The second von Willebrand type A domain of cochlin has high affinity for type I, type II and type IV collagens

Ildikó Nagy, M. Trexler, L. Patthy

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Cochlin is colocalized with type II collagen in the extracellular matrix of cochlea and has been suggested to interact with this collagen. Here we show that the second von Willebrand type A domain of cochlin has affinity for type II collagen, as well as type I and type IV collagens whereas the LCCL-domain of cochlin has no affinity for these proteins. The implications of these findings for the mechanism whereby cochlin mutations cause the dominant negative DFNA9-type hearing loss are discussed. Structured summary: MINT-6796048:type I collagen (uniprotkb:P02452) binds (MI:0407) to cochlin-vWA2 uniprotkb:O43405) by surface plasmon resonance (MI:0107)MINT-6796166:type III collagen (uniprotkb:P02462) binds (MI:0407) to cochlin-vWA2 (uniprotkb:O43405) by surface plasmon resonance (MI:0107)MINT-6796062:type II collagen (uniprotkb:P02458) binds (MI:0407) to cochlin-vWA2 (uniprotkb:O43405) by surface plasmon resonance (MI:0107).

Original languageEnglish
Pages (from-to)4003-4007
Number of pages5
JournalFEBS Letters
Volume582
Issue number29
DOIs
Publication statusPublished - Dec 10 2008

Fingerprint

Collagen Type IV
Collagen Type II
Surface Plasmon Resonance
Surface plasmon resonance
Collagen Type I
Collagen Type III
Cochlea
Audition
Hearing Loss
Extracellular Matrix
Collagen
Mutation
Proteins

Keywords

  • Cochlin
  • Collagen
  • Deafness
  • DFNA9
  • vWA domain

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

The second von Willebrand type A domain of cochlin has high affinity for type I, type II and type IV collagens. / Nagy, Ildikó; Trexler, M.; Patthy, L.

In: FEBS Letters, Vol. 582, No. 29, 10.12.2008, p. 4003-4007.

Research output: Contribution to journalArticle

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N2 - Cochlin is colocalized with type II collagen in the extracellular matrix of cochlea and has been suggested to interact with this collagen. Here we show that the second von Willebrand type A domain of cochlin has affinity for type II collagen, as well as type I and type IV collagens whereas the LCCL-domain of cochlin has no affinity for these proteins. The implications of these findings for the mechanism whereby cochlin mutations cause the dominant negative DFNA9-type hearing loss are discussed. Structured summary: MINT-6796048:type I collagen (uniprotkb:P02452) binds (MI:0407) to cochlin-vWA2 uniprotkb:O43405) by surface plasmon resonance (MI:0107)MINT-6796166:type III collagen (uniprotkb:P02462) binds (MI:0407) to cochlin-vWA2 (uniprotkb:O43405) by surface plasmon resonance (MI:0107)MINT-6796062:type II collagen (uniprotkb:P02458) binds (MI:0407) to cochlin-vWA2 (uniprotkb:O43405) by surface plasmon resonance (MI:0107).

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