Evidence map›Paper›PMID 21515415›Full record

ArticleBiochimica et biophysica acta2011

Impact of site-specific N-glycosylation on cellular secretion, activity and specific activity of the plasma phospholipid transfer protein.

John J Albers, Joseph R Day, Gertrud Wolfbauer, Hal Kennedy, Simona Vuletic, Marian C Cheung

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 31% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Structural basis of the lipid transfer mechanism of phospholipid transfer protein (PLTP).Biochimica et biophysica acta. Molecular and cell biology of lipids · 2018
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

John J AlbersNorthwest Lipid Metrobolism and Diabetes Research Laboratories, Division of Metabolism, Endocrinology, and Nutrition, Department of Medicine, University of Washington, Seattle, Washington 98109-4517, USA. jja@uw.edu
Joseph R Day
Gertrud Wolfbauer
Hal Kennedy
Simona Vuletic
Marian C Cheung
University of Washington · US

Funding

Serum Amyloid and Inflammation in AtherogenesisP01HL030086 · NHLBI · UNIVERSITY OF WASHINGTON · PI HEINECKE, JAY W · 1985 to 2009
$14.7M
NHLBI NIH HHS HL030086NHLBI NIH HHS P01 HL030086
6 · The paper itself

Abstract

The plasma phospholipid transfer protein (PLTP) plays a key role in lipid and lipoprotein metabolism. It has six potential N-glycosylation sites. To study the impact of these sites on PLTP secretion and activity, six variants containing serine to alanine point mutations were prepared by site-directed mutagenesis and expressed in Chinese hamster ovary Flp-In cells. The apparent size of each of the six PLTP mutants was slightly less than that of wild type by Western blot, indicating that all six sites are glycosylated or utilized. The size of the carbohydrate at each N-glycosylation site ranged from 3.14 to 4.2kDa. The effect of site-specific N-glycosylation removal on PLTP secretion varied from a modest enhancement (15% and 60%), or essentially no effect, to a reduction in secretion (8%, 14% and 32%). Removal of N-glycosylation at any one of the six glycosylation sites resulted in a significant 35-78% decrease in PLTP activity, and a significant 29-80% decrease in PLTP specific activity compared to wild type. These data indicate that although no single N-linked carbohydrate chain is a requirement for secretion or activity, the removal of the carbohydrate chains had a quantitative impact on cellular secretion of PLTP and its phospholipid transfer activity.

Indexed as

MutationAlanineAmino Acid SubstitutionAnimalsBinding SitesBlotting, WesternCarbohydratesCHO CellsCricetinaeCricetulusCulture Media, ConditionedElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayGlycosylationHumansMutagenesis, Site-DirectedAlanineCarbohydratesCulture Media, ConditionedMutant ProteinsPhospholipid Transfer ProteinsPLTP protein, humanSerine

Identifiers

PMID21515415
PMCPMC3112057
OpenAlexW2076619726

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.