Evidence map›Paper›PMID 33306155›Full record

ArticleCell and tissue research2021

Integrin α11β1 is a receptor for collagen XIII.

Jarkko Koivunen, Hongmin Tu, Antti Kemppainen, Padmanabhan Anbazhagan, Mikko A Finnilä, Simo Saarakkala, Jarmo Käpylä, Ning Lu, Anne Heikkinen, André H Juffer and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Cell and tissue research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Unraveling the Causal Linkages ofBioMed research international · 2026
    Article
  2. Targeting collagen to optimize cancer immunotherapy.Experimental hematology & oncology · 2025
    Review
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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

13 authors at 3 institutions in 2 countries.

Jarkko KoivunenOulu Center for Cell-Matrix Research, Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, FIN-90014, Oulu, Finland.
Hongmin TuBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5000, FIN-90014, Oulu, Finland.
Antti KemppainenOulu Center for Cell-Matrix Research, Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, FIN-90014, Oulu, Finland.
Padmanabhan AnbazhaganBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5000, FIN-90014, Oulu, Finland.
Mikko A FinniläResearch Unit of Medical Imaging, Physics and Technology, University of Oulu, P.O. Box 5000, FIN-90014, Oulu, Finland.
Simo SaarakkalaResearch Unit of Medical Imaging, Physics and Technology, University of Oulu, P.O. Box 5000, FIN-90014, Oulu, Finland.
Jarmo KäpyläDepartment of Biochemistry and MediCity Research Laboratory, University of Turku, Tykistökatu 6A, 20520, Turku, Finland.
Ning LuDepartment of Biomedicine and Center of Cancer Biomarkers, University of Bergen, Jonas Lies vei 91, N-5009, Bergen, Norway.
Anne HeikkinenOulu Center for Cell-Matrix Research, Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, FIN-90014, Oulu, Finland.
André H JufferBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5000, FIN-90014, Oulu, Finland.
Jyrki HeinoDepartment of Biochemistry and MediCity Research Laboratory, University of Turku, Tykistökatu 6A, 20520, Turku, Finland.
Donald GullbergDepartment of Biomedicine and Center of Cancer Biomarkers, University of Bergen, Jonas Lies vei 91, N-5009, Bergen, Norway.
Taina PihlajaniemiOulu Center for Cell-Matrix Research, Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, FIN-90014, Oulu, Finland. taina.pihlajaniemi@oulu.fi.ORCID http://orcid.org/0000-0002-1664-9045
University of Oulu · FIUniversity of Bergen · NOUniversity of Turku · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagen XIII is a conserved transmembrane collagen mainly expressed in mesenchymal tissues. Previously, we have shown that collagen XIII modulates tissue development and homeostasis. Integrins are a family of receptors that mediate signals from the environment into the cells and vice versa. Integrin α11β1 is a collagen receptor known to recognize the GFOGER (O=hydroxyproline) sequence in collagens. Interestingly, collagen XIII and integrin α11β1 both have a role in the regulation of bone homeostasis. To study whether α11β1 is a receptor for collagen XIII, we utilized C2C12 cells transfected to express α11β1 as their only collagen receptor. The interaction between collagen XIII and integrin α11β1 was also confirmed by surface plasmon resonance and pull-down assays. We discovered that integrin α11β1 mediates cell adhesion to two collagenous motifs, namely GPKGER and GF(S)QGEK, that were shown to act as the recognition sites for the integrin α11-I domain. Furthermore, we studied the in vivo significance of the α11β1-collagen XIII interaction by crossbreeding α11 null mice (Itga11

Indexed as

Bone and BonesAnimalsCell AdhesionCell LineCollagen Type XIIIHumansIntegrin alpha ChainsIntegrinsMiceMice, KnockoutReceptors, CollagenCollagen Type XIIIintegrin alpha11beta1Integrin alpha ChainsIntegrinsITGA11 protein, humanReceptors, CollagenBone homeostasisCell adhesionCollagenECM receptorsIntegrin

Identifiers

PMID33306155
PMCPMC7960628
OpenAlexW3112439676

What OpenQuestion holds

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LicenceCC BY
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.