Evidence map›Paper›PMID 21127050›Full record

ArticleThe Journal of biological chemistry2011

Identification and characterization of the integrin alpha2beta1 binding motif in chondroadherin mediating cell attachment.

Lisbet Haglund, Viveka Tillgren, Laura Addis, Christina Wenglén, Anneliese Recklies, Dick Heinegård

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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

27 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
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  11. Review
  12. Gene expression profiles of the meniscus avascular phenotype: A guide for meniscus tissue engineering.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2018
    Article
  13. Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin.Matrix biology : journal of the International Society for Matrix Biology · 2017
    Article
  14. Article
  15. Article
  16. Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.Matrix biology : journal of the International Society for Matrix Biology · 2015
    Review
  17. Article
  18. Article
  19. A tribute to Dick Heinegård.Matrix biology : journal of the International Society for Matrix Biology · 2014
    Article
  20. Integrins and chondrocyte-matrix interactions in articular cartilage.Matrix biology : journal of the International Society for Matrix Biology · 2014
    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

6 authors at 2 institutions in 2 countries.

Lisbet HaglundDepartment of Clinical Sciences Lund, Lund University, BMC Plan C12, SE-22184 Lund, Sweden.
Viveka Tillgren
Laura Addis
Christina Wenglén
Anneliese Recklies
Dick Heinegård
Lund University · SEShriners Hospitals for Children - Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chondroadherin is a leucine-rich repeat protein known to mediate adhesion of isolated cells via the integrin α(2)β(1) and to interact with collagen. In this work, we show that cell adhesion to chondroadherin leads to activation of MAPKs but does not result in cell spreading and division. This is in contrast to the spreading and dividing of cells grown on collagen, although the binding is mediated via the same α(2)β(1) receptor. We identified a cell binding motif, CQLRGLRRWLEAK(318) by mass spectrometry after protease digestion of chondroadherin. Cells adhering to the synthetic peptide CQLRGLRRWLEAK(318) remained round, as was observed when they bound to the intact protein. The peptide added in solution was able to inhibit cell adhesion to the intact protein in a dose-dependent manner and was also verified to bind to the α(2)β(1) integrin. A cyclic peptide, CQLRGLRRWLEAKASRPDATC(326), mimicking the structural constraints of this sequence in the intact protein, showed similar efficiency in inhibiting binding to chondroadherin. The unique peptide motif responsible for cellular binding is primarily located in the octamer sequence LRRWLEAK(318). Binding of cells to the active peptide or to chondroadherin immobilized on cell culture plates rapidly induces intracellular signaling (i.e. ERK phosphorylation). Thus, chondroadherin interaction with cells may be central for maintaining the adult chondrocyte phenotype and cartilage homeostasis. The peptides, particularly the more stable cyclic peptide, open new opportunities to modulate cell behavior in situations of tissue pathology.

Indexed as

Binding SitesCell AdhesionAmino Acid SequenceAnimalsCattleCell DivisionCell ShapeExtracellular Matrix ProteinsExtracellular Signal-Regulated MAP KinasesHumansIntegrin alpha2beta1Mitogen-Activated Protein Kinase KinasesPeptides, CyclicPhosphorylationProtein BindingchondroadherinExtracellular Matrix ProteinsExtracellular Signal-Regulated MAP KinasesIntegrin alpha2beta1Mitogen-Activated Protein Kinase KinasesPeptides, Cyclic

Identifiers

PMID21127050
PMCPMC3030393
OpenAlexW2055364080

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.