Evidence map›Paper›PMID 23707811›Full record

ArticleBiochemical and biophysical research communications2013

Peptide p5 binds both heparinase-sensitive glycosaminoglycans and fibrils in patient-derived AL amyloid extracts.

Emily B Martin, Angela Williams, Eric Heidel, Sallie Macy, Stephen J Kennel, Jonathan S Wall

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 19 citations in OpenAlex.

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  10. Probing the structural requirements of polybasic peptides for effective and specific amyloid reactivity.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2017
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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

6 authors at 2 institutions in 1 country.

Emily B MartinDepartment of Medicine, University of Tennessee Graduate School of Medicine, 1924 Alcoa Highway, Knoxville, TN 37922, USA.
Angela Williams
Eric Heidel
Sallie Macy
Stephen J Kennel
Jonathan S Wall
Alcoa (United States) · USUniversity of Tennessee at Knoxville · US

Funding

Preclinical Diagnostic Imaging of AmyloidR01DK079984 · NIDDK · UNIVERSITY OF TENNESSEE KNOXVILLE · PI WALL, JONATHAN S · 2009 to 2016
$3.4M
NIDDK NIH HHS R01 DK079984NIDDK NIH HHS R01DK079984
6 · The paper itself

Abstract

In previously published work, we have described heparin-binding synthetic peptides that preferentially recognize amyloid deposits in a mouse model of reactive systemic (AA) amyloidosis and can be imaged by using positron and single photon emission tomographic imaging. We wanted to extend these findings to the most common form of visceral amyloidosis, namely light chain (AL); however, there are no robust experimental animal models of AL amyloidosis. To further define the binding of the lead peptide, p5, to AL amyloid, we characterized the reactivity in vitro of p5 with in situ and patient-derived AL amyloid extracts which contain both hypersulfated heparan sulfate proteoglycans as well as amyloid fibrils. Histochemical staining demonstrated that the peptide specifically localized with tissue-associated AL amyloid deposits. Although we anticipated that p5 would undergo electrostatic interactions with the amyloid-associated glycosaminoglycans expressing heparin-like side chains, no significant correlation between peptide binding and glycosaminoglycan content within amyloid extracts was observed. In contrast, following heparinase I treatment, although overall binding was reduced, a positive correlation between peptide binding and amyloid fibril content became evident. This interaction was further confirmed using synthetic light chain fibrils that contain no carbohydrates. These data suggest that p5 can bind to both the sulfated glycosaminoglycans and protein fibril components of AL amyloid. Understanding these complex electrostatic interactions will aid in the optimization of synthetic peptides for use as amyloid imaging agents and potentially as therapeutics for the treatment of amyloid diseases.

Indexed as

Alcian BlueAmyloidAmyloidosisBenzothiazolesCarbohydratesGlycosaminoglycansHeparinHeparin LyaseHumansPeptidesProtein BindingStatic ElectricityThiazolesAlcian BlueAmyloidamyloid protein ALBenzothiazolesCarbohydratesGlycosaminoglycansHeparinHeparin LyasePeptidesThiazolesthioflavin T

Identifiers

PMID23707811
PMCPMC3735914
OpenAlexW1970703718

What OpenQuestion holds

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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.