Evidence map›Paper›PMID 21757696›Full record

ArticleThe Journal of biological chemistry2011

Reactivity of the N-terminal region of fibronectin protein to transglutaminase 2 and factor XIIIA.

Brian R Hoffmann, Douglas S Annis, Deane F Mosher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Serotonylation: Serotonin Signaling and Epigenetics.Frontiers in molecular neuroscience · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Activity-regulating structural changes and autoantibody epitopes in transglutaminase 2 assessed by hydrogen/deuterium exchange.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Article
  12. Transglutaminase 2-mediated serotonylation in pulmonary hypertension.American journal of physiology. Lung cellular and molecular physiology · 2014
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Dynamic structure of plasma fibronectin.Critical reviews in biochemistry and molecular biology
    Review
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.

Brian R HoffmannDepartment of Biomolecular Chemistry and Medicine, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Douglas S Annis
Deane F Mosher
University of Wisconsin–Madison · US

Funding

RESEARCH TRAINING IN HEMATOLOGYT32HL007899 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Jane Ellen Churpek · 1998 to 2026
$8.2M
STUDIES OF FIBRONECTIN AND RELATED GLYCOPROTEINSR01HL021644 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MOSHER, DEANE FREMONT · 1985 to 2010
$3.2M
MALDI TOF/TOF Mass SpectrometerS10RR024601 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI GELLMAN, SAMUEL H. · 2008 to 2008
$376k
NCRR NIH HHS S10 RR024601NHLBI NIH HHS R01 HL021644NHLBI NIH HHS R01HL021644NHLBI NIH HHS T32 HL007899NHLBI NIH HHS T32-HL007899PHS HHS NCRR 1S10RR024601-1
6 · The paper itself

Abstract

Transglutaminase 2 (TG2) is secreted by a non-classical pathway into the extracellular space, where it has several activities pertinent to fibronectin (FN), including binding to the gelatin-binding domain of FN and acting as an integrin co-receptor. Glutamines in the N-terminal tail of FN are known to be susceptible to transamidation by both TG2 and activated blood coagulation factor XIII (FXIIIa). We used immunoblotting, limited proteolysis, and mass spectrometry to localize glutamines within FN that are subject to TG2-catalyzed incorporation of dansylcadaverine in comparison to residues modified by FXIIIa. Such analysis of plasma FN indicated that Gln-3, Gln-7, and Gln-9 in the N-terminal tail and Gln-246 of the linker between fifth and sixth type I modules ((5)F1 and (6)F1) are transamidated by both enzymes. Only minor incorporation of dansylcadaverine was detected elsewhere. Labeling of C-terminally truncated FN constructs revealed efficient TG2- or FXIIIa-catalyzed dansylcadaverine incorporation into the N-terminal residues of constructs as small as the 29-kDa fragment that includes (1-5)F1 and lacks modules from the adjacent gelatin-binding domain. However, when only (1-3)F1 were present, dansylcadaverine incorporation into the N-terminal residues of FN was lost and instead was in the enzymes, near the active site of TG2 and terminal domains of FXIIIa. Thus, these results demonstrate that FXIIIa and TG2 act similarly on glutamines at either end of (1-5)F1 and transamidation specificity of both enzymes is achieved through interactions with the intact 29K fragment.

Indexed as

Catalytic DomainFactor XIIIaFibronectinsGlutamineGTP-Binding ProteinsHumansProtein Glutamine gamma Glutamyltransferase 2Protein Processing, Post-TranslationalProtein Structure, TertiaryTransglutaminasesFactor XIIIaFibronectinsGlutamineGTP-Binding ProteinsProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID21757696
PMCPMC3173148
OpenAlexW1990178542

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.