Molecular Cloning and Expression of Serum Calcium- decreasing Factor (Caldecrin) (∗)

We previously reported on the purification of a serum calcium-decreasing factor, referred to as caldecrin, from porcine pancreas, that is thought to be a serine protease (Tomomura, A., Fukushige, T., Noda, T., Noikura, T., and Saheki, T.(1992) FEBS Lett. 301, 277-281). In the present study, we purif...

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Bibliographic Details
Published in:The Journal of biological chemistry 1995-12, Vol.270 (51), p.30315-30321
Main Authors: Tomomura, Akito, Tomomura, Mineko, Fukushige, Tomoko, Akiyama, Masashi, Kubota, Naoki, Kumaki, Kenji, Nishii, Yasuho, Noikura, Takenori, Saheki, Takeyori
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Biological Assay
Bone and Bones - drug effects
Bone and Bones - metabolism
Bone Resorption
Calcium - metabolism
Cloning, Molecular
DNA Primers
DNA, Complementary
Fetus
Gene Expression
Hormone Antagonists - isolation & purification
Hormone Antagonists - pharmacology
Humans
Male
Mice
Mice, Inbred BALB C
Molecular Sequence Data
Mutagenesis, Site-Directed
Organ Culture Techniques
Organ Specificity
Pancreas - chemistry
Pancreas - metabolism
Pancreatic Elastase - biosynthesis
Peptide Fragments - chemistry
Peptide Fragments - isolation & purification
Point Mutation
Polymerase Chain Reaction
Protein Sorting Signals - biosynthesis
Rats
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - pharmacology
Sequence Homology, Amino Acid
Serine Endopeptidases - biosynthesis
Serine Endopeptidases - isolation & purification
Serine Endopeptidases - pharmacology
Swine
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Summary:We previously reported on the purification of a serum calcium-decreasing factor, referred to as caldecrin, from porcine pancreas, that is thought to be a serine protease (Tomomura, A., Fukushige, T., Noda, T., Noikura, T., and Saheki, T.(1992) FEBS Lett. 301, 277-281). In the present study, we purified caldecrin from rat pancreas and determined its primary structure by cDNA cloning. The predicted caldecrin protein is presumed to be synthesized as a preproenzyme of 268 amino acids with a signal peptide of 16 amino acids and an activation peptide of 13 amino acids, and is, with the exception of a central region, almost identical to the reported rat pancreatic elastase IV sequence. The caldecrin gene is selectively expressed in the pancreas, as judged by Northern blot analysis. After expression in BMT-10 cells, immunoreactive caldecrin was found in the culture supernatant, and it inhibited the parathyroid hormone-stimulated 45Ca release from cultured fetal long bones. Catalytic site mutants were synthesized in a baculovirus system, and recombinant mutants also decreased the serum calcium level of mice. These data implicate caldecrin, a protease closely related to elastase IV, in the regulation of blood calcium levels.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.51.30315