Vibrio cholerae VC1741 (PsrA) enhances the colonization of the pathogen in infant mice intestines in the presence of the long-chain fatty acid, oleic acid

2020 ◽  
Vol 147 ◽  
pp. 104443
Author(s):  
Shuang Yang ◽  
Daoyi Xi ◽  
Xiaochen Wang ◽  
Yuehua Li ◽  
Yujia Li ◽  
...  
Keyword(s):  
Oleic Acid ◽  
Fatty Acid ◽  
Vibrio Cholerae ◽  
Chain Fatty Acid ◽  
Long Chain Fatty Acid ◽  
Long Chain

scholarly journals FAT/CD36-mediated Long-Chain Fatty Acid Uptake in Adipocytes Requires Plasma Membrane Rafts

2005 ◽  
Vol 16 (1) ◽  
pp. 24-31 ◽  
Author(s):  
Jürgen Pohl ◽  
Axel Ring ◽  
Ümine Korkmaz ◽  
Robert Ehehalt ◽  
Wolfgang Stremmel
Keyword(s):  
Plasma Membrane ◽  
Oleic Acid ◽  
Fatty Acid ◽  
Lipid Rafts ◽  
Chain Fatty Acid ◽  
Dominant Negative Mutant ◽  
Acid Uptake ◽  
Long Chain Fatty Acid ◽  
Lcfa Uptake ◽  
Long Chain

We previously reported that lipid rafts are involved in long-chain fatty acid (LCFA) uptake in 3T3-L1 adipocytes. The present data show that LCFA uptake does not depend on caveolae endocytosis because expression of a dominant negative mutant of dynamin had no effect on uptake of [3H]oleic acid, whereas it effectively prevented endocytosis of cholera toxin. Isolation of detergent-resistant membranes (DRMs) from 3T3-L1 cell homogenates revealed that FAT/CD36 was expressed in both DRMs and detergent-soluble membranes (DSMs), whereas FATP1 and FATP4 were present only in DSMs but not DRMs. Disruption of lipid rafts by cyclodextrin and specific inhibition of FAT/CD36 by sulfo-N-succinimidyl oleate (SSO) significantly decreased uptake of [3H]oleic acid, but simultaneous treatment had no additional or synergistic effects, suggesting that both treatments target the same mechanism. Indeed, subcellular fractionation demonstrated that plasma membrane fatty acid translocase (FAT/CD36) is exclusively located in lipid rafts, whereas intracellular FAT/CD36 cofractionated with DSMs. Binding assays confirmed that [3H]SSO predominantly binds to FAT/CD36 within plasma membrane DRMs. In conclusion, our data strongly suggest that FAT/CD36 mediates raft-dependent LCFA uptake. Plasma membrane lipid rafts might control LCFA uptake by regulating surface availability of FAT/CD36.

scholarly journals Acylation of lysolecithin in the intestinal mucosa of rats

1970 ◽  
Vol 118 (2) ◽  
pp. 241-246 ◽  
Author(s):  
P. V. Subbaiah ◽  
P. S. Sastry ◽  
J. Ganguly
Keyword(s):  
Oleic Acid ◽  
Fatty Acid ◽  
Palmitic Acid ◽  
Intestinal Mucosa ◽  
Brush Border ◽  
Chain Fatty Acid ◽  
Long Chain Fatty Acid ◽  
Free Oleic Acid ◽  
Acyl Acceptors ◽  
Long Chain

1. The presence of an active acyl-CoA–lysolecithin (1-acylglycerophosphorylcholine) acyltransferase was demonstrated in rat intestinal mucosa. 2. ATP and CoA were necessary for the incorporation of free [1-14C]oleic acid into lecithin (phosphatidylcholine). 3. The reaction was about 20 times as fast with [1-14C]oleoyl-CoA as with free oleic acid, CoA and ATP. 4. With 1-acylglycerophosphorylcholine as the acceptor, both oleic acid and palmitic acid were incorporated into the β-position of lecithin; the incorporation of palmitic acid was 60% of that of oleic acid. 5. Of the various analogues of lysolecithin tested as acyl acceptors from [1-14C]oleoyl CoA, a lysolecithin with a long-chain fatty acid at the 1-position was most efficient. 6. The enzyme was mostly present in the brush-border-free particulate fraction of the intestinal mucosa. 7. Of the various tissues of rats tested for the activity, intestinal mucosa was found to be the most active, with testes, liver, kidneys and spleen following it in decreasing order.

scholarly journals Long-chain fatty acid-induced changes in gene expression in neonatal cardiac myocytes

2000 ◽  
Vol 41 (1) ◽  
pp. 41-47 ◽  
Author(s):  
Karin A. J.M. van der Lee ◽  
Michaël M. Vork ◽  
Johan E. De Vries ◽  
Peter H.M. Willemsen ◽  
Jan F.C. Glatz ◽  
...  
Keyword(s):  
Gene Expression ◽  
Fatty Acid ◽  
Cardiac Myocytes ◽  
Chain Fatty Acid ◽  
Long Chain Fatty Acid ◽  
Induced Changes ◽  
Long Chain
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