FEBS Letters
Volume 582, Issue 29 , Pages 4003-4007, 10 December 2008

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

Edited by Gianni Cesareni

Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, P.O. Box 7, Karolina út 29, H-1518, Hungary

Received 7 October 2008; accepted 25 October 2008. published online 12 November 2008.

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)

Keywords: Cochlin, Collagen, Deafness, DFNA9, vWA domain

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PII: S0014-5793(08)00898-3

doi:10.1016/j.febslet.2008.10.050

FEBS Letters
Volume 582, Issue 29 , Pages 4003-4007, 10 December 2008

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