Complete primary structure of calcium-dependent serine proteinase capable of degrading extracellular matrix proteins.
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 sequences of CASP revealed that it has a 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 anticoagulation factor, protein C.
Kinoshita
H
H
Division of Physiology and Pathology, National Institute of Radiological Sciences, Chiba, Japan.
Sakiyama
H
H
Tokunaga
K
K
Imajoh-Ohmi
S
S
Hamada
Y
Y
Isono
K
K
Sakiyama
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002118:Calcium / Q000378:metabolism*; D006224:Cricetinae; D003412:Cricetulus; D005109:Extracellular Matrix / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011498:Protein Precursors / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism*
D011498:Protein Precursors; D011506:Proteins; D012697:Serine Endopeptidases; D002118:Calcium