Forschungsdatenbank PMU-SQQUID

Functional characterization of wild-type and a mutated form of SLC26A4 identified in a patient with Pendred syndrome.
Dossena, S; Vezzoli, V; Cerutti, N; Bazzini, C; Tosco, M; Sironi, C; Rodighiero, S; Meyer, G; Fascio, U; Fürst, J; Ritter, M; Fugazzola, L; Persani, L; Zorowka, P; Storelli, C; Beck-Peccoz, P; Bottà, G; Paulmichl, M;
Cell Physiol Biochem. 2006; 17(5-6): 245-256.
Originalarbeiten (Zeitschrift)

Abstract/Keywords Web of Science PubMed Full Text

PMU-Autor/inn/en

Dossena Silvia
Paulmichl Markus
Ritter Markus

Abstract

Malfunction of the SLC26A4 protein leads to prelingual deafness often associated with mild thyroid dysfunction and goiter. It is assumed that SLC26A4 acts as a chloride/anion exchanger responsible for the iodide organification in the thyroid gland, and conditioning of the endolymphatic fluid in the inner ear.

Useful keywords (using NLM MeSH Indexing)

4,4"-Diisothiocyanostilbene-2,2"-Disulfonic Acid/pharmacology

Biological Transport/drug effects

Cells, Cultured

Chlorides/metabolism

Cytoplasm/metabolism

Goiter/genetics*

Hearing Loss, Sensorineural/genetics*

Humans

Hypothyroidism/genetics*

Iodides/metabolism

Membrane Transport Proteins/drug effects

Membrane Transport Proteins/genetics*

Membrane Transport Proteins/metabolism*

Mutation*

Niflumic Acid/pharmacology

Nitrobenzoates/pharmacology

Syndrome

Find related publications in this database (Keywords)

pendred syndrome
SLC26A4
chloride/bicarbonate exchanger
chloride uptake
ion transport
NPPB
DIDS
niflumic acid