Evidence map›Paper›PMID 31870425›Full record

ArticleBMC nephrology2019

Typing of hereditary renal amyloidosis presenting with isolated glomerular amyloid deposition.

Danyang Li, Dan Liu, Hui Xu, Xiao-Juan Yu, Fu-de Zhou, Ming-Hui Zhao, Su-Xia Wang

Open access · goldAbstract readCase Reports
In one paragraph

Article in BMC nephrology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 3 countries.

Danyang LiLaboratory of Electron Microscopy, Pathological Center, Peking University First Hospital, Beijing, 100034, People's Republic of China.
Dan LiuProteomics Laboratory, Medical and Healthy Analytical Center, Peking University Health Science Center, Beijing, 100191, People's Republic of China.
Hui XuLaboratory of Electron Microscopy, Pathological Center, Peking University First Hospital, Beijing, 100034, People's Republic of China.
Xiao-Juan YuRenal Division, Department of Medicine, Peking University First Hospital; Institute of Nephrology, Peking University; Key Laboratory of Renal Disease, Ministry of Health of China; Key Laboratory of CKD Prevention and Treatment, Ministry of Education of China, Beijing, 100034, People's Republic of China.
Fu-de ZhouRenal Division, Department of Medicine, Peking University First Hospital; Institute of Nephrology, Peking University; Key Laboratory of Renal Disease, Ministry of Health of China; Key Laboratory of CKD Prevention and Treatment, Ministry of Education of China, Beijing, 100034, People's Republic of China.
Ming-Hui ZhaoRenal Division, Department of Medicine, Peking University First Hospital; Institute of Nephrology, Peking University; Key Laboratory of Renal Disease, Ministry of Health of China; Key Laboratory of CKD Prevention and Treatment, Ministry of Education of China, Beijing, 100034, People's Republic of China.
Su-Xia WangLaboratory of Electron Microscopy, Pathological Center, Peking University First Hospital, Beijing, 100034, People's Republic of China. suxiawang@bjmu.edu.cn.ORCID 0000-0001-7631-6464
Peking University · CNKing University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe commonly used methods for amyloid typing include immunofluorescence or immunohistochemistry (IHC), which sometimes may come with diagnostic pitfalls. Mass spectrometry (MS)-based proteomics has been recognized as a reliable technique in amyloid typing. CASE PRESENTATION: We reported two middle-aged patients who presented with proteinuria, hypertension and normal renal function, and both had a family history of renal diseases. The renal biopsies of both patients revealed renal amyloidosis with the similar pattern by massive exclusively glomerular amyloid deposition. The IHC was performed by using a panel of antibodies against the common types of systemic amyloidosis, and demonstrated co-deposition of fibrinogen Aα chain and apolipoprotein A-I in the glomerular amyloid deposits of each patient. Then the MS on amyloid deposits captured by laser microdissection (LMD/MS) and genetic study of gene mutations were investigated. The large spectra corresponding to ApoA-I in case 1, and fibrinogen Aα chain in case 2 were identified by LMD/MS respectively. Further analysis of genomic DNA mutations demonstrated a heterozygous mutation of p. Trp74Arg in ApoA-I in case 1, and a heterozygous mutation of p. Arg547GlyfsTer21 in fibrinogen Aα chain in case 2.

conclusionsThe current study revealed that IHC was not reliable for accurate amyloid typing, and that MS-based proteomics and genetic analysis were essential for typing of hereditary amyloidosis.

Indexed as

AdultAmino Acid SequenceAmyloidosisGenotyping TechniquesHumansKidney DiseasesKidney GlomerulusMaleMiddle AgedGene mutationHereditary amyloidosisImmunohistochemistryKidneyMass spectrometry

Identifiers

PMID31870425
PMCPMC6929319
OpenAlexW2995045502

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.