November 1, 1995Journal of Lipid ResearchOpen Access

Structural features in lipoprotein lipase necessary for the mediation of lipoprotein uptake into cells

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Population

Cultured Hep3b cells and COS-cells expressing naturally occurring variants and lipoprotein lipase mutants

Comparison

LpL mutants produced by site-directed mutagenesis vs Wild type LpL

Design

Preclinical

Authors

AKA. KrappUniversität Hamburg HZH ZhangUniversity of British Columbia DGDavid G. GinzingerThermo Fisher Scientific (United States)

Discussion

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Implication

Residues 390-393 and Arg294 support LpL-mediated uptake in vitro; hypothesis-generating for therapeutic targeting in dyslipidemia.

Structured PICO

Population

Cultured Hep3b cells and COS-cells expressing naturally occurring variants and lipoprotein lipase (LpL) mutants

Intervention

LpL mutants produced by site-directed mutagenesis (Asp156Gly, Trp390Ala, Trp393Ala, substitution of 390-393 with homologous hepatic lipase sequence, deletion of 390-393, Arg294Ala)

Comparator

Wild type LpL

Outcome

Ability to mediate the uptake of 125I-labeled beta-VLDLsurrogate

Sites involved in heparin and lipid binding between residues 390-421, as well as the monomer/dimer ratio, are critical for LpL-mediated lipoprotein uptake into cells.

Cite This Study

Krapp et al. (1995) studied this question.

synapsesocial.com/papers/6a82c140a7c6f3cae68addeb https://doi.org/10.1016/s0022-2275(20)39717-0

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Structural features in lipoprotein lipase necessary for the mediation of lipoprotein uptake into cells

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Structural features in lipoprotein lipase necessary for the mediation of lipoprotein uptake into cells

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider