CRYM mutations cause deafness through thyroid hormone binding properties in the fibrocytes of the cochlea.
J Med Genet
; 43(6): e25, 2006 Jun.
Article
em En
| MEDLINE
| ID: mdl-16740909
ABSTRACT
BACKGROUND:
In a search for mutations of mu-crystallin (CRYM), a taxion specific crystalline which is also known as an NADP regulated thyroid hormone binding protein, two mutations were found at the C-terminus in patients with non-syndromic deafness.OBJECTIVE:
To investigate the mechanism of hearing loss caused by CRYM mutationsMETHODS:
T3 binding activity of mutant mu-crystallin was compared with that of wild-type mu-crystallin, because mu-crystallin is known to be identical to T3 binding protein. To explore the sites within the cochlea where mu-crystallin is functioning, its localisation in the mouse cochlea was investigated immunocytochemically using a specific antibody.RESULTS:
One mutant was shown to have no binding capacity for T3, indicating that CRYM mutations cause auditory dysfunction through thyroid hormone binding properties. Immunocytochemical results indicated that mu-crystallin was distributed within type II fibrocytes of the lateral wall, which are known to contain Na,K-ATPase.CONCLUSIONS:
CRYM mutations may cause auditory dysfunction through thyroid hormone binding effects on the fibrocytes of the cochlea. mu-Crystallin may be involved in the potassium ion recycling system together with Na,K-ATPase. Future animal experiments will be necessary to confirm a causal relation between Na,K-ATPase, T3, and deafness.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Tri-Iodotironina
/
Cóclea
/
Mutação de Sentido Incorreto
/
Cristalinas
/
Surdez
Limite:
Animals
/
Humans
Idioma:
En
Revista:
J Med Genet
Ano de publicação:
2006
Tipo de documento:
Article