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Complete primary structure of a calcium‐dependent serine proteinase capable of degrading extracellular matrix proteins
Author(s) -
Kinoshita Hirohisa,
Sakiyama Hisako,
Tokunaga Kastuo,
Imajoh-Ohmi Shinobu,
Hamada Yoshio,
Isono Kaichi,
Sakiyama Shigeru
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80766-5
Subject(s) - serine , biochemistry , amino acid , hamster , extracellular matrix , extracellular , peptide sequence , oligonucleotide , chemistry , biology , dna , microbiology and biotechnology , enzyme , gene
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.