Evidence map›Paper›PMID 17609251›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2007

Identification of two GTP-independent alternatively spliced forms of tissue transglutaminase in human leukocytes, vascular smooth muscle, and endothelial cells.

Thung-S Lai, Yusha Liu, Weidong Li, Charles S Greenberg

Open access · greenAbstract readComparative StudyValidation Study
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Identification of a FXIIIA variant in human neuroblastoma cell lines.International journal of biochemistry and molecular biology · 2013
    Article
  18. Manipulating the microvasculature and its microenvironment.Critical reviews in biomedical engineering · 2013
    Review
  19. Article
  20. Regulation of the activities of the mammalian transglutaminase family of enzymes.Protein science : a publication of the Protein Society · 2012
    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

4 authors at 2 institutions in 1 country.

Thung-S LaiDepartment of Medicine, Duke University Medical Center, Durham, NC 27710, USA.
Yusha Liu
Weidong Li
Charles S Greenberg
Duke University · USDuke Medical Center · US

Funding

Tissue Transglutaminase and Vascular RepairR01HL072184 · NHLBI · DUKE UNIVERSITY · PI GREENBERG, CHARLES S · 2003 to 2006
$1.4M
Tissue Transglutaminase in Neurologic InjuryR21NS050541 · NINDS · DUKE UNIVERSITY · PI LAI, THUNG-SHEN · 2006 to 2007
$345k
NHLBI NIH HHS HL072184NHLBI NIH HHS R01 HL072184NINDS NIH HHS NS050541NINDS NIH HHS R21 NS050541
6 · The paper itself

Abstract

Tissue transglutaminase (tTG) is a multifunctional enzyme with transglutaminase crosslinking (TGase), GTP binding, and hydrolysis activities that play a role in many different disorders. We identified, characterized, and investigated the function and stability of two alternatively spliced forms of tTG using biochemical, cellular, and molecular biological approaches. Using a human aortic vascular smooth muscle cells (VSMC) cDNA library, we identified two cDNAs encoding C-terminal truncated forms, tTG(V1) and tTG(V2). tTG(V1,2) mRNAs were synthesized by a rare splicing event using alternate splice sites within exons 12 and 13 of the tTG gene, respectively. Quantitative PCR and immunoblotting demonstrated that there was unique expression and localization of tTG(V1,2) compared with tTG in human umbilical vein endothelial cells (HUVECs), VSMC, and leukocytes. The loss of C-terminal 52 amino acid residues (AAs) in tTG(V1,2) altered GTP binding, enhanced GTP hydrolysis, rendered the variants insensitive to GTP inhibition, and resulted in <10% residual Ca(+2)-dependent TGase activity. Transfection in HEK293 demonstrated a 28- and 5-fold reduction in the expression of tTG(V1) and tTG(V2), respectively, demonstrating that the C-terminal GTP-binding domain is important in stabilizing and promoting the half-life of tTG. The altered affinity for GTP allowed tTG(V1,2) to exhibit enhanced TGase activity when there is a transient increase in Ca(+2) levels. The abundance of tTG(V1,2) and its distinct intracellular expression patterns in human vascular cells and leukocytes indicate these isoforms likely have unique physiological functions.

Indexed as

Alternative SplicingAmino Acid SequenceAortaCell LineEndothelial CellsGene Expression Regulation, EnzymologicGTP-Binding ProteinsGuanosine TriphosphateHL-60 CellsHumansIntracellular FluidIsoenzymesLeukocytesMolecular Sequence DataMuscle, Smooth, VascularProtein Glutamine gamma Glutamyltransferase 2GTP-Binding ProteinsGuanosine TriphosphateIsoenzymesProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID17609251
PMCPMC2157556
OpenAlexW2100321916

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.