Integrin-mediated cell adhesion to type I collagen fibrils

Johanna Jokinen, Elina Dadu, Petri Nykvist, Jarmo Käpylä, Daniel J. White, Johanna Ivaska, Piia Vehviläinen, Hilkka Reunanen, Hannu Larjava, Lari Häkkinen, Jyrki Heino (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

216 Citations (Scopus)

Abstract

In the integrin family, the collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, α1β1 and α2β1 integrins, are known to bind to monomeric form of type I collagen. However, in tissues type I collagen monomers are organized into large fibrils immediately after they are released from cells. Here, we studied collagen fibril recognition by integrins. By an immunoelectron microscopy method we showed that integrin α2I domain is able to bind to classical D-banded type I collagen fibrils. However, according to the solid phase binding assay, the collagen fibril formation appeared to reduce integrin α1I and α2I domain avidity to collagen and to lower the number of putative αI domain binding sites on it. Respectively, cellular α1β1 integrin was able to mediate cell spreading significantly better on monomeric than on fibrillar type I collagen matrix, whereas α2β1 integrin appeared still to facilitate both cell spreading on fibrillar type I collagen matrix and also the contraction of fibrillar type I collagen gel. Additionally, α2β1 integrin promoted the integrin-mediated formation of long cellular projections typically induced by fibrillar collagen. Thus, these findings suggest that α2β1 integrin is a functional cellular receptor for type I collagen fibrils, whereas α1β1 integrin may only effectively bind type I collagen monomers. Furthermore, when the effect of soluble αI domains on type I collagen fibril formation was tested in vitro, the observations suggest that integrin type collagen receptors might guide or even promote pericellular collagen fibrillogenesis.
Original languageEnglish
Pages (from-to)31956 - 31963
Number of pages8
JournalJournal of Biological Chemistry
Volume279
Issue number30
DOIs
Publication statusPublished - 2004
MoE publication typeA1 Journal article-refereed

Fingerprint

Cell adhesion
Collagen Type I
Cell Adhesion
Integrins
Fibrillar Collagens
Collagen
Collagen Receptors
Monomers
Immunoelectron Microscopy
Assays
Microscopic examination
Gels
Binding Sites
Tissue

Keywords

  • collagens
  • integrin
  • fibrils

Cite this

Jokinen, J., Dadu, E., Nykvist, P., Käpylä, J., White, D. J., Ivaska, J., ... Heino, J. (2004). Integrin-mediated cell adhesion to type I collagen fibrils. Journal of Biological Chemistry, 279(30), 31956 - 31963. https://doi.org/10.1074/jbc.M401409200
Jokinen, Johanna ; Dadu, Elina ; Nykvist, Petri ; Käpylä, Jarmo ; White, Daniel J. ; Ivaska, Johanna ; Vehviläinen, Piia ; Reunanen, Hilkka ; Larjava, Hannu ; Häkkinen, Lari ; Heino, Jyrki. / Integrin-mediated cell adhesion to type I collagen fibrils. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 30. pp. 31956 - 31963.
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Jokinen, J, Dadu, E, Nykvist, P, Käpylä, J, White, DJ, Ivaska, J, Vehviläinen, P, Reunanen, H, Larjava, H, Häkkinen, L & Heino, J 2004, 'Integrin-mediated cell adhesion to type I collagen fibrils', Journal of Biological Chemistry, vol. 279, no. 30, pp. 31956 - 31963. https://doi.org/10.1074/jbc.M401409200

Integrin-mediated cell adhesion to type I collagen fibrils. / Jokinen, Johanna; Dadu, Elina; Nykvist, Petri; Käpylä, Jarmo; White, Daniel J.; Ivaska, Johanna; Vehviläinen, Piia; Reunanen, Hilkka; Larjava, Hannu; Häkkinen, Lari; Heino, Jyrki (Corresponding Author).

In: Journal of Biological Chemistry, Vol. 279, No. 30, 2004, p. 31956 - 31963.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Integrin-mediated cell adhesion to type I collagen fibrils

AU - Jokinen, Johanna

AU - Dadu, Elina

AU - Nykvist, Petri

AU - Käpylä, Jarmo

AU - White, Daniel J.

AU - Ivaska, Johanna

AU - Vehviläinen, Piia

AU - Reunanen, Hilkka

AU - Larjava, Hannu

AU - Häkkinen, Lari

AU - Heino, Jyrki

PY - 2004

Y1 - 2004

N2 - In the integrin family, the collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, α1β1 and α2β1 integrins, are known to bind to monomeric form of type I collagen. However, in tissues type I collagen monomers are organized into large fibrils immediately after they are released from cells. Here, we studied collagen fibril recognition by integrins. By an immunoelectron microscopy method we showed that integrin α2I domain is able to bind to classical D-banded type I collagen fibrils. However, according to the solid phase binding assay, the collagen fibril formation appeared to reduce integrin α1I and α2I domain avidity to collagen and to lower the number of putative αI domain binding sites on it. Respectively, cellular α1β1 integrin was able to mediate cell spreading significantly better on monomeric than on fibrillar type I collagen matrix, whereas α2β1 integrin appeared still to facilitate both cell spreading on fibrillar type I collagen matrix and also the contraction of fibrillar type I collagen gel. Additionally, α2β1 integrin promoted the integrin-mediated formation of long cellular projections typically induced by fibrillar collagen. Thus, these findings suggest that α2β1 integrin is a functional cellular receptor for type I collagen fibrils, whereas α1β1 integrin may only effectively bind type I collagen monomers. Furthermore, when the effect of soluble αI domains on type I collagen fibril formation was tested in vitro, the observations suggest that integrin type collagen receptors might guide or even promote pericellular collagen fibrillogenesis.

AB - In the integrin family, the collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, α1β1 and α2β1 integrins, are known to bind to monomeric form of type I collagen. However, in tissues type I collagen monomers are organized into large fibrils immediately after they are released from cells. Here, we studied collagen fibril recognition by integrins. By an immunoelectron microscopy method we showed that integrin α2I domain is able to bind to classical D-banded type I collagen fibrils. However, according to the solid phase binding assay, the collagen fibril formation appeared to reduce integrin α1I and α2I domain avidity to collagen and to lower the number of putative αI domain binding sites on it. Respectively, cellular α1β1 integrin was able to mediate cell spreading significantly better on monomeric than on fibrillar type I collagen matrix, whereas α2β1 integrin appeared still to facilitate both cell spreading on fibrillar type I collagen matrix and also the contraction of fibrillar type I collagen gel. Additionally, α2β1 integrin promoted the integrin-mediated formation of long cellular projections typically induced by fibrillar collagen. Thus, these findings suggest that α2β1 integrin is a functional cellular receptor for type I collagen fibrils, whereas α1β1 integrin may only effectively bind type I collagen monomers. Furthermore, when the effect of soluble αI domains on type I collagen fibril formation was tested in vitro, the observations suggest that integrin type collagen receptors might guide or even promote pericellular collagen fibrillogenesis.

KW - collagens

KW - integrin

KW - fibrils

U2 - 10.1074/jbc.M401409200

DO - 10.1074/jbc.M401409200

M3 - Article

VL - 279

SP - 31956

EP - 31963

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 30

ER -

Jokinen J, Dadu E, Nykvist P, Käpylä J, White DJ, Ivaska J et al. Integrin-mediated cell adhesion to type I collagen fibrils. Journal of Biological Chemistry. 2004;279(30):31956 - 31963. https://doi.org/10.1074/jbc.M401409200