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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| Veröffentlicht in: | The Journal of biological chemistry 1995-12, Vol.270 (51), p.30315-30321 |
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| container_title | The Journal of biological chemistry |
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| creator | Tomomura, Akito Tomomura, Mineko Fukushige, Tomoko Akiyama, Masashi Kubota, Naoki Kumaki, Kenji Nishii, Yasuho Noikura, Takenori Saheki, Takeyori |
| description | 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. |
| doi_str_mv | 10.1074/jbc.270.51.30315 |
| format | Article |
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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.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.51.30315</identifier><identifier>PMID: 8530454</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>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</subject><ispartof>The Journal of biological chemistry, 1995-12, Vol.270 (51), p.30315-30321</ispartof><rights>1995 © 1995 ASBMB. 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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.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological Assay</subject><subject>Bone and Bones - drug effects</subject><subject>Bone and Bones - metabolism</subject><subject>Bone Resorption</subject><subject>Calcium - metabolism</subject><subject>Cloning, Molecular</subject><subject>DNA Primers</subject><subject>DNA, Complementary</subject><subject>Fetus</subject><subject>Gene Expression</subject><subject>Hormone Antagonists - isolation & purification</subject><subject>Hormone Antagonists - pharmacology</subject><subject>Humans</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Organ Culture Techniques</subject><subject>Organ Specificity</subject><subject>Pancreas - chemistry</subject><subject>Pancreas - metabolism</subject><subject>Pancreatic Elastase - biosynthesis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - isolation & purification</subject><subject>Point Mutation</subject><subject>Polymerase Chain Reaction</subject><subject>Protein Sorting Signals - biosynthesis</subject><subject>Rats</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine Endopeptidases - biosynthesis</subject><subject>Serine Endopeptidases - isolation & purification</subject><subject>Serine Endopeptidases - pharmacology</subject><subject>Swine</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM1O3DAQxy1URLe0dy6VfKgQHLL1R6zY3NAKChKIQwvqzXImE9YoiRd7A_QNeIO-H09SL7vigNS5jDT_D41-hOxxNuWsKr_f1TAVFZsqPpVMcrVFJpxpWUjFf38gE8YEL4xQ-iP5lNIdy1MavkN2tJKsVOWE3FyGDmHsXKSzLgx-uKVuaOjJ0yJiSj4MNLT0J8axpzPXgR_7gjYIEV1aeU8dLEOkB1lbXf1wSA9env8efibbresSftnsXXJ9evJrdlZcXP04nx1fFKC4XBZGllJACaYyYLCsnRBGo9BZFVlr2xpBCa0BV98qjZWCWjPjEJhyTMldsr_uXcRwP2Ja2t4nwK5zA4YxWV4xoYwU2cjWRoghpYitXUTfu_jHcmZXKG1GaTNKq7h9RZkjXzfdY91j8xbYsMv6t7U-97fzRx_R1j7AHPv3NUdrG2YODx6jTeBxAGxyBJa2Cf7_P_wDHX2NzA</recordid><startdate>19951222</startdate><enddate>19951222</enddate><creator>Tomomura, Akito</creator><creator>Tomomura, Mineko</creator><creator>Fukushige, Tomoko</creator><creator>Akiyama, Masashi</creator><creator>Kubota, Naoki</creator><creator>Kumaki, Kenji</creator><creator>Nishii, Yasuho</creator><creator>Noikura, Takenori</creator><creator>Saheki, Takeyori</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19951222</creationdate><title>Molecular Cloning and Expression of Serum Calcium- decreasing Factor (Caldecrin) (∗)</title><author>Tomomura, Akito ; Tomomura, Mineko ; Fukushige, Tomoko ; Akiyama, Masashi ; Kubota, Naoki ; Kumaki, Kenji ; Nishii, Yasuho ; Noikura, Takenori ; Saheki, Takeyori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c513t-93432c4c979c9e4ba2298e28c512934ffbec5288ce045458e75cb809aec05a053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological Assay</topic><topic>Bone and Bones - drug effects</topic><topic>Bone and Bones - metabolism</topic><topic>Bone Resorption</topic><topic>Calcium - metabolism</topic><topic>Cloning, Molecular</topic><topic>DNA Primers</topic><topic>DNA, Complementary</topic><topic>Fetus</topic><topic>Gene Expression</topic><topic>Hormone Antagonists - isolation & purification</topic><topic>Hormone Antagonists - pharmacology</topic><topic>Humans</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Organ Culture Techniques</topic><topic>Organ Specificity</topic><topic>Pancreas - chemistry</topic><topic>Pancreas - metabolism</topic><topic>Pancreatic Elastase - biosynthesis</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - isolation & purification</topic><topic>Point Mutation</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Sorting Signals - biosynthesis</topic><topic>Rats</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine Endopeptidases - biosynthesis</topic><topic>Serine Endopeptidases - isolation & purification</topic><topic>Serine Endopeptidases - pharmacology</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tomomura, Akito</creatorcontrib><creatorcontrib>Tomomura, Mineko</creatorcontrib><creatorcontrib>Fukushige, Tomoko</creatorcontrib><creatorcontrib>Akiyama, Masashi</creatorcontrib><creatorcontrib>Kubota, Naoki</creatorcontrib><creatorcontrib>Kumaki, Kenji</creatorcontrib><creatorcontrib>Nishii, Yasuho</creatorcontrib><creatorcontrib>Noikura, Takenori</creatorcontrib><creatorcontrib>Saheki, Takeyori</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tomomura, Akito</au><au>Tomomura, Mineko</au><au>Fukushige, Tomoko</au><au>Akiyama, Masashi</au><au>Kubota, Naoki</au><au>Kumaki, Kenji</au><au>Nishii, Yasuho</au><au>Noikura, Takenori</au><au>Saheki, Takeyori</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Cloning and Expression of Serum Calcium- decreasing Factor (Caldecrin) (∗)</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-12-22</date><risdate>1995</risdate><volume>270</volume><issue>51</issue><spage>30315</spage><epage>30321</epage><pages>30315-30321</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8530454</pmid><doi>10.1074/jbc.270.51.30315</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1995-12, Vol.270 (51), p.30315-30321 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| 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 |
| title | Molecular Cloning and Expression of Serum Calcium- decreasing Factor (Caldecrin) (∗) |
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