Evidence map›Paper›PMID 21807994›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

In vivo molecular imaging of peripheral amyloidosis using heparin-binding peptides.

Jonathan S Wall, Tina Richey, Alan Stuckey, Robert Donnell, Sallie Macy, Emily B Martin, Angela Williams, Keiichi Higuchi, Stephen J Kennel

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Article
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  8. Article
  9. Article
  10. Review
  11. Mechanistic insights into the pH-dependent membrane peptide ATRAM.Journal of controlled release : official journal of the Controlled Release Society · 2019
    Article
  12. Article
  13. Article
  14. Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018
    Review
  15. Article
  16. Heparan Sulfate Proteoglycans as Relays of Neuroinflammation.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. Preliminary characterization of a novel peptide-Fc-fusion construct for targeting amyloid deposits.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2017
    Article
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

9 authors at 3 institutions in 2 countries.

Jonathan S WallDepartment of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, USA. jwall@utmck.edu
Tina Richey
Alan Stuckey
Robert Donnell
Sallie Macy
Emily B Martin
Angela Williams
Keiichi Higuchi
Stephen J Kennel
University of Tennessee at Knoxville · USUniversity of Tennessee System · USShinshu University · JP

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

Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, ALκ, ALλ, transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ.

Indexed as

PeptidesAmino Acid SequenceAmyloidosisAnimalsAutoradiographyHeparinHumansImmunohistochemistryIodine RadioisotopesLiverMiceMolecular ImagingMolecular Sequence DataProtein BindingSpleenStaining and LabelingHeparinIodine RadioisotopesPeptides

Identifiers

PMID21807994
PMCPMC3161606
OpenAlexW2127166575

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.