Evidence map›Paper›PMID 10215596›Full record

ArticleThe Biochemical journal1999

Expression of normal and truncated forms of human endoglin.

U Raab, B Velasco, P Lastres, A Letamendía, C Calés, C Langa, E Tapia, J P López-Bote, E Páez, C Bernabéu

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 40 citations in OpenAlex.

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  16. Generation of a floxed allele of the mouse Endoglin gene.Genesis (New York, N.Y. : 2000) · 2007
    Article
  17. Review
  18. 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

10 authors at 2 institutions in 1 country.

U RaabCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Velazquez 144, 28006 Madrid, Spain.
B Velasco
P Lastres
A Letamendía
C Calés
C Langa
E Tapia
J P López-Bote
E Páez
C Bernabéu
Centro de Investigaciones Biológicas Margarita Salas · ESConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoglin is a transmembrane glycoprotein 633 residues in length expressed at the surface of endothelial cells as a disulphide-linked homodimer; the specific cysteine residues involved in endoglin dimerization are unknown. Mutations in the coding region of the endoglin gene are responsible for hereditary haemorrhagic telangiectasia type 1 (HHT1), a dominantly inherited vascular disorder. Many of these mutations, if translated, would lead to truncated forms of the protein. It is therefore of interest to assess the protein expression of different truncated forms of endoglin. Infections in vitro or in vivo with recombinant vaccinia virus, as well as transient transfections with expression vectors, were used to express normal and truncated forms of endoglin. Truncated mutants could be classified into three different groups: (1) those that did not produce stable transcripts; (2) those that produced stable transcripts but did not secrete the protein; and (3) those that secreted a soluble dimeric protein. This is the first time that a recombinant truncated form of endoglin has been found to be expressed in a soluble form. Because a chimaeric construct encoding the N-terminal sequence of platelet/endothelial cell adhesion molecule (PECAM-1) antigen fused to residues Ile281-Ala658 of endoglin also yielded a dimeric surface protein, these results suggest that cysteine residues contained within the fragment Cys330-Cys412 are involved in disulphide bond formation. Infection with vaccinia recombinants encoding an HHT1 mutation did not affect the expression of the normal endoglin, and did not reveal an association of the recombinant soluble form with the transmembrane endoglin, supporting a haploinsufficiency model for HHT1.

Indexed as

Gene ExpressionAnimalsAntigens, CDCell LineCell MembraneCysteineDimerizationDisulfidesEndoglinEndothelium, VascularHumansPeptide FragmentsProtein BindingProtein IsoformsReceptors, Cell SurfaceRecombinant Fusion ProteinsAntigens, CDCysteineDisulfidesEndoglinENG protein, humanPeptide FragmentsProtein IsoformsReceptors, Cell SurfaceRecombinant Fusion ProteinsReducing AgentsRNA, MessengerTransforming Growth Factor betaVascular Cell Adhesion Molecule-1

Identifiers

PMID10215596
PMCPMC1220193
OpenAlexW2039583599

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.