University of Oulu

Koivunen, J., Tu, H., Kemppainen, A. et al. Integrin α11β1 is a receptor for collagen XIII. Cell Tissue Res 383, 1135–1153 (2021).

Integrin α11β1 is a receptor for collagen XIII

Saved in:
Author: Koivunen, Jarkko1; Tu, Hongmin2; Kemppainen, Antti1;
Organizations: 1Oulu Center for Cell-Matrix Research, Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, FIN-90014, Oulu, Finland
2Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5000, FIN-90014, Oulu, Finland
3Research Unit of Medical Imaging, Physics and Technology, University of Oulu, P.O. Box 5000, FIN-90014, Oulu, Finland
4Department of Biochemistry and MediCity Research Laboratory, University of Turku, Tykistökatu 6A, 20520, Turku, Finland
5Department of Biomedicine and Center of Cancer Biomarkers, University of Bergen, Jonas Lies vei 91, N-5009, Bergen, Norway
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 1.8 MB)
Persistent link:
Language: English
Published: Springer Nature, 2021
Publish Date: 2021-01-26


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−/−) with mice overexpressing Col13a1 (Col13a1oe). When we evaluated the bone morphology by microcomputed tomography, Col13a1oe mice had a drastic bone overgrowth followed by severe osteoporosis, whereas the double mutant mouse line showed a much milder bone phenotype. To conclude, our data identifies integrin α11β1 as a new collagen XIII receptor and demonstrates that this ligand-receptor pair has a role in the maintenance of bone homeostasis.

see all

Series: Cell and tissue research
ISSN: 0302-766X
ISSN-E: 1432-0878
ISSN-L: 0302-766X
Volume: 383
Pages: 1135 - 1153
DOI: 10.1007/s00441-020-03300-y
Type of Publication: A1 Journal article – refereed
Field of Science: 3111 Biomedicine
Funding: Open access funding provided by University of Oulu including Oulu University Hospital. This work was supported by the Finnish Centre of Excellence Programme (251314 years 2012–2017) of the Academy of Finland (294617 to JK, 308867 to TP, 268378 and 273571 to SS), the Sigrid Jusélius Foundation (TP) and by grants from Centre for Cancer Biomarkers (Centre of Excellence funded by Research council of Norway, Project No 223250 to DG), and The Norwegian Centre for International Cooperation in Education (Diku: NNA-2016/10026 to DG). European Research Council under the European Union’s Seventh Framework Programme (FP/2007-2013)/ERC Grant Agreement no. 336267 to SS. Part of research infrastructure has been supported by the European Commission Regional Development Fund (decision nr. 538/2010).
EU Grant Number: (336267) 3D-OA-HISTO - Development of 3D Histopathological Grading of Osteoarthritis
Academy of Finland Grant Number: 251314
Detailed Information: 251314 (Academy of Finland Funding decision)
294617 (Academy of Finland Funding decision)
308867 (Academy of Finland Funding decision)
268378 (Academy of Finland Funding decision)
273571 (Academy of Finland Funding decision)
Dataset Reference: Electronic supplementary material:
Copyright information: © The Author(s) 2020. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit