Primary structure of a novel ABC transporter with a chromosomal localization on the band encoding the multidrug resistance‐associated protein

FEBS Letters

Klugbauer, Norbert¹  Hofmann, Franz¹ 

[1] Institut für Pharmakologie und Toxikologie der Technischen Universität München, Biedersteiner Str. 29, 80802 Munich, Germany

关键词: ABC transporter;    Chemotherapy;    Multidrug resistance;    Thyroid carcinoma;    ABC;    ATP-binding cassette;    ATS;    active transport signature;    hMTC;    human medullary thyroid carcinoma;   

DOI  :  10.1016/0014-5793(96)00700-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Complementary DNA clones encoding a novel protein, ABC-C, with the typical structural features of the ABC transporter family were identified in a human medullary thyroid carcinoma cell line. The transporter consists of 1704 amino acid residues with two homologous repeats, each harboring six putative transmembrane helices and an ATP-binding cassette motif. The mRNA is expressed highest in normal lung, but also in varying amounts in other tissues and in C-cell carcinoma. The ABC-C gene is mapped on chromosome 16p13.3, in close physical proximity to another ABC transporter, the multidrug resistance-associated protein. This related protein is assumed to confer resistance to chemotherapeutic drugs in small cell lung carcinoma. The genomic clustering of both transporters, typical also for other members of the ABC family, supports the notion that ABC-C may be involved in development of resistance to xenobiotics.

【 授权许可】

Unknown