Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase.

Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase. Research Abstract Details 

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Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase. Abstract Text:

T Nakamura,H Reicher,W Sattler,

The purpose of the present investigation was to test whether permanent skeletal muscle cells (rat L6 cells) could serve as an in vitro model for alpha-tocopherol (alphaTocH) biodiscrimination studies. L6 cells were incubated in the presence of high density lipoprotein (HDL), low density lipoprotein (LDL), and very low density lipoprotein (VLDL) labeled in the lipid moiety with either all-rac- or RRR-[14C]alphaTocH. These incubations were performed either in the absence or in the presence of exogenously added bovine lipoprotein lipase (LPL) since skeletal muscle is one of the major expression sites of LPL in vivo. Time-dependent uptake studies (up to 24 h) in the absence of LPL have shown that equipotent doses of all-rac- and RRR-[14C]alphaTocH (1.36:1) led to almost identical accumulation of the tracer, independent of the lipoprotein class used as alphaTocH carrier. With regard to alphaTocH donor capacity, it appeared that HDL is the most potent alphaTocH donor, followed by LDL and VLDL. In the presence of LPL, all-rac- and RRR-[14C]alphaTocH uptake was significantly enhanced (between two- and tenfold). Biodiscrimination studies using chiral high-performance liquid chromatographic analysis with radiometric detection of the corresponding methyl ether derivatives on a Chiralcel OD column have demonstrated that the 2S-and 2R-isomers of alphaTocH were taken up in a 1:1 ratio by L6 cells independent of the absence or presence of LPL. In addition, we have not observed biodiscrimination between the four 2R-isomers, i.e., there was no preferential accumulation of the RRR-isomer. These data suggest that L6 cells do not discriminate between different alphaTocH isomers and that the addition of endogenous LPL significantly enhances the uptake of RRR- and all-rac-alphaTocH.

Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase. Publishing Authors By Initials

T Nakamura,H Reicher,W Sattler,

For similar heterocyclic compounds: heterocyclic compounds, 2-ring: benzopyrans: vitamin e: tocopherols: alpha-tocopherol research abstracts see: heterocyclic compounds: heterocyclic compounds, 2-ring: benzopyrans: vitamin e: tocopherols: alpha-tocopherol research

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Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Lipids

VOLUME: 33

Page Numbers: 1001-8

Journal Abbreviation: Lipids

ISSN: 0024-4201

DAY: 19

MONTH: Oct

YEAR: 1998

Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 60450

Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase. Keywords Mesh Terms:

KEYWORDS: alpha-Tocopherol

MESH TERMS: analogs & derivatives

Chemical & Substance for Abstract: Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase. Information

Substance Name: Lipoprotein Lipase

Registry Number: EC 3.1.1.34

Grant and Affiliation Information for Comparison of RRR-alpha- and all-rac-alpha-tocopherol uptake by permanent rat skeletal muscle myoblasts (L6 cells): effects of exogenous lipoprotein lipase.

AFFILIATION: Eisai Co., Ltd., Vitamin E Technology Section, Tokyo, Japan.

Country: UNITED STATES

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MEDLINETA: Lipids

REFSOURCE: Lipids 1999 Jan;34(1):93

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