Disease relevance of farnesol

• In vivo interaction between the polyprenol phosphate mannose synthase Ppm1 and the integral membrane protein Ppm2 from Mycobacterium smegmatis revealed by a bacterial two-hybrid system [1].
• Rv3265c shows homology to the Escherichia coli gene wbbL, which encodes a dTDP-Rha:alpha-D-GlcNAc-pyrophosphate polyprenol, alpha-3-L-rhamnosyltransferase [2].
• Tunicamycin is a reversible inhibitor of polyprenol-phosphate: N-acetylhexosamine-1-phosphate translocases and is produced by several Streptomyces species [3].
• Prophylactic activity of dihydroheptaprenol, a synthetic polyprenol derivative, against Sendai virus infection in mice [4].
• One of the five polyprenol preparations tested, preparation N1, which had the lowest hydrophilic-lipophilic balance (8.6), produced a significant protective effect when injected in a dose of 2000 microg/mouse 2 days before aerosol infection of mice with influenza virus [5].

High impact information on farnesol

• A Chinese hamster ovary cell mutant F2A8 utilizes polyprenol rather than dolichol for its lipid-dependent asparagine-linked glycosylation reactions [6].
• Next, the mixture of the prenol type (polyprenol) and dolichol type (dihydropolyprenol) was subjected to this capillary HPLC system, and the separation of each homolog was successfully achieved [7].
• Enhancement of resistance to Escherichia coli infection in mice by dihydroheptaprenol, a synthetic polyprenol derivative [8].
• The lipid moiety of the mannosyl derivative formed behaved as a polyprenol having 11 isoprene residues as judged by t.l.c. and be gel filtration in sodium deoxycholate-containing buffers [9].
• Alkaline hydrolysis of the glycolipid, followed by high-pressure liquid chromatography, showed the presence of a series of polyprenol homologues identical with those isolated directly from Saccharomyces cerevisiae (baker's yeast) [10].

Biological context of farnesol

• None of these compounds was degraded by catalytic hydrogenation, and so the lipid moiety in each case was probably an alpha-saturated polyprenol [11].
• This review focuses on the catalytic mechanism and substrate specificity of these bacterial UDP-D-N-acetylhexosamine: polyprenol phosphate D-N-acetylhexosamine 1-P transferases and may provide insights for the development of selective inhibitors of cell wall biosynthesis [12].
• These findings are significant in terms of understanding the glycosylation phenotypes of Chinese hamster ovary cell mutants of the Lec9 complementation group, which lack the ability to convert polyprenol into dolichol [13].
• It is clear that microsomes from plant systems can catalyze the phosphorylation of polyprenol better than rat liver when compared with their abilities to catalyze the phosphorylation of dolichol [14].
• Seasonal variations were observed in the polyprenol content in green leaves [15].

Anatomical context of farnesol

• The biosynthesis of crustacean chitin. Isolation and characterization of polyprenol-linked intermediates from brine shrimp microsomes [16].
• Modulation of properties of phospholipid membranes by the long-chain polyprenol (C(160)) [17].
• Hydrogenated polyprenol phosphates - exogenous lipid acceptors of glucose from UDP glucose in rat liver microsomes [18].
• Dihydroheptaprenol (DHP), a synthetic polyprenol derivative, markedly stimulated the generation of peripheral blood neutrophils after intramuscular injection in miniature pigs [19].
• It has been found that rabbit reticulocyte plasma membranes contain the enzymatic activities responsible for the synthesis of all the polyprenol-bound sugars that are intermediates in the glycosylation of proteins [20].

Associations of farnesol with other chemical compounds

• The polyprenol product of Srt1p is longer in chain length than that of Rer2p and is not sufficiently converted to dolichol and dolichyl phosphate, unlike that of Rer2p [21].
• Using ESI(Li+)-MS and ESI(Li+)-MS/MS analysis, we screened for polyprenol products of an octaprenyl pyrophosphate synthase of Plasmodium falciparum and dolichols in a complex mixture of compounds produced by Leishmania amazonensis and P. falciparum [22].
• A new branched polyprenol, designated cupaniol, has been isolated from the methanol extract of the leaves of Cupania latifolia (Sapindaceae) [23].
• Synthesis of a mannosyl phosphoryl polyprenol by the cellular slime mold Dictyostelium discoideum [24].

Gene context of farnesol

• Our results suggest that the activities of two yeast cis-prenyltransferases Rer2p and Srt1p and polyprenol reductase are not co-regulated and that reductase may be the rate-limiting enzyme in dolichol synthesis if the amount of polyisoprenoids synthesized exceeds a certain level [25].
• Evaluation of these compounds as potential substrates or inhibitors of a polyprenol monophosphomannose-dependent alpha-(1-->6)-mannosyltransferase involved in mycobacterial LAM biosynthesis demonstrated that the enzyme is somewhat tolerant substitution at this site [26].

Analytical, diagnostic and therapeutic context of farnesol

• We attempted an analysis of naturally occurring polyprenol and dolichol using a monolithic silica capillary column in HPLC [7].
• Single polyprenol and dolichol isolation by semipreparative high-performance liquid chromatography technique [27].
• A high-resolution analysis of polyprenol mixtures was achieved by supercritical fluid chromatography (SFC) [28].

References