Cloning of the PABA peptide hydrolase alpha subunit (PPHα) from human small intestine and its expression in COS‐1 cells

FEBS Letters

Dumermuth, Eric²  Grünberg, Jürgen²  Eldering, Joyce A.²  Sterchi, Erwin E.²  Jiang, Weiping¹ 

[1] Department of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey, PA 17033, USA;Institute of Biochemistry and Molecular Biology, University of Berne, Bühlstrasse 28, CH-3012 Berne, Switzerland

关键词: PABA peptide hydrolase;    Meprin;    Astacin;    Zinc-metalloendopeptidase;    Human;    Enterocyte;    COS-1;    PPH;    PABA peptide hydrolase;    SDS-PAGE;    sodium dodecylsulfate polyacrylamide gel electrophoresis;    EGF;    epidermal growth factor;    ER;    endoplasmic reticulum;    NP40;    Nonidet 40;    DOC;    deoxycholate;    PBS;    phosphate-buffered saline;   

DOI  :  10.1016/0014-5793(93)80421-P

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

PABA peptide hydrolase (PPH) from human enterocytes is comprised of two submits, alpha and beta. PPHα is over 70% identical to meprin, a protease isolated from mouse and rat kidney. The enzyme shows a modular organization in that it contains an astacin protease domain, an adhesive domain, an EGF-like domain, and a putative C-terminal membrane spanning domain. Expression of a chimeric meprin-PPHα cDNA in COS-1 cells led to the synthesis of immature, transport-incompetent homodimers. In addition, complex glycosylated forms were detected in the culture medium, suggesting that the enzyme is secreted after proteolytic removal of the membrane anchor.

【 授权许可】

Unknown