Molecular cloning and expression of human caldecrin

FEBS Letters

Saheki, Takeyori²  Yoshino, Izumi²  Akiyama, Masashi³  Nishii, Yasuho³  Noikura, Takenori¹  Tomomura, Mineko²  Tomomura, Akito²  Itoh, Hirotaka³ 

[1] Department of Dental Radiology, Faculty of Dentistry, Kagoshima University, Sakuragaoka 8-35-1, Kagoshima 890, Japan;Department of Biochemistry, Faculty of Medicine, Kagoshima University, Sakuragaoka 8-35-1, Kagoshima 890, Japan;Fuji Gotemba Research Laboratories, Chugai Pharmaceutical Co. Ltd., Komakado 1-135, Gotemba, Shizuoka 412, Japan

关键词: Pancreas;    Calcium;    Elastase;    Human;    caldecrin;    serum calcium-decreasing factor;    SCDA;    serum calcium-decreasing activity;    PCR;    polymerase chain reaction;    APMSF;    4-amidinophenylmethanesulphonyl fluoride;    PMSF;    phenylmethylsulfonyl fluoride;    PAGE;    polyacrylamide gel electrophoresis;    PX;    pancreatic extract;   

DOI  :  10.1016/0014-5793(96)00377-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Earlier we reported the primary structure of serum calcium-decreasing factor (caldecrin) from rat pancreas, a protein which is considered to be a member of the elastase family. In this report, we describe the isolation of the two homologous cDNA clones encoding caldecrin from human pancreas, the structures of which are identical except for one base and the corresponding amino acid residue. These human caldecrin isoforms are composed of a signal peptide of 16 amino acids, a propeptide of 13 amino acids, and a mature form of 239 amino acids. Both recombinant caldecrins showed the same chymotrypsin-type protease activity and hypocalcemic activity. The hypocalcemic activity of both remained intact even after treatment with PMSF to abolish their protease activity. These results suggest that human caldecrin possesses hypocalcemic activity that has no connection with its protease activity.

【 授权许可】

Unknown