Effects of chain length and sulphur position of thia fatty acids on their incorporation into phospholipids in 7800 C1 hepatoma cells and isolated rat hepatocytes, and their effects on fatty acid composition of phospholipids.
Incorporation of thia fatty acids and their effects on the fatty acid composition in phospholipids has been investigated in 7800 C1 hepatoma cells and cultured hepatocytes. 3-Thia fatty acids of chain lengths from dodecyl-to hexadecyl-thioacetic acid were incorporated into phospholipids during a 3-day incubation. Longer and shorter 3-thia fatty acids were barely detectable. Tetradecylthioacetic acid, 3-thia stearate, and their delta9- desaturated derivatives were maximally incorporated into whole-cell phospholipids. The amount of tetradecylthioacetic acid incorporated into phospholipids of hepatoma cells remained almost identical in cells cultured for 3 days or adapted over a period of 1 year. Delta9-desaturated metabolites of long chain thia fatty acids (C13-to C16-S-acetic acid) were identified by GC-MS in phospholipids. 3-Thia stearate appeared to be the best substrated for delta9 desaturase. Incubation of hepatoma cells with thia fatty acids led to alterations in the amount of normal fatty acids in total phospholipids. The amounts of 16:0 and 18:1 decreased and 18:2 (n-6) and 20:5 (n-3) increased. Changes in the normal fatty acid composition of phospholipids were seen both with thia acids incorporated into phospholipids and those not incorporated. These effects, therefore, may be only partially dependent on displacement of normal fatty acids by thia fatty acids. Morris 7800 C1 hepatoma cell acyl-CoA synthetase (ACS) and peroxisomal acyl-CpA oxidase (ACO) were induced by thia fatty acids of all chain lengths, and with the sulphur atom(s) in different positions. Control experiments with hepatocytes revealed a similar incorporation of thia fatty acids in these physiologically more normal cells.
Wu
P
P
Institute of Medical Biochemistry, University of Oslo, Norway.
Grav
H J
HJ
Horn
R
R
Bremer
J
J
D042962:Acyl-CoA Oxidase; D000818:Animals; D002478:Cells, Cultured; D003066:Coenzyme A Ligases / Q000096:biosynthesis; D004790:Enzyme Induction; D005227:Fatty Acids / Q000378:metabolism* / Q000494:pharmacology; D008099:Liver / Q000166:cytology / Q000378:metabolism; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D008297:Male; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000096:biosynthesis; D010743:Phospholipids / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D013329:Structure-Activity Relationship; D013440:Sulfides / Q000378:metabolism* / Q000494:pharmacology; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
D005227:Fatty Acids; D010743:Phospholipids; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D013440:Sulfides; C062078:1-(carboxymethylthio)tetradecane; D010088:Oxidoreductases; D042962:Acyl-CoA Oxidase; D003066:Coenzyme A Ligases; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase