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March 1, 1997Journal of Biological ChemistryOpen Access

In Vitro Reconstitution of Assembly of Apolipoprotein B48-containing Lipoproteins

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Key result

Co-translational lipid synthesis favored the assembly of apoB48 with newly synthesized lipids and its translocation into the microsomal lumen, even without microsomal triacylglycerol transfer protein.

Population

In vitro model using rabbit reticulocyte lysate and microsomes derived from rat liver or dog pancreas for…

Comparison

Addition of precursors of glycerolipids to… vs Translation without active co-translational…

Design

Preclinical

Authors

ARAntonio E. RusiñolEast Tennessee State UniversityHJHaris JamilUniversity of SussexJVJean E. VanceUniversity of Alberta

Discussion

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Implication

In vitro co-translational lipid synthesis may aid apoB-lipoprotein assembly; leaves open in vivo relevance for hepatic VLDL production.

Structured PICO

P
Population
In vitro model using rabbit reticulocyte lysate and microsomes derived from rat liver or dog pancreas for translation of human apolipoprotein B48 (apoB48) and apoB15.
I
Intervention
Addition of precursors of glycerolipids (acylcoenzyme A, glycerol 3-phosphate, and CDP-choline) to reconstitute lipid synthesis before, during, or after translation.
C
Comparator
Translation without active co-translational lipid synthesis, or comparison between apoB48 and apoB15.
O
Outcome
Assembly and translocation of apoB48 and apoB15 into the microsomal lumen.surrogate

This in vitro study demonstrates that active co-translational lipid synthesis promotes the assembly and translocation of apoB48-containing lipoproteins, a process that can occur independently of microsomal triacylglycerol transfer protein activity.

Cite This Study

Rusiñol et al. (1997) studied this question. Co-translational lipid synthesis vs. Absence of co-translational lipid synthesis was evaluated on Translocation and assembly of apoB48. Co-translational lipid synthesis favored the assembly of apoB48 with newly synthesized lipids and its translocation into the microsomal lumen, even without microsomal triacylglycerol transfer protein.

synapsesocial.com/papers/6a6cf03d75498292b707ae6bhttps://doi.org/10.1074/jbc.272.12.8019
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Carboxyl-terminal truncation impairs lipid recruitment by apolipoprotein B100 but does not affect secretion of the truncated apolipoprotein B-containing lipoproteins.1994 · 84 citations
  2. 2Microsomal triglyceride transfer protein, the abetalipoproteinemia gene product, mediates the secretion of apolipoprotein B-containing lipoproteins from heterologous cells.1994 · 157 citations
  3. 3Translocation of apolipoprotein B across the endoplasmic reticulum is blocked in abetalipoproteinemia.1996 · 63 citations
  4. 4Proteolysis and lipid-facilitated translocation are distinct but competitive processes that regulate secretion of apolipoprotein B in Hep G2 cells.1993 · 138 citations
  5. 5Oleate stimulates secretion of apolipoprotein B-containing lipoproteins from Hep G2 cells by inhibiting early intracellular degradation of apolipoprotein B.1991 · 420 citations