Evidence map›Paper›PMID 20510729›Full record

ReviewAdvances in immunology2010

The immunological functions of saposins.

Alexandre Darmoise, Patrick Maschmeyer, Florian Winau

Open access · greenAbstract readReview
In one paragraph

Review in Advances in immunology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 58 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Alexandre DarmoiseProgram in Cellular and Molecular Medicine at Children's Hospital, Immune Disease Institute, Department of Pathology, Harvard Medical School, Boston, MA, USA.
Patrick Maschmeyer
Florian Winau
Harvard University · US

Funding

Function of stellate cells in immunity and T cell instructionR01AI083426 · NIAID · IMMUNE DISEASE INSTITUTE, INC. · PI WINAU, FLORIAN · 2010 to 2014
$2.5M
NIAID NIH HHS R01 AI083426
6 · The paper itself

Abstract

Saposins or sphingolipid activator proteins (SAPs) are small, nonenzymatic glycoproteins that are ubiquitously present in lysosomes. SAPs comprise the five molecules saposins A-D and the GM2 activator protein. Saposins are essential for sphingolipid degradation and membrane digestion. On the one hand, they bind the respective hydrolases required to catabolize sphingolipid molecules; on the other hand, saposins can interact with intralysosomal membrane structures to render lipids accessible to their degrading enzymes. Thus, saposins bridge the physicochemical gap between lipid substrate and hydrophilic hydrolases. Accordingly, defects in saposin function can lead to lysosomal lipid accumulation. In addition to their specific functions in sphingolipid metabolism, saposins have membrane-perturbing properties. At the low pH of lysosomes, saposins get protonated and exhibit a high binding affinity for anionic phospholipids. Based on their universal principle to interact with membrane bilayers, we present the immunological functions of saposins with regard to lipid antigen presentation to CD1-restricted T cells, processing of apoptotic bodies for antigen delivery and cross-priming, as well as their potential antimicrobial impact.

Indexed as

Antigen PresentationAntigens, CD1dEndosomesGlucosylceramidaseGlycoproteinsLipid MetabolismLymphocyte ActivationLysosomesNatural Killer T-CellsSaposinsSphingolipidsAntigens, CD1dGlucosylceramidaseGlycoproteinsSaposinsSphingolipids

Identifiers

PMID20510729
PMCPMC4030616
OpenAlexW1539628793

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.