Gene structure and 5'‐upstream sequence of rat cathepsin L

FEBS Letters

Katunuma, Nobuhiko²  Kominami, Eiki¹  Suzuki, Koichi³  Ishidoh, Kazumi³ 

[1] Department of Biochemistry, Juntendo University School of Medicine. Hongo 2-1-1, Bunkyo-ku, Tokyo 113, Japan;Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima 770, Japan;Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Honkomagome 3-18-22, Bunkyo-ku, Tokyo 113, Japan

关键词: Cathepsin L;    Gene structure;    Lysosomal proteinase;    Major excreted protein;    Promoter-enhancer;    MEP;    major excreted protein;    TPA;    4-O-tetradecanoyl phorbol-13-acetate;    PDGF;    platelet-derived growth factor;    kbp;    kilobase pairs;    bp;    base pairs;    b;    bases;    AP-2;    activator protein 2;    CRE;    cAMP regulatory element;   

DOI  :  10.1016/0014-5793(89)81497-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of rat cathepsin L gene has been determined. The gene spans 8.5 kilobase pairs comprising 8 exons, and has an intron located near the active site cysteine residue. The gene structure does not correspond well to the functional units of the proteinase. These characteristics are found to be in common with the cysteine proteinase gene family. In the 5'-upstream region, one CAAT-box and four SP-1 binding sites, together with two AP-2 binding sites and CRE, but no typical TATA-box are found. Further, SP-1 and AP-2 binding sites and an octamer motif are also found in the 1st intron, suggesting a complex regulatory mechanism for the expression of the cathepsin L gene.

【 授权许可】

Unknown