Skip to main content

Analysis of Collagen-Binding Integrin Interactions with Supramolecular Aggregates of the Extracellular Matrix

  • Protocol
  • First Online:
Collagen

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1944))

Abstract

Integrin-mediated interactions of cells with the extracellular matrix (ECM) are important for their activities. The ECM itself is a complex network of macromolecules forming aggregates or suprastructures. Moreover, the molecular composition is important for the macromolecular organization and, thereby, the functional properties of the ECM. In addition, collagen molecules lose their integrin-binding capabilities after incorporation into fibrils. Therefore, we have established detailed protocols for the analysis of integrin-matrix interactions at the supramolecular level.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 149.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Hardcover Book
USD 199.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Lu P, Weaver VM, Werb Z (2012) The extracellular matrix: a dynamic niche in cancer progression. J Cell Biol 196:395–406

    Article  CAS  Google Scholar 

  2. Nelson CM, Bissell MJ (2006) Of extracellular matrix, scaffolds, and signaling: tissue architecture regulates development, homeostasis, and cancer. Annu Rev Cell Dev Biol 22:287–309

    Article  CAS  Google Scholar 

  3. Blaschke UK, Eikenberry EF, Hulmes DJS, Galla HJ, Bruckner P (2000) Collagen XI nucleates assembly and limit lateral growth of cartilage fibrils. J Biol Chem 275:10370–10378

    Article  CAS  Google Scholar 

  4. Mercier I, Lechaire JP, Desmouliere A, Gaill F, Aumailley M (1996) Interactions of human skin fibroblasts with monomeric or fibrillar collagens induce different organization of the cytoskeleton. Exp Cell Res 225:245–256

    Article  CAS  Google Scholar 

  5. Woltersdorf C, Bonk M, Leitinger B, Huhtala M, Käpylä J, Heino J et al (2017) The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on noncollagenous surface macromolecules rather than the collagens in cartilage fibrils. Matrix Biol 63:91–105

    Article  CAS  Google Scholar 

  6. Eble JA, Beermann B, Hinz HJ, Schmidt-Hederich A (2001) α2β1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen. J Biol Chem 276:12274–12284

    Article  CAS  Google Scholar 

  7. de Santana Evangelista K, Andrich F, Figueiredo de Rezende F, Niland S, Cordeiro MN, Horlacher T et al (2009) Plumieribetin, a fish lectin homologous to mannose-binding B-type lectins, inhibits the collagen-binding α1β1 integrin. J Biol Chem 284:34747–34759

    Article  Google Scholar 

  8. Tulla M, Pentikäinen OT, Viitasalo T, Käpylä J, Impola U, Nykvist P et al (2001) Selective binding of collagen subtypes by integrin α1I, α2I, and α10I domains. J Biol Chem 276:48206–48212

    Article  CAS  Google Scholar 

  9. Käpylä J, Ivaska J, Riikonen R, Nykvist P, Pentikainen O, Johnson M, Heino J (2000) Integrin alpha2 I-domain recognizes type I and type IV collagens by different mechanisms. J Biol Chem 275:3348–3354

    Article  Google Scholar 

  10. Leitinger B (2003) Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2: identification of collagen binding sites in DDR2. J Biol Chem 278:16761–16769

    Article  CAS  Google Scholar 

  11. Xu H, Raynal N, Stathopoulos S, Myllyharju J, Farndale RW, Leitinger B (2011) Collagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1. Matrix Biol 30:16–26

    Article  Google Scholar 

  12. Böhme K, Winterhalter KH, Bruckner P (1995) Terminal differentiation of chondrocytes in culture is a spontaneous process and is arrested by transforming growth factor-beta2 and basic fibroblast growth factor in synergy. Exp Cell Res 216:191–198

    Article  Google Scholar 

  13. Bruckner P, Hörler I, Mendler M, Houze Y, Winterhalter KH, Eich-Bender SG, Spycher MA (1989) Induction and prevention of chondrocyte hypertrophy in culture. J Cell Biol 109:2537–2545

    Article  CAS  Google Scholar 

  14. Mendler M, Eich-Bender SG, Vaughan L, Winterhalter KH, Bruckner P (1989) Cartilage contains mixed fibrils of collagen types II, IX, and XI. J Cell Biol 108:191–197

    Article  CAS  Google Scholar 

  15. Lenter M, Uhlig H, Hamann A, Jenö P, Imhof B, Vestweber D (1993) A monoclonal antibody against an activation epitope on mouse integrin chain β1 blocks adhesion of lymphocytes to the endothelial integrin α6β1. Proc Natl Acad Sci U S A 90:9051–9055

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This work was supported by Deutsche Forschungsgemeinschaft grants BR1497/4-1 and EB177/9-1 to PB and JAE and a grant from BBSRC UK (BB/I011226/1) to BL.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Uwe Hansen .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2019 Springer Science+Business Media, LLC, part of Springer Nature

About this protocol

Check for updates. Verify currency and authenticity via CrossMark

Cite this protocol

Hansen, U. (2019). Analysis of Collagen-Binding Integrin Interactions with Supramolecular Aggregates of the Extracellular Matrix. In: Sagi, I., Afratis, N. (eds) Collagen. Methods in Molecular Biology, vol 1944. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9095-5_12

Download citation

  • DOI: https://doi.org/10.1007/978-1-4939-9095-5_12

  • Published:

  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-9094-8

  • Online ISBN: 978-1-4939-9095-5

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics