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Results for “ESTERIFICATION”

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At least 721 records · Page 40Linked to original sources

PubMed2001

Cholesteryl ester transfer and cholesterol esterification in type 1 diabetes: relationships with plasma glucose.

The activities of two crucial enzymes of reverse cholesterol transport, cholesterol ester transfer protein (CETP) and lecithin:cholesterol acyltransferase (LCAT), and their relationships with lipid profile and fasting plasma glucose were examined in 35 type 1 diabetic children. The CETP and LCAT activities were significantly lower (p<0.05) in the 4 subjects with normal fasting plasma glucose levels (<6.39 mmol/l) than in the 28 with high plasma glucose levels (CEPT activity, 10.63+/-3.81 vs. 32.18+/-13.94 nmol/ml h; LCAT activity, 25.52+/-4.53 vs. 39.52+/-12.52 nmol/ml h; both p<0.05). The subjects with high plasma glucose levels also had higher total and LDL-cholesterol than those with normal glucose levels. CETP activity was positively correlated with fasting plasma glucose, CETP concentration, LCAT activity, total cholesterol, free cholesterol, LDL-C, and LDL-cholesteryl ester, while negatively correlated with cholesteryl ester to free cholesterol ratio, LDL triglyceride to protein ratio, and LDL triglyceride to cholesteryl ester ratio. LCAT activity was found to positively correlate with CETP activity, total cholesterol, free cholesterol, LDL-C, CETP concentration, and LDL-cholesteryl ester, while it negatively correlated with cholesteryl ester to free cholesterol ratio. The results observed in type 1 diabetic subjects suggest that (1) accelerated LCAT and CETP activities may result in the accumulation of LDL-cholesteryl ester; and (2) fasting plasma glucose may be a major determinant of CETP activity.

Blood Glucose↗

PubMed2004

Oxidation rate of conjugated linoleic acid and conjugated linolenic acid is slowed by triacylglycerol esterification and alpha-tocopherol.

We have recently shown that alpha-eleostearic acid (alpha-ESA), a conjugated linolenic acid, has a stronger antitumor effect than conjugated linoleic acid (CLA), both in vitro and in vivo. In this study, the oxidative stability of alpha-ESA was examined compared with linoleic acid (LA), alpha-linolenic acid (LnA), and CLA. Thin layers of the FA (LA, 9Z,11 E-CLA, 10E,12Z-CLA, LnA, and alpha-ESA) were auto-oxidized at 37 degrees C, and the FA remaining, the absorbed oxygen volume, the lipid hydroperoxide content, and the TBARS content were determined. The oxidation rate of alpha-ESA was faster than that of the unconjugated FA and CLA (9Z, 11 E-CLA and 10E, 12Z-CLA). However, the lipid hydroperoxide and TBARS contents following alpha-ESA oxidation were low, suggesting production of only small amounts of rapid-reacting secondary oxidation products. Furthermore, the oxidative stability of conjugated FA (CLA and CLnA) in which the carboxylic acid group was esterified with triacylglycerol was greater than that of the FFA. Addition of an antioxidant (alpha-tocopherol) also increased the stability of the conjugated FA to a level similar to that of the unconjugated FA.

Esterification↗

PubMed2004

Beta-oxidation, esterification, and secretion of radiolabeled fatty acids in cultivated Atlantic salmon skeletal muscle cells.

The white muscle of Atlantic salmon metabolizes FA with different chain lengths and different saturations at different rates, but few details are available on the processes involved or the products formed. We have investigated how multinucleated muscle cells (myotubes) in culture metabolize [1-(14)C]8:0, [1-(14)C]18:1n-9, and [1-(14)C]20:5n-3. The myotubes were formed by the differentiation of isolated myosatellite cells from the white skeletal muscle of salmon fry. Almost all (98%) of the [1-(14)C]8:0 substrate was oxidized to acid-soluble products (ASP) and (14)CO2 after 48 h of incubation, whereas only approximately 50% of the [1-(14)C]18:1n-9 and [1-(14)C]20:5n-3 substrates were oxidized. However, only one cycle of beta-oxidation was measured by the method used. For all three substrates, the main ASP were acetate and a combined fraction of oxaloacetate and malate. Nearly twice as much radioactivity from the [1-(14)C]20:5n-3 substrate was found in the cellular lipids as radioactivity from [1-(14)C]18:1n-9, indicating that [1-(14)C]20:5n-3 was taken up into muscle cells more rapidly than [1-(14)C]18:1n-9. Approximately 10% of the added [1-(14)C]20:5n-3 substrate and 5% of the added [1-(14)C]18:1n-9 substrate was secreted from the muscle cells into the culture media as esterified lipids. Immunocytochemical staining showed that the cells synthesized apolipoprotein A-I. Differentiated muscle cells also expressed peroxisome proliferator-activated receptor alpha (PPARalpha) and PPARbeta, two transcription factors that are involved in regulating beta-oxidation.

Animals↗

PubMed1953