Structure–function relationships of the extracellular domain of the autosomal dominant polycystic kidney disease‐associated protein, polycystin‐1

FEBS Letters

Weston, Benjamin S.¹  Malhas, Ashraf N.¹  Price, Robert G.¹ 

[1] Biochemistry Section, Department of Life Sciences, King's College London, London SE1 9NN, UK

关键词: Polycystic kidney disease;    Polycystin-1;    Extracellular matrix protein;    Cell adhesion;    ADPKD;    autosomal dominant polycystic kidney disease;    LRRs;    leucine-rich repeats;    ECM;    extracellular matrix;    LDL;    low-density lipoprotein;    REJ;    receptor for egg jelly;    GPS;    G protein-coupled receptor proteolytic site;    PC-1;    polycystin-1;   

DOI  :  10.1016/S0014-5793(03)00130-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Polycystin-1 (PC-1) is a member of a novel family of proteins that have a multidomain structure. Although the C-terminal intracellular segments have been extensively studied, mainly with respect to their putative involvement in cell signalling, the potential function of the extracellular domains has received less attention. Mutations in PC-1 result in autosomal dominant polycystic kidney disease (ADPKD) which is characterised by perturbation of transport resulting in fluid accumulation, cell proliferation and modification of the extracellular matrix. The possibility that the interaction of a component of the extracellular matrix or some external factor with PC-1 may be important in the initiation or progression of ADPKD cannot currently be ruled out. The purpose of this review is to assess current evidence for the function of the PC-1 extracellular domains, and their potential implications for ADPKD.

【 授权许可】

Unknown