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Molecular cloning and expression of human caldecrin
Author(s) -
Tomomura Akito,
Akiyama Masashi,
Itoh Hirotaka,
Yoshino Izumi,
Tomomura Mineko,
Nishii Yasuho,
Noikura Takenori,
Saheki Takeyori
Publication year - 1996
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(96)00377-8
Subject(s) - amino acid , protease , complementary dna , biochemistry , chymotrypsin , recombinant dna , signal peptide , pmsf , microbiology and biotechnology , chemistry , protein primary structure , peptide sequence , biological activity , molecular cloning , biology , trypsin , enzyme , gene , in vitro
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.