Evidence map›Paper›PMID 32975399›Full record

ArticleACS chemical biology2020

Generation and Characterization of Anti-Glucosepane Antibodies Enabling Direct Detection of Glucosepane in Retinal Tissue.

Matthew D Streeter, Sheldon Rowan, Jason Ray, David M McDonald, Jonathan Volkin, Jonathan Clark, Allen Taylor, David A Spiegel

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. The chemical language of protein glycation.Nature chemical biology · 2025
    Review
  2. Review
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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 3 institutions in 2 countries.

Matthew D StreeterDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06511, United States.
Sheldon RowanTufts University, JM-USDA Human Nutrition Research Center on Aging, 711 Washington Street, Boston, Massachusetts 02111, United States.
Jason RayDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06511, United States.
David M McDonaldDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06511, United States.
Jonathan VolkinTufts University, JM-USDA Human Nutrition Research Center on Aging, 711 Washington Street, Boston, Massachusetts 02111, United States.
Jonathan ClarkBiological Chemistry Laboratory, Babraham Institute, Cambridge CB21 3AT, United Kingdom.
Allen TaylorTufts University, JM-USDA Human Nutrition Research Center on Aging, 711 Washington Street, Boston, Massachusetts 02111, United States.
David A SpiegelDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06511, United States.ORCID 0000-0002-1102-8012
Yale University · USTufts University · USBabraham Institute · GB

Funding

Predoc Training at the Interface Chemistry and BiologyT32GM067543 · NIGMS · YALE UNIVERSITY · PI CRAWFORD, JASON MICHAEL · 2003 to 2022
$7.4M
NIGMS NIH HHS T32 GM067543
6 · The paper itself

Abstract

Although there is ample evidence that the advanced glycation end-product (AGE) glucosepane contributes to age-related morbidities and diabetic complications, the impact of glucosepane modifications on proteins has not been extensively explored due to the lack of sufficient analytical tools. Here, we report the development of the first polyclonal anti-glucosepane antibodies using a synthetic immunogen that contains the core bicyclic ring structure of glucosepane. We investigate the recognition properties of these antibodies through ELISAs involving an array of synthetic AGE derivatives and determine them to be both high-affinity and selective in binding glucosepane. We then employ these antibodies to image glucosepane in aging mouse retinae via immunohistochemistry. Our studies demonstrate for the first time accumulation of glucosepane within the retinal pigment epithelium, Bruch's membrane, and choroid: all regions of the eye impacted by age-related macular degeneration. Co-localization studies further suggest that glucosepane colocalizes with lipofuscin, which has previously been associated with lysosomal dysfunction and has been implicated in the development of age-related macular degeneration, among other diseases. We believe that the anti-glucosepane antibodies described in this study will prove highly useful for examining the role of glycation in human health and disease.

Indexed as

AgingAnimalsAntibodiesBruch MembraneFemaleGlycation End Products, AdvancedImmunohistochemistryMice, Inbred C57BLPigment Epithelium of EyeRabbitsRetinaAntibodiesglucosepaneGlycation End Products, Advanced

Identifiers

PMID32975399
PMCPMC10625846
OpenAlexW3088935245

What OpenQuestion holds

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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.