Evidence map›Paper›PMID 18653767›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2008

Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis.

Manuel A Pallero, Carrie A Elzie, Jiping Chen, Deane F Mosher, Joanne E Murphy-Ullrich

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.6field-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

49 citing papers in PubMed, 83 citations in OpenAlex.

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  15. Article
  16. Thrombospondin 1 and Its Diverse Roles as a Regulator of Extracellular Matrix in Fibrotic Disease.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2019
    Review
  17. Unfolding the Role of Calreticulin in Myeloproliferative Neoplasm Pathogenesis.Clinical cancer research : an official journal of the American Association for Cancer Research · 2019
    Review
  18. Article
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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

5 authors at 2 institutions in 1 country.

Manuel A PalleroDepartment of Pathology, VH 668 1530 3rd Ave., South, Birmingham, AL 35294-0019, USA.
Carrie A Elzie
Jiping Chen
Deane F Mosher
Joanne E Murphy-Ullrich
University of Alabama at Birmingham · USUniversity of Wisconsin–Madison · US

Funding

Comprehensive Training Grant in Bone Biology and DiseaseT32AR047512 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI ZAYZAFOON, MAJD · 2002 to 2011
$2.3M
Intermediate cell adhesion: role of calreticulin and LRPR01HL079644 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MURPHY-ULLRICH, JOANNE E · 2005 to 2008
$1.4M
Oral Health Research TrainingT32DE014300 · NIDCR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI REDDY, MICHAEL S · 2001 to 2006
$1.2M
EXTRAMURAL RESEARCH FACILITIES CONTRUCTIONC06RR015490 · NCRR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI GERRITY, LAURETTA W · 2000 to 2000
$1.0M
NCRR NIH HHS C06 RR015490NCRR NIH HHS C06 RR 15490NHLBI NIH HHS HL079644NHLBI NIH HHS R01 HL079644NIAMS NIH HHS T32 AR047512NIAMS NIH HHS T32AR47512-01A1NIDCR NIH HHS T32 DE014300NIDCR NIH HHS T32DE014300
6 · The paper itself

Abstract

Anoikis, apoptotic cell death due to loss of cell adhesion, is critical for regulation of tissue homeostasis in tissue remodeling. Fibrogenesis is associated with reduced fibroblast apoptosis. The matricellular protein thrombospondin 1 (TSP1) regulates cell adhesion and motility during tissue remodeling and in fibrogenesis. The N-terminal domain of TSP1 binds to the calreticulin-LRP1 receptor co-complex to signal down-regulation of cell adhesion and increased cell motility through focal adhesion disassembly. TSP1 signaling through calreticulin-LRP1 activates cell survival signals such as PI3-kinase. Therefore, we tested the hypothesis that TSP1 supports cell survival under adhesion-independent conditions to facilitate tissue remodeling. Here, we show that platelet TSP1, its N-terminal domain (NoC1) as a recombinant protein, or a peptide comprising the calreticulin-LRP1 binding site [amino acids 17-35 (hep I)] in the N-terminal domain promotes fibroblast survival under anchorage-independent conditions. TSP1 activates Akt and decreases apoptotic signaling through caspase 3 and PARP1 in suspended fibroblasts. Inhibition of PI3K/Akt activity blocks TSP1-mediated anchorage-independent survival. Fibroblasts lacking LRP1 or expressing calreticulin lacking the TSP1 binding site do not respond to TSP1 with anchorage-independent survival. These data define a novel role for TSP1 signaling through the calreticulin/LRP1 co-complex in tissue remodeling and fibrotic responses through stimulation of anoikis resistance.-Pallero, M. A., Elzie, C. A., Chen, J., Mosher, D. F., Murphy-Ullrich, J. E. Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis.

Indexed as

AnimalsAnoikisBinding SitesCalreticulinCaspase 3Cell AdhesionCell SurvivalFibroblastsHumansLow Density Lipoprotein Receptor-Related Protein-1MiceMice, KnockoutPeptidesPhosphatidylinositol 3-KinasesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesCalreticulinCASP3 protein, humanCasp3 protein, mouseCaspase 3Low Density Lipoprotein Receptor-Related Protein-1Lrp1 protein, mousePARP1 protein, humanParp1 protein, mousePeptidesPhosphatidylinositol 3-KinasesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProto-Oncogene Proteins c-aktReceptors, LDLThrombospondin 1Tumor Suppressor Proteins

Identifiers

PMID18653767
PMCPMC2574023
OpenAlexW2051871263

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.