Evidence map›Paper›PMID 29426977›Full record

ArticleJournal of bioenergetics and biomembranes2018

Investigation of the phosphatidylserine binding properties of the lipid biosensor, Lactadherin C2 (LactC2), in different membrane environments.

Kathryn Del Vecchio, Robert V Stahelin

Open access · greenAbstract read
In one paragraph

Article in Journal of bioenergetics and biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

25 citing papers in PubMed, 49 citations in OpenAlex.

  1. The Inner Nuclear Membrane Has a Unique Lipid Signature.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
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  18. An update on genetically encoded lipid biosensors.Molecular biology of the cell · 2022
    Article
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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

2 authors at 1 institution in 1 country.

Kathryn Del VecchioDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Robert V StahelinDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA. rstaheli@purdue.edu.
University of Notre Dame · US

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
LIPID-PROTEIN INTERACTIONS IN VIRAL ASSEMBLY AND VIRUS LIKE PARTICLE FORMATIONR01AI081077 · NIAID · PURDUE UNIVERSITY · PI STAHELIN, ROBERT VIRGIL · 2009 to 2019
$3.5M
National Institute of Allergy and Infectious Diseases AI081077NIAID NIH HHS R01 AI081077NIGMS NIH HHS GM075762NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

Lipid biosensors are robust tools used in both in vitro and in vivo applications of lipid imaging and lipid detection. Lactadherin C2 (LactC2) was described in 2000 as being a potent and specific sensor for phosphatidylserine (PS) (Andersen et al. Biochemistry 39:6200-6206, 2000). PS is an anionic phospholipid enriched in the inner leaflet of the plasma membrane and has paramount roles in apoptosis, cells signaling, and autophagy. The myriad roles PS plays in membrane dynamics make monitoring PS levels and function an important endeavor. LactC2 has functioned as a tantamount PS biosensor namely in the field of cellular imaging. While PS specificity and high affinity of LactC2 for PS containing membranes has been well established, much less is known regarding LactC2 selectivity for subcellular pools of PS or PS within different membrane environments (e.g., in the presence of cholesterol). Thus, there has been a lack of studies that have compared LactC2 PS sensitivity based upon the acyl chain length and saturation or the presence of other host lipids such as cholesterol. Here, we use surface plasmon resonance as a label-free method to quantitatively assess the apparent binding affinity of LactC2 for membranes containing PS with different acyl chains, different fluidity, as well as representative lipid vesicle mimetics of cellular membranes. Results demonstrate that LactC2 is an unbiased sensor for PS, and can sensitively interact with membranes containing PS with different acyl chain saturation and interact with PS species in a cholesterol-independent manner.

Indexed as

Membranes, ArtificialAnimalsBiosensing TechniquesCattleCell MembraneDiagnostic ImagingHumansMilk ProteinsPhosphatidylserinesProtein BindingSurface Plasmon ResonanceMembranes, ArtificialMilk ProteinsPhosphatidylserinesBiosensorCholesterolLactadherinLipid-protein interactionPhosphatidylserineSurface plasmon resonance

Identifiers

PMID29426977
PMCPMC5820145
OpenAlexW2790807370

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.