungi. The mechanism of action (MOA) of bengazole A was explored in Candida albicans under both liquid culture and surface culture on Mueller-Hinton agar. Pronounced dose-dependent synergistic antifungal activity was observed with bengazole A in the presence of bengamide A, which is also a natural product from Jaspis sp. The MOA of bengazole A was further explored by monitoring the sterol composition of C. albicans in the presence of sub-lethal concentrations of bengazole A. The GCMS of solvent extracts prepared from liquid cultures of C. albicans in the presence of clotrimazole―a clinically approved azole antifungal drug that suppresses ergosterol biosynthesis by the inhibition of 14α-demethylase―showed reduced cellular ergosterol content and increased concentrations of lanosterol and 24-methylenedihydrolanosterol (a shunt metabolite of ergosterol biosynthesis). No change in relative sterol composition was observed when C. albicans was cultured with bengazole A. These results eliminate an azole-like MOA for the bengazoles, and suggest that another as-yet unidentified mechanism is operative.
5 citations
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22 Jan 2003
TL;DR: In this article, a method for the production of zymosterol, the biosynthetic intermediate or subsequent products thereof by cultivation of organisms, in particular yeasts, which have an increased lanosterol C14-demethylase activity and an increased HMG-CoA reductase activity, was described.
Abstract: The invention relates to a method for the production of zymosterol the biosynthetic intermediate or subsequent products thereof by cultivation of organisms, in particular yeasts, which have an increased lanosterol C14-demethylase activity and an increased HMG-CoA reductase activity, the nucleic acid constructs necessary for the production of the genetically-modified organisms and the genetically modified organisms, in particular the yeasts themselves.
5 citations
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TL;DR: It is reported that a frequently occurring azole-resistance strategy makes C. albicans less susceptible to azole treatment while, at the same time, affects its cell wall architecture, potentially leading to exposure of the pathogen to a more effective host immune response.
Abstract: The opportunistic pathogen Candida albicans is responsible for life-threating infections in immunocompromised individuals. Azoles and polyenes are two of the most commonly used antifungals and target the ergosterol biosynthesis pathway or ergosterol itself. A limited number of clinically employed antifungals correspond to the development of resistance mechanisms. One resistance mechanism observed in clinical isolates of azole-resistant C. albicans is the introduction of point mutations in the ERG11 gene, which encodes a key enzyme (lanosterol 14-α-demethylase) on the ergosterol biosynthesis pathway. Here, we demonstrate that a point mutation K143R in ERG11 (C. albicans ERG11K143R/K143R) contributes not only to azole resistance, but causes increased gene expression. Overexpression of ERG11 results in increased ergosterol content and a significant reduction in plasma membrane fluidity. Simultaneously, the same point mutation caused cell wall remodeling. This could be facilitated by the unmasking of chitin and β-glucan on the fungal cell surface, which can lead to recognition of the highly immunogenic β-glucan, triggering a stronger immunological reaction. For the first time, we report that a frequently occurring azole-resistance strategy makes C. albicans less susceptible to azole treatment while, at the same time, affects its cell wall architecture, potentially leading to exposure of the pathogen to a more effective host immune response.
5 citations
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TL;DR: The present paper describes the purification, by a method based on that of Yoshida et al. (l977), of the cytochrome P-450 from Saccharomyces cerevisiae which has been used for the binding studies and presents evidence that the fungicide diclobutrazol I (2RS.3RS)1 (2, 4-dichlorophenyl)-4,4-dimethyl2(1 H1,2,4tri
Abstract: Many potent fungicides discovered recently have been shown to inhibit the 14a-demethylation reaction of ergosterol biosynthesis, leading to an accumulation of lanosterol or 24-methylene24,25-dihydrolanosterol (Baldwin, 1983). The reaction is known to be cytochrome P-450-dependent (Alexander et al., 1974) and we have presented evidence that the fungicide diclobutrazol I (2RS.3RS)1 (2,4-dichlorophenyl)-4,4-dimethyl2(1 H1,2,4triazol-l-yl)pentan-3-ol~ (Bent & Skidmore, 1979) binds to cytochrome P-450 giving a Type I1 difference spectrum (Wiggins & Baldwin, 1983). The present paper describes the purification, by a method based on that of Yoshida et al. (l977), of the cytochrome P-450 from Saccharomyces cerevisiae which has been used for the binding studies. Saccharomyces cerevisiae (N.C.Y.C. 739) was grown semianaerobically on 20% (w/v) glucose as described by Wiseman et al. (1975). After 3 days the cells were collected by centrifuga-
5 citations