Evidence map›Paper›PMID 17484767›Full record

ArticleImmunology2007

Synthesis of beta(2)-microglobulin-free, disulphide-linked HLA-G5 homodimers in human placental villous cytotrophoblast cells.

Pedro J Morales, Judith L Pace, Jeralyn Sue Platt, Daudi K Langat, Joan S Hunt

Open access · bronzeAbstract read
In one paragraph

Article in Immunology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 19% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.

  1. Pooled it
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  20. Some basic aspects of HLA-G biology.Journal of immunology research · 2014
    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

5 authors at 1 institution in 1 country.

Pedro J MoralesDepartment of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, KS 66160-7400, USA.
Judith L Pace
Jeralyn Sue Platt
Daudi K Langat
Joan S Hunt
University of Kansas Medical Center · US

Funding

UNDERSTANDING THE ROLE OF SMALL RNAS IN ARABIDOPSIS POLLEN DEVELOPMENTP20RR016475 · NCRR · UNIVERSITY OF KANSAS MEDICAL CENTER · PI AZUMA, MIZUKI · 2001 to 2011
$38.1M
UTERINE VASCULAR CHANGES &ANGIOGENESIS DURING IMPLANTATIONU54HD033994 · NICHD · UNIVERSITY OF KANSAS MEDICAL CENTER · PI TERRANOVA, PAUL FRANK · 2001 to 2005
$5.6M
TROPHOBLAST MDR EFFLUX SYSTEM AND FETAL PROTECTIONP01HD039878 · NICHD · UNIVERSITY OF KANSAS MEDICAL CENTER · PI SOARES, MICHAEL J · 2002 to 2006
$4.7M
Motor Map Plasticity in Constraint Therapy for StrokeR01HD040984 · NICHD · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI WITTENBERG, GEORGE · 2002 to 2005
$1.9M
NCRR NIH HHS P20 RR016475NCRR NIH HHS P20 RR16475NICHD NIH HHS P01 HD039878NICHD NIH HHS P01 HD39878NICHD NIH HHS P01 HD40984NICHD NIH HHS R01 HD040984NICHD NIH HHS U54 HD033994NICHD NIH HHS U54 HD33994
6 · The paper itself

Abstract

Human leucocyte antigen-G (HLA-G) is a natural immunosuppressant produced in human placentas that binds differently to the inhibitory leucocyte immunoglobulin-like receptors LILRB1 (ILT2) and LILRB2 (ILT4) according to its biochemical structure. To predict the binding functions of the HLA-G5 soluble isoform synthesized in placental villous cytotrophoblast (vCTB) cells, we investigated structural features of this protein. Biochemical and immunological studies showed that vCTB cell HLA-G5 heavy (H)-chain proteins are disulphide-bonded homodimers unassociated with beta(2)-microglobulin (beta2m) light-chain proteins. Although comparatively low levels of beta2m messenger RNA (mRNA) were identified by real-time reverse transcription-polymerase chain reaction, immunoprecipitation studies failed to detect beta2m protein even when specific mRNA was doubled by transduction of a lentivirus-beta2m complementary DNA into vCTB cells. No abnormalities were identified in the translational start codon of vCTB cell beta2m mRNA and differentiation into syncytium did not promote beta2m synthesis. The failure of vCTB cells to exhibit beta2m in vitro was paralleled by a lack of detectable beta2m in vCTB cells in vivo. Lack of the beta2m protein could be the result of low levels of beta2m transcripts or of as yet unidentified translational defects. Experiments with recombinant ectodomains of LILRB indicate that beta2m-free HLA-G binds strongly to LILRB2, a receptor that is expressed by macrophages. This potentially immunosuppressive cell type is abundant in the pregnant uterus. Thus, our findings are consistent with the postulate that the natural beta2m-free homodimeric form of HLA-G5 synthesized in primary vCTB cells could comprise a particularly effective tolerogenic molecule at the maternal-fetal interface.

Indexed as

beta 2-MicroglobulinCells, CulturedDisulfidesEpidermal Growth FactorHistocompatibility Antigens Class IHLA AntigensHLA-G AntigensHumansImmune ToleranceLentivirusPlacentaProtein BiosynthesisRNA, MessengerTransduction, GeneticTrophoblastsbeta 2-MicroglobulinDisulfidesEpidermal Growth FactorHistocompatibility Antigens Class IHLA AntigensHLA-G AntigensRNA, Messenger

Identifiers

PMID17484767
PMCPMC2266009
OpenAlexW1994937984

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.