scholarly journals 577 Plasma exosomal miR-375-3p regulates ferroptosis in keratinocytes by targeting lipid transporter GPX4 in SJS/TEN

2020 ◽  
Vol 140 (7) ◽  
pp. S79
Author(s):  
C. Zhang ◽  
G. Wang ◽  
M. Fu
Keyword(s):  
Lipid Transporter

Homozygous mutation in ABCA3 Lipid-Transporter defect (EXON 9) and low level of surfactant protein C

2010 ◽  
Vol 222 (S 01) ◽  
Author(s):  
J Pöschl ◽  
P Ruef ◽  
M Griese ◽  
P Lohse ◽  
C Aslanidis ◽  
...  
Keyword(s):  
Protein C ◽  
Surfactant Protein ◽  
Homozygous Mutation ◽  
Surfactant Protein C ◽  
Low Level ◽  
Exon 9 ◽  
Lipid Transporter

scholarly journals Structure of a proton-dependent lipid transporter involved in lipoteichoic acids biosynthesis

2020 ◽  
Vol 27 (6) ◽  
pp. 561-569
Author(s):  
Bing Zhang ◽  
Xue Liu ◽  
Elisabeth Lambert ◽  
Guillaume Mas ◽  
Sebastian Hiller ◽  
...  
Keyword(s):  
Lipid Transporter ◽  
Lipoteichoic Acids

scholarly journals MmpL3 is a lipid transporter that binds trehalose monomycolate and phosphatidylethanolamine

2019 ◽  
Vol 116 (23) ◽  
pp. 11241-11246 ◽  
Author(s):  
Chih-Chia Su ◽  
Philip A. Klenotic ◽  
Jani Reddy Bolla ◽  
Georgiana E. Purdy ◽  
Carol V. Robinson ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Envelope ◽  
Native Mass Spectrometry ◽  
Mycolic Acids ◽  
Mycobacterial Cell ◽  
Exact Function ◽  
Species Specific ◽  
Mycobacterial Cell Wall ◽  
Trehalose Monomycolate ◽  
Lipid Transporter

The cell envelope ofMycobacterium tuberculosisis notable for the abundance of mycolic acids (MAs), essential to mycobacterial viability, and of other species-specific lipids. The mycobacterial cell envelope is extremely hydrophobic, which contributes to virulence and antibiotic resistance. However, exactly how fatty acids and lipidic elements are transported across the cell envelope for cell-wall biosynthesis is unclear. Mycobacterial membrane protein Large 3 (MmpL3) is essential and required for transport of trehalose monomycolates (TMMs), precursors of MA-containing trehalose dimycolates (TDM) and mycolyl arabinogalactan peptidoglycan, but the exact function of MmpL3 remains elusive. Here, we report a crystal structure ofMycobacterium smegmatisMmpL3 at a resolution of 2.59 Å, revealing a monomeric molecule that is structurally distinct from all known bacterial membrane proteins. A previously unknown MmpL3 ligand, phosphatidylethanolamine (PE), was discovered inside this transporter. We also show, via native mass spectrometry, that MmpL3 specifically binds both TMM and PE, but not TDM, in the micromolar range. These observations provide insight into the function of MmpL3 and suggest a possible role for this protein in shuttling a variety of lipids to strengthen the mycobacterial cell wall.

scholarly journals Therv1184cLocus Encodes Chp2, an Acyltransferase in Mycobacterium tuberculosis Polyacyltrehalose Lipid Biosynthesis

2014 ◽  
Vol 197 (1) ◽  
pp. 201-210 ◽  
Author(s):  
Megan H. Touchette ◽  
Cynthia M. Holsclaw ◽  
Mary L. Previti ◽  
Viven C. Solomon ◽  
Julie A. Leary ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Cell Envelope ◽  
Selective Inhibition ◽  
Serine Hydrolase ◽  
Acyltransferase Activity ◽  
Content Type ◽  
Regulatory Interactions ◽  
Similar Phenotype ◽  
Lipid Transporter

