On the oxidation of long-chain polyunsaturated alcohols by myelinating rat brain

Su, Kwei Lee; Schmid, Harald H.O.

doi:10.1016/0006-291x(72)90348-8

Cited by 7 publications

(6 citation statements)

References 14 publications

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“…Further more, the proportion of octadecenyl alcohol in the lipids of this tissue which was initially low did not change throughout this time period. Since the total amount of long-chain alcohols present in brain is small, and long-chain alcohols if injected into the brain are known to be readily oxidized to long chain acids, one would expect octadecenyl alcohol to represent a large proportion of the total long-chain alcohols after a 2-week feeding interval if this lipid type can penetrate the blood-brain barrier (18,22).…”

Section: Discussionmentioning

confidence: 99%

“…Information concerning the enzymes involved in long-chain alcohol biosyn thesis in brain is limited, but it is known that long-chain acids can be reduced to long-chain aldehydes and alcohols in this tissue (4,18,23) and that the aldehyde reductase of brain is inhibited by drugs such as chlorpromazine and the barbitu rates (20.21).…”

Section: Discussionmentioning

confidence: 99%

“…Whether the long-chain alcohols of plasma enter the brain is of particular interest, since long-chain alcohols of varying degrees of unsaturation and chain length injected directly into the brain are readily oxidized to long-chain acids or incorporated into the alkoxy glycerols of brain (19). Yet qualitative analysis of the alkoxy glycerols of brain has shown a restricted distribution of the fatty chains in these ether moitiés (14,18,19).…”

Section: Introductionmentioning

confidence: 99%

“…Yet qualitative analysis of the alkoxy glycerols of brain has shown a restricted distribution of the fatty chains in these ether moitiés (14,18,19). Furthermore, drugs such as chlorpro mazine and the barbiturates are known to be effective inhibitors of the aldehyde reductase of brain (20,21).…”

Section: Introductionmentioning

confidence: 99%

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Permeability of the Blood-Brain Barrier to Long-Chain Alcohols from Plasma

Gelman¹,

Gilbertson²

1975

Ann Nutr Metab

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Cis-9-octadecenyl alcohol was fed as a dietary supplement to adult male rats for 7 and 14 days. At the end of these feeding intervals, lipids were extracted from brain and liver. The neutral lipids were analyzed for free and esterified long-chain alcohols and alkyl and alk-1-enyl glycerols. Total lipid phosphorus, alkyl acyl and alk-1-enyl acyl phosphoglycerides were determined in the phospholipid fraction. A marked change was observed in these lipid types in the liver, but not in the brain. In liver the free and esterified long-chain alcohols increased threefold following feeding of the dietary supplement. Feeding cis-9-octadecenyl alcohol had no effect on the neutral alkoxy lipids of liver but resulted in an approximately three- to eightfold increase in the ionic alkoxy lipids.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Permeability of the Blood-Brain Barrier to Long-Chain Alcohols from Plasma

Gelman¹,

Gilbertson²

1975

Ann Nutr Metab

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“…[ l-'4C]Hexadecanol was prepared by lithium aluminum hydride reduction of the corresponding fatty acid methyl ester, purified by TLC ( Su and Schmid, 1972), and oxidized to the aldehyde with pyridinium chlorochromate in dichloromethane (Corey and Suggs, 1975). The crude [Z-14C]palmitaldehyde was purified by TLC (silica gel H) using hexane-diethyl ether (9: 1).…”

Section: Preparation Of [ L-14c]palmitaldehydementioning

confidence: 99%

Biosynthesis of Long‐Chain Alcohols by Developing and Regenerating Rat Sciatic Nerve

Natarajan¹,

Schmid²,

Sastry³

1984

Journal of Neurochemistry

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Cell-free preparations of rat sciatic nerve were found to catalyze the reduction of fatty acid to alcohol in the presence of NADPH as reducing cofactor. The reductase was membrane-bound and associated primarily with the microsomal fraction. When fatty acid was the substrate, ATP, coenzyme A (CoA), and Mg2+ were required, indicating the formation of acyl CoA prior to reduction. When acyl CoA was used as substrate, the presence of albumin was required to inhibit acyl CoA hydrolase activity. Fatty acid reductase activity was highest with palmitic and stearic acids, and somewhat lower with lauric and myristic acids. It was inhibited by sulfhydryl reagents, indicating the participation of thiol groups in the reduction. Only traces of long-chain aldehyde could be detected or trapped as semicarbazone. Fatty acid reductase activity in rat sciatic nerve was highest between the second and tenth days after birth and decreased substantially thereafter. Microsomal preparations of sciatic nerve from 10-day-old rats exhibited about four times higher fatty acid reductase activity than brain or spinal cord microsomes from the same animals. Wallerian degeneration and regeneration of adult rat sciatic nerve resulted in enhanced fatty acid reductase activity, which reached a maximum at about 12 days after crush injury.

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