Evidence map›Paper›PMID 17543577›Full record

ReviewBiochimica et biophysica acta2007

Sterol carrier protein-2: new roles in regulating lipid rafts and signaling.

Friedhelm Schroeder, Barbara P Atshaves, Avery L McIntosh, Adalberto M Gallegos, Stephen M Storey, Rebecca D Parr, John R Jefferson, Judith M Ball, Ann B Kier

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Frontiers in immunology · 2025
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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

9 authors at 2 institutions in 1 country.

Friedhelm SchroederDepartment of Physiology and Pharmacology, Texas A&M University, TVMC, College Station, TX 77843-4466, USA. Fschroeder@cvm.tamu.edu
Barbara P Atshaves
Avery L McIntosh
Adalberto M Gallegos
Stephen M Storey
Rebecca D Parr
John R Jefferson
Judith M Ball
Ann B Kier
Texas A&M University · USLuther College · US

Funding

FATTY ACID BINDING PROTEINS-LIGAND SPECIFICITYR01DK041402 · NIDDK · UNIVERSITY OF CINCINNATI · PI SCHROEDER, FRIEDHELM · 1989 to 2010
$4.4M
ASYMMETRIC DISTRIBUTION OF CHOLESTEROL IN MEMBRANESR01GM031651 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI SCHROEDER, FRIEDHELM · 1985 to 2010
$3.4M
NIDDK NIH HHS DK41402NIDDK NIH HHS R01 DK041402NIGMS NIH HHS GM31651NIGMS NIH HHS GM63236NIGMS NIH HHS R01 GM031651
6 · The paper itself

Abstract

Sterol carrier protein-2 (SCP-2) was independently discovered as a soluble protein that binds and transfers cholesterol as well as phospholipids (nonspecific lipid transfer protein, nsLTP) in vitro. Physiological functions of this protein are only now beginning to be resolved. The gene encoding SCP-2 also encodes sterol carrier protein-x (SCP-x) arising from an alternate transcription site. In vitro and in vivo SCP-x serves as a peroxisomal 3-ketoacyl-CoA thiolase in oxidation of branched-chain lipids (cholesterol to form bile acids; branched-chain fatty acid for detoxification). While peroxisomal SCP-2 facilitates branched-chain lipid oxidation, the role(s) of extraperoxisomal (up to 50% of total) are less clear. Studies using transfected fibroblasts overexpressing SCP-2 and hepatocytes from SCP-2/SCP-x gene-ablated mice reveal that SCP-2 selectively remodels the lipid composition, structure, and function of lipid rafts/caveolae. Studies of purified SCP-2 and in cells show that SCP-2 has high affinity for and selectively transfers many lipid species involved in intracellular signaling: fatty acids, fatty acyl CoAs, lysophosphatidic acid, phosphatidylinositols, and sphingolipids (sphingomyelin, ceramide, mono-di-and multi-hexosylceramides, gangliosides). SCP-2 selectively redistributes these signaling lipids between lipid rafts/caveolae and intracellular sites. These findings suggest SCP-2 serves not only in cholesterol and phospholipid transfer, but also in regulating multiple lipid signaling pathways in lipid raft/caveolae microdomains of the plasma membrane.

Indexed as

Lipid MetabolismSignal TransductionAnimalsBiological TransportCarrier ProteinsCell LineCell MembraneCholesterolFatty AcidsHumansMembrane LipidsMembrane MicrodomainsMiceModels, BiologicalSterolsStructure-Activity RelationshipCarrier ProteinsCholesterolFatty AcidsMembrane Lipidssterol carrier proteinsSterols

Identifiers

PMID17543577
PMCPMC1989133
OpenAlexW2172217058

What OpenQuestion holds

Textmetadata
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.