Trehalose glycolipids are found in many bacteria in the suborderCorynebacterineae, but methyl-branched acyltrehaloses are exclusive to virulent species such as the human pathogenMycobacterium tuberculosis. InM. tuberculosis, the acyltransferase PapA3 catalyzes the formation of diacyltrehalose (DAT), but the enzymes responsible for downstream reactions leading to the final product, polyacyltrehalose (PAT), have not been identified. The PAT biosynthetic gene locus is similar to that of another trehalose glycolipid, sulfolipid 1. Recently, Chp1 was characterized as the terminal acyltransferase in sulfolipid 1 biosynthesis. Here we provide evidence that the homologue Chp2 (Rv1184c) is essential for the final steps of PAT biosynthesis. Disruption ofchp2led to the loss of PAT and a novel tetraacyltrehalose species, TetraAT, as well as the accumulation of DAT, implicating Chp2 as an acyltransferase downstream of PapA3. Disruption of the putative lipid transporter MmpL10 resulted in a similar phenotype. Chp2 activity thus appears to be regulated by MmpL10 in a relationship similar to that between Chp1 and MmpL8 in sulfolipid 1 biosynthesis. Chp2 is localized to the cell envelope fraction, consistent with its role in DAT modification and possible regulatory interactions with MmpL10. Labeling of purified Chp2 by an activity-based probe was dependent on the presence of the predicted catalytic residue Ser141 and was inhibited by the lipase inhibitor tetrahydrolipstatin (THL). THL treatment ofM. tuberculosisresulted in selective inhibition of Chp2 over PapA3, confirming Chp2 as a member of the serine hydrolase superfamily. Efforts to producein vitroreconstitution of acyltransferase activity using straight-chain analogues were unsuccessful, suggesting that Chp2 has specificity for native methyl-branched substrates.

scholarly journals The ATP Binding Cassette Multidrug Transporter LmrA and Lipid Transporter MsbA Have Overlapping Substrate Specificities

2003 ◽  
Vol 278 (37) ◽  
pp. 35193-35198 ◽  
Author(s):  
Galya Reuter ◽  
Tavan Janvilisri ◽  
Henrietta Venter ◽  
Sanjay Shahi ◽  
Lekshmy Balakrishnan ◽  
...  
Keyword(s):  
Atp Binding ◽  
Multidrug Transporter ◽  
Substrate Specificities ◽  
Lipid Transporter ◽  
Atp Binding Cassette

scholarly journals Structure of MlaFEDB lipid transporter reveals an ABC exporter fold and two bound phospholipids

2020 ◽  
Vol 76 (a1) ◽  
pp. a82-a82
Author(s):  
Damian Ekiert ◽  
Nicolas Coudray ◽  
Georgia Isom ◽  
Mark MacRae ◽  
Mariyah Saiduddin ◽  
...  
Keyword(s):  
Lipid Transporter

scholarly journals T329S Mutation in the FMO3 Gene Alleviates Lipid Metabolic Diseases in Chickens in the Late Laying Period

Animals ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 48
Author(s):  
Jianlou Song ◽  
Mingyi Huang ◽  
Xuefeng Shi ◽  
Xianyu Li ◽  
Xia Chen ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Serum Lipid ◽  
Metabolic Diseases ◽  
Laying Hens ◽  
Total Bile Acid ◽  
Production Performance ◽  
Atherosclerotic Lesions ◽  
Similar Body ◽  
Lipid Transporter ◽  
Lipid Parameters

The T329S mutation in flavin-containing monooxygenase 3 (FMO3) impairs the trimethylamine (TMA) metabolism in laying hens. The TMA metabolic pathway is closely linked to lipid metabolic diseases, such as atherosclerosis and fatty liver disease. We aimed to evaluate the effects of the T329S mutation in FMO3 on lipid metabolism in chickens during the late laying period. We selected 18 FMO3 genotyped individuals (consisting of six AA, six AT, and six TT hens) with similar body weight and production performance. The lipid metabolism and deposition characteristics of the laying hens with different genotypes were compared. The T329S mutation moderated the serum-lipid parameters in TT hens compared to those in AA and AT hens from 49 to 62 weeks. Furthermore, it reduced the serum trimethylamine N-oxide concentrations and increased the serum total bile acid (p < 0.05) and related lipid transporter levels in TT hens. Moreover, it significantly (p < 0.01) decreased atherosclerotic lesions and hepatic steatosis in TT hens compared to those in the AA and AT hens. Our findings may help improve the health status in laying hens during the late laying period.

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