The second von Willebrand type A domain of cochlin has high affinity for type I, type II and type IV collagens.
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.
Nagy
Ildikó
I
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, P.O. Box 7, Karolina út 29, H-1518, Hungary.
Trexler
Mária
M
Patthy
László
L
D002460:Cell Line; D003051:Cochlea / Q000378:metabolism; D024042:Collagen Type I / Q000378:metabolism*; D024043:Collagen Type II / Q000378:metabolism*; D024141:Collagen Type IV / Q000378:metabolism*; D005109:Extracellular Matrix / Q000378:metabolism; D016326:Extracellular Matrix Proteins; D034381:Hearing Loss / Q000235:genetics / Q000378:metabolism; D006801:Humans; D017434:Protein Structure, Tertiary / Q000235:genetics; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014841:von Willebrand Factor / Q000737:chemistry
C110668:COCH protein, human; D024042:Collagen Type I; D024043:Collagen Type II; D024141:Collagen Type IV; D016326:Extracellular Matrix Proteins; D011506:Proteins; D014841:von Willebrand Factor