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.

Effects of glucose on fatty acid oxidation by diaphragms from normal and alloxan-diabetic fed and starved rats

1960 ◽  
Vol 198 (1) ◽  
pp. 39-44 ◽  
Author(s):  
Irving B. Fritz ◽  
Eli Kaplan
Keyword(s):  
Fatty Acid ◽  
Palmitic Acid ◽  
Fatty Acid Oxidation ◽  
Octanoic Acid ◽  
Diabetic Rats ◽  
Chain Fatty Acid ◽  
Acid Oxidation ◽  
Long Chain Fatty Acid ◽  
Fatty Acid Degradation ◽  
Long Chain

Palmitic acid-1-C14 oxidation by hemidiaphragms was measured in tissues from fed and starved normal and alloxanized rats. Muscle from normal rats starved for 3 days or longer showed an enhanced conversion of added palmitate to C14O2, while fasting for 1 or 2 days had little effect on fatty acid degradation by diaphragms from normal rats. Tissues from fed or starved alloxan diabetic animals had an augmented oxidation of labeled palmitate. The addition of glucose to the medium spared fatty acid oxidation by diaphragms from starved or diabetic rats but did not influence palmitate degradation by tissues from normal fed rats. The presence of insulin increased the glucose sparing action on long-chain fatty acid oxidation but was without effect on palmitate oxidation in the absence of added glucose. The conversion of C14-octanoic acid to C14O2 by muscle was not influenced by previous starvation nor by addition of glucose to the medium. Glucose-U-C14 and glucose-1-C14 conversion to C14O2 and glycogen were essentially the same in diaphragms from fed and starved animals.

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 The binding of L-tryptophan to serum albumins in the presence of non-esterified fatty acids

1975 ◽  
Vol 146 (3) ◽  
pp. 653-658 ◽  
Author(s):  
V J Cunningham ◽  
L Hay ◽  
H B Stoner
Keyword(s):  
Fatty Acids ◽  
Oleic Acid ◽  
Fatty Acid ◽  
Palmitic Acid ◽  
Lauric Acid ◽  
Human Albumin ◽  
Acid Sites ◽  
Chain Fatty Acid ◽  
Serum Albumins ◽  
Long Chain

Bovine, human and rat serum albumins were defatted and palmitic acid, oleic acid and lauric acid added in various molar ratios. The binding of L-tryptophan to these albumins was measured at 20 degrees C in a 0.138 M salt solution at pH 7.4, by using an ultrafiltration technique, and analysed in terms of n, the number of available tryptophan-binding sites per albumin molecule, with apparent association constant, k. 2. n and k were 0.90 and 2.3}10(-4)M(minus-1) respectively for defatted bovine serum albumin and 0.87 and 9.7}10(-3)M(-minus-1) for human albumin. Addition of palmitic acid did not decrease n until the molar ratio, fatty acid/bovine albumin, approached and exceeded 2. The decrease in k was small and progressive. In contrast, lauric caused a marked decrease in n and k at ratios as low as 0.5. A similar distinction between the effects on n of palmitic acid and oleic acid and those of lauric acid was seen for human albumin. k for human albumin was not significantly affected by fatty acids under the conditions studied. 3. It is concluded that primary long-chain fatty acid sites interact only weakly with the tryptophan site on albumin and that inhibition of tryptophan binding occurs when secondary long-chain sites are occupied. Primary medium-chain fatty acid sites are distinct from primary long-chain sites but may be grouped with secondary long-chain sites. 4. The relationship between free and bound tryptophan in samples of rat plasma (Stoner et al., 1975) is discussed in terms of a similar but limited study of rat albumin.

Long Chain Fatty Acid Uptake by Human Intestinal Mucosa in vitro: Mechanisms of Transport

Digestion ◽  
2003 ◽  
Vol 67 (1-2) ◽  
pp. 32-36 ◽  
Author(s):  
Célia Regina M. Chaves ◽  
Paulo Roberto P. Elias ◽  
Wanli Cheng ◽  
Cyrla Zaltman ◽  
Antônio Carlos R. Iglesias ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Intestinal Mucosa ◽  
Fatty Acid Uptake ◽  
Chain Fatty Acid ◽  
Acid Uptake ◽  
Long Chain Fatty Acid ◽  
Long Chain
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