Evidence map›Paper›PMID 25102446›Full record

ArticlePeptides2014

Dynamic PET and SPECT imaging with radioiodinated, amyloid-reactive peptide p5 in mice: a positive role for peptide dehalogenation.

Emily B Martin, Stephen J Kennel, Tina Richey, Craig Wooliver, Dustin Osborne, Angela Williams, Alan Stuckey, Jonathan S Wall

Open access · greenAbstract read
In one paragraph

Article in Peptides, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Mechanistic insights into the pH-dependent membrane peptide ATRAM.Journal of controlled release : official journal of the Controlled Release Society · 2019
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Indium-based and iodine-based labeling of HPMA copolymer-epirubicin conjugates: Impact of structure on the in vivo fate.Journal of controlled release : official journal of the Controlled Release Society · 2016
    Article
  13. Article
  14. The pattern recognition reagents RAGE VC1 and peptide p5 share common binding sites and exhibit specific reactivity with AA amyloid in mice.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2016
    Article
  15. 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

8 authors at 3 institutions in 1 country.

Emily B MartinDepartment of Medicine, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States. Electronic address: emarti15@vols.utk.edu.
Stephen J KennelDepartment of Medicine, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States; Department of Radiology, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States. Electronic address: skennel@utmck.edu.
Tina RicheyDepartment of Medicine, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States. Electronic address: trichey@utmck.edu.
Craig WooliverDepartment of Medicine, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States. Electronic address: dwooliver@utmck.edu.
Dustin OsborneDepartment of Radiology, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States. Electronic address: dosborne@utmck.edu.
Angela WilliamsDepartment of Medicine, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States. Electronic address: awilliams@utmck.edu.
Alan StuckeyDepartment of Radiology, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States. Electronic address: astuckey@utmck.edu.
Jonathan S WallDepartment of Medicine, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States; Department of Radiology, University of Tennessee Medical Center, 1924 Alcoa Highway, Knoxville, TN 37920, United States. Electronic address: jwall@utmck.edu.
Alcoa (United States) · USUniversity of Tennessee Medical Center · 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

Dynamic molecular imaging provides bio-kinetic data that is used to characterize novel radiolabeled tracers for the detection of disease. Amyloidosis is a rare protein misfolding disease that can affect many organs. It is characterized by extracellular deposits composed principally of fibrillar proteins and hypersulfated proteoglycans. We have previously described a peptide, p5, which binds preferentially to amyloid deposits in a murine model of reactive (AA) amyloidosis. We have determined the whole body distribution of amyloid by molecular imaging techniques using radioiodinated p5. The loss of radioiodide from imaging probes due to enzymatic reaction has plagued the use of radioiodinated peptides and antibodies. Therefore, we studied iodine-124-labeled p5 by using dynamic PET imaging of both amyloid-laden and healthy mice to assess the rates of amyloid binding, the relevance of dehalogenation and the fate of the radiolabeled peptide. Rates of blood pool clearance, tissue accumulation and dehalogenation of the peptide were estimated from the images. Comparisons of these properties between the amyloid-laden and healthy mice provided kinetic profiles whose differences may prove to be indicative of the disease state. Additionally, we performed longitudinal SPECT/CT imaging with iodine-125-labeled p5 up to 72h post injection to determine the stability of the radioiodinated peptide when bound to the extracellular amyloid. Our data show that amyloid-associated peptide, in contrast to the unbound peptide, is resistant to dehalogenation resulting in enhanced amyloid-specific imaging. These data further support the utility of this peptide for detecting amyloidosis and monitoring potential therapeutic strategies in patients.

Indexed as

Molecular ImagingPositron-Emission TomographyTomography, Emission-Computed, Single-PhotonAmyloidAnimalsHalogenationIodine RadioisotopesMiceMice, Inbred BALB CPeptide FragmentsAmyloidIodine RadioisotopesPeptide FragmentsAmyloid imagingDehalogenationDynamic PET imagingPeptide radiotracerSPECT

Identifiers

PMID25102446
PMCPMC4169731
OpenAlexW2094077828

What OpenQuestion holds

Textmetadata
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.