Complete primary structure of a calcium‐dependent serine proteinase capable of degrading extracellular matrix proteins

FEBS Letters

Imajoh-Ohmi, Shinobu¹  Kinoshita, Hirohisa³  Hamada, Yoshio²  Isono, Kaichi⁵  Tokunaga, Kastuo⁴  Sakiyama, Hisako³  Sakiyama, Shigeru⁴ 

[1] The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minatoku, Tokyo 108, Japan;Laboratory of Tissue and Cell Culture, National Institute for Basic Biology,azaki 444 Japan;Division of Physiology and Pathology, National Institute of Radiological Sciences, 4-9-1 Anagawa, Chiba 260, Japan;Division of Biochemistry, Chiba Cancer Center, 666-2 Nitona, Chiba 280, Japan;2nd Department of Surgery, Chiba University School of Medicine, Chiba 280, Japan

关键词: Ca2+;    Serine protease;    Ca2+-dependent;    cDNA;    Protein;    extracellular matrix;   

DOI  :  10.1016/0014-5793(89)80766-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel calcium-dependent serine proteinase (CASP) secreted from malignant hamster embryo fibroblast Ni 12C2 degrades extracellular matrix proteins. A complementary DNA encoding CASP has been isolated with the use of oligonucleotide probes synthesized based on partial amino acid sequences of CASP. The complete amino acid sequence of CASP revealed that it has a serine active site at the C-terminal side. Glu rich and proEGF homologous sites are found at the N-terminal site suggesting that it is structurally similar to blood coagulation factors such as IX, X and an anti-coagulation factor, protein C.

【 授权许可】

Unknown