What does this research mean for the field?

The N-terminal 17% of human apolipoprotein B (apoB-17) is capable of binding lipids to form discoidal particles and likely contributes to the stabilization of triglyceride-rich lipoproteins. Novelty: ClaimNovelty.INCREMENTAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

August 15, 1991Proceedings of the National Academy of SciencesOpen Access

Expression, secretion, and lipid-binding characterization of the N-terminal 17% of apolipoprotein B.

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Structured PICO

Population

Murine C127 cells transfected with a bovine papilloma virus-based expression vector to express the N-terminal 17% of human apolipoprotein B (apoB-17)

Intervention

Expression of apoB-17 and exposure to 1.2 mM oleate or dimyristoylphosphatidylcholine (DMPC)

Outcome

Secretion kinetics, lipid-binding properties, and structural characteristics of apoB-17surrogate

The N-terminal 17% of apoB-100 can bind lipid and form lipoprotein-like particles, suggesting it contributes to the stabilization of triglyceride-rich lipoproteins.

Discussion

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Implication

Hypothesis-generating for apoB N-terminal lipid binding; human validation required before any clinical relevance.

Cite This Study

Herscovitz et al. (1991) studied this question.

synapsesocial.com/papers/6a1d705f73c56dd1bd2fae29 https://doi.org/10.1073/pnas.88.16.7313

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Expression, secretion, and lipid-binding characterization of the N-terminal 17% of apolipoprotein B.

Structured PICO

Discussion

Implication

Cite This Study

Expression, secretion, and lipid-binding characterization of the N-terminal 17% of apolipoprotein B.

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider