Tomomura A, Akiyama M, Itoh H, Yoshino I, Tomomura M, Nishii Y, Noikura T, Saheki T
Department of Biochemistry, Faculty of Medicine, Kagoshima University, Japan.
FEBS Lett. 1996 May 13;386(1):26-8. doi: 10.1016/0014-5793(96)00377-8.
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.
