Evidence map›Paper›PMID 20592285›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2010

Placental leucine aminopeptidase efficiently generates mature antigenic peptides in vitro but in patterns distinct from endoplasmic reticulum aminopeptidase 1.

Dimitra Georgiadou, Arron Hearn, Irini Evnouchidou, Angeliki Chroni, Leondios Leondiadis, Ian A York, Kenneth L Rock, Efstratios Stratikos

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Is There an Interplay Between the Functional Domains of IRAP?Frontiers in cell and developmental biology · 2020
    Review
  4. IRAP Endosomes Control Phagosomal Maturation in Dendritic Cells.Frontiers in cell and developmental biology · 2020
    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

8 authors at 5 institutions in 4 countries.

Dimitra GeorgiadouProtein Chemistry Laboratory, Institute of Radioisotopes and Radiodiagnostic Products, National Centre for Scientific Research "Demokritos," Athens 15310, Greece.
Arron Hearn
Irini Evnouchidou
Angeliki Chroni
Leondios Leondiadis
Ian A York
Kenneth L Rock
Efstratios Stratikos
Japan Radioisotope Association · JPUniversity of Massachusetts Chan Medical School · USMichigan State University · USNational Centre of Scientific Research "Demokritos" · GRResearch Institute of Radio · RU

Funding

IMMUNOBIOLOGY OF CTL RESPONSES TO EXOGENOUS ANTIGENSR01AI043543 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ROCK, KENNETH L · 1999 to 2013
$5.1M
IMMUNOBIOLOGY OF MHC RESTRICTION OF T CELLSR37AI020248 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ROCK, KENNETH L · 1998 to 2008
$2.4M
IMMUNOLOGY OF MHC RESTRICTION OF T CELLSR01AI020248 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ROCK, KENNETH L · 1985 to 2013
$2.0M
NIAID NIH HHS R01 AI020248NIAID NIH HHS R01 AI043543NIAID NIH HHS R37 AI020248
6 · The paper itself

Abstract

All three members of the oxytocinase subfamily of M1 aminopeptidases, endoplasmic reticulum aminopeptidase 1 (ERAP1), ERAP2, and placental leucine aminopeptidase (PLAP), also known as insulin-regulated aminopeptidase, have been implicated in the generation of MHC class I-presented peptides. ERAP1 and 2 trim peptides in the endoplasmic reticulum for direct presentation, whereas PLAP has been recently implicated in cross-presentation. The best characterized member of the family, ERAP1, has unique enzymatic properties that fit well with its role in Ag processing. ERAP1 can trim a large variety of long peptide sequences and efficiently accumulate mature antigenic epitopes of 8-9 aa long. In this study, we evaluate the ability of PLAP to process antigenic peptide precursors in vitro and compare it with ERAP1. We find that, similar to ERAP1, PLAP can trim a variety of long peptide sequences efficiently and, in most cases, accumulates appreciable amounts of correct length mature antigenic epitope. Again, similar to ERAP1, PLAP continued trimming some of the epitopes tested and accumulated smaller products effectively destroying the epitope. However, the intermediate accumulation properties of ERAP1 and PLAP are distinct and epitope dependent, suggesting that these two enzymes may impose different selective pressures on epitope generation. Overall, although PLAP has the necessary enzymatic properties to participate in generating or destroying MHC class I-presented peptides, its trimming behavior is distinct from that of ERAP1, something that supports a separate role for these two enzymes in Ag processing.

Indexed as

Amino Acid SequenceAminopeptidasesAntigen PresentationAntigensCell LineCystinyl AminopeptidaseEpitopesHistocompatibility Antigens Class IHumansIntracellular FluidMinor Histocompatibility AntigensMolecular Sequence DataPeptide BiosynthesisPeptidesPregnancy ProteinsProtein PrecursorsAminopeptidasesAntigensCystinyl AminopeptidaseEpitopesERAP1 protein, humanHistocompatibility Antigens Class Ileucyl-cystinyl aminopeptidaseMinor Histocompatibility AntigensPeptidesPregnancy ProteinsProtein PrecursorsRecombinant Proteins

Identifiers

PMID20592285
PMCPMC2910840
OpenAlexW1924947656

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.