Evidence map›Paper›PMID 22128163›Full record

ArticleThe Journal of biological chemistry2012

ApoB-100-containing lipoproteins are major carriers of 3-iodothyronamine in circulation.

Gouriprassana Roy, Ekaterina Placzek, Thomas S Scanlan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 3-Iodothyronamine and Derivatives: New Allies Against Metabolic Syndrome?International journal of molecular sciences · 2020
    Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Thyroid hormone regulation of metabolism.Physiological reviews · 2014
    Review
  12. Review
  13. 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

3 authors at 1 institution in 1 country.

Gouriprassana RoyDepartment of Physiology and Pharmacology, Oregon Health and Science University, Portland, Oregon 97239-3098, USA.
Ekaterina Placzek
Thomas S Scanlan
Oregon Health & Science University · US

Funding

Understanding the origins of rapid recurrence of pancreatic cancer after resectionP30CA069533 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI Luiz Eduardo Bertassoni · 1997 to 2026
$60.5M
Proteomics CoreP30EY010572 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI TED S ACOTT · 1995 to 2026
$19.4M
Thyroid Hormone ActionR01DK052798 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SCANLAN, THOMAS STERLING · 1997 to 2020
$5.7M
Chemical Biology Studies of 3-Iodothyronamine and Related Thyroid Hormone MetabolR01DK091539 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SCANLAN, THOMAS STERLING · 2012 to 2015
$1.3M
Thyroid Hormone ActionR56DK052798 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SCANLAN, THOMAS STERLING · 2009 to 2021
$581k
NCI NIH HHS 5P30CA-069533NCI NIH HHS P30 CA069533NEI NIH HHS 5P30EY-010572NEI NIH HHS P30 EY010572NIDDK NIH HHS DK-52798NIDDK NIH HHS R01 DK052798NIDDK NIH HHS R01 DK091539NIDDK NIH HHS R56 DK052798
6 · The paper itself

Abstract

3-Iodothyronamine (T(1)AM) is a biogenic amine derivative of thyroid hormone present in tissue and blood of vertebrates. Approximately 99% of the circulating thyroid hormones are bound to plasma proteins, including three major thyroid hormone-binding proteins, and the question arises as to whether circulating T(1)AM is also bound to serum factors. We report here that T(1)AM is largely bound to a single protein component of human serum. Using T(1)AM-affinity chromatography, we isolated this protein, and sequence analysis identified it as apolipoprotein B-100 (apoB-100), the protein component of several low density lipoprotein particles. Consistent with this finding, we demonstrate that >90% of specifically bound T(1)AM in human serum resides in the apoB-100-containing low density lipoprotein fraction. T(1)AM reversibly binds to apoB-100-containing lipoprotein particles with an equilibrium dissociation constant (K(D)) of 17 nm and a T(1)AM/apoB-100 stoichiometry of 1:1. Competition binding assays demonstrate that this binding site is highly selective for T(1)AM. Intracellular T(1)AM uptake is significantly enhanced by apoB-100-containing lipoprotein particles. Modest enhancements to apoB-100 cellular uptake and secretion by T(1)AM were observed; however, multidose T(1)AM treatment did not affect lipid or lipoprotein inventory in vivo. Thus, it appears that apoB-100 serves as a carrier of circulating T(1)AM and affords a novel mechanism by which T(1)AM gains entry to cells.

Indexed as

AnimalsApolipoprotein B-100Carrier ProteinsHep G2 CellsHumansProtein BindingRatsThyronines3-iodothyronamineApolipoprotein B-100Carrier ProteinsThyronines

Identifiers

PMID22128163
PMCPMC3265861
OpenAlexW1994735484

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.