Purification, cDNA Cloning, and Characterization of a New Serpin with Megakaryocyte Maturation Activity
A new member of the serine protease inhibitor (serpin) superfamily with megakaryocyte maturation activity was purified, and its cDNA was cloned and characterized. The predicted amino acid sequence consisting of 380 residues was unique and was 38% identical to the serpin plasminogen activator inhibit...
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| Veröffentlicht in: | The Journal of biological chemistry 1997-06, Vol.272 (24), p.15373-15380 |
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| creator | Tsujimoto, Masafumi Tsuruoka, Nobuo Ishida, Nobuhiro Kurihara, Tatsuya Iwasa, Fuyuki Yamashiro, Kyoko Rogi, Tomohiro Kodama, Shiho Katsuragi, Naruto Adachi, Mayumi Katayama, Toyoko Nakao, Masahiro Yamaichi, Kozo Hashino, Junko Haruyama, Munetada Miura, Kenju Nakanishi, Toshihiro Nakazato, Hiroshi Teramura, Masanao Mizoguchi, Hideaki Yamaguchi, Nozomi |
| description | A new member of the serine protease inhibitor (serpin) superfamily with megakaryocyte maturation activity was purified, and its cDNA was cloned and characterized. The predicted amino acid sequence consisting of 380 residues was unique and was 38% identical to the serpin plasminogen activator inhibitor type 2 (PAI-2). The recombinant factor expressed in Chinese hamster ovary cells showed species-specific activity on the induction of megakaryocyte maturationin vitro. When injected into mice, the factor indeed elicited an increase in the number of platelets in plasma. The sequence alignment indicated that the factor possessed a lysine residue at the P1 position, suggesting that it might function as an inhibitor of Lys-specific proteases. Although we could not show any inhibitory activities toward several known Lys-specific proteases, we detected the activity toward protease activity present in the culture supernatant of COLO 201 cells. These results suggested that the protein might influence the maturation of megakaryocytes via action as a serpin. |
| doi_str_mv | 10.1074/jbc.272.24.15373 |
| format | Article |
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The predicted amino acid sequence consisting of 380 residues was unique and was 38% identical to the serpin plasminogen activator inhibitor type 2 (PAI-2). The recombinant factor expressed in Chinese hamster ovary cells showed species-specific activity on the induction of megakaryocyte maturationin vitro. When injected into mice, the factor indeed elicited an increase in the number of platelets in plasma. The sequence alignment indicated that the factor possessed a lysine residue at the P1 position, suggesting that it might function as an inhibitor of Lys-specific proteases. Although we could not show any inhibitory activities toward several known Lys-specific proteases, we detected the activity toward protease activity present in the culture supernatant of COLO 201 cells. These results suggested that the protein might influence the maturation of megakaryocytes via action as a serpin.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.272.24.15373</identifier><identifier>PMID: 9182567</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; CHO Cells ; Chromatography, Gel ; Chromatography, Ion Exchange ; Cloning, Molecular ; Cricetinae ; Culture Media, Conditioned ; DNA, Complementary ; GPI-Linked Proteins ; Humans ; Membrane Glycoproteins ; Mice ; Molecular Sequence Data ; Proteins - genetics ; Proteins - isolation & purification ; Sequence Homology, Amino Acid ; Serpins - genetics ; Serpins - isolation & purification</subject><ispartof>The Journal of biological chemistry, 1997-06, Vol.272 (24), p.15373-15380</ispartof><rights>1997 © 1997 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-b721eac35035631d7a50efaa0fb4f4c33e3fe1ffe0208db1837a117ddc029faf3</citedby><cites>FETCH-LOGICAL-c447t-b721eac35035631d7a50efaa0fb4f4c33e3fe1ffe0208db1837a117ddc029faf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9182567$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsujimoto, Masafumi</creatorcontrib><creatorcontrib>Tsuruoka, Nobuo</creatorcontrib><creatorcontrib>Ishida, Nobuhiro</creatorcontrib><creatorcontrib>Kurihara, Tatsuya</creatorcontrib><creatorcontrib>Iwasa, Fuyuki</creatorcontrib><creatorcontrib>Yamashiro, Kyoko</creatorcontrib><creatorcontrib>Rogi, Tomohiro</creatorcontrib><creatorcontrib>Kodama, Shiho</creatorcontrib><creatorcontrib>Katsuragi, Naruto</creatorcontrib><creatorcontrib>Adachi, Mayumi</creatorcontrib><creatorcontrib>Katayama, Toyoko</creatorcontrib><creatorcontrib>Nakao, Masahiro</creatorcontrib><creatorcontrib>Yamaichi, Kozo</creatorcontrib><creatorcontrib>Hashino, Junko</creatorcontrib><creatorcontrib>Haruyama, Munetada</creatorcontrib><creatorcontrib>Miura, Kenju</creatorcontrib><creatorcontrib>Nakanishi, Toshihiro</creatorcontrib><creatorcontrib>Nakazato, Hiroshi</creatorcontrib><creatorcontrib>Teramura, Masanao</creatorcontrib><creatorcontrib>Mizoguchi, Hideaki</creatorcontrib><creatorcontrib>Yamaguchi, Nozomi</creatorcontrib><title>Purification, cDNA Cloning, and Characterization of a New Serpin with Megakaryocyte Maturation Activity</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A new member of the serine protease inhibitor (serpin) superfamily with megakaryocyte maturation activity was purified, and its cDNA was cloned and characterized. The predicted amino acid sequence consisting of 380 residues was unique and was 38% identical to the serpin plasminogen activator inhibitor type 2 (PAI-2). The recombinant factor expressed in Chinese hamster ovary cells showed species-specific activity on the induction of megakaryocyte maturationin vitro. When injected into mice, the factor indeed elicited an increase in the number of platelets in plasma. The sequence alignment indicated that the factor possessed a lysine residue at the P1 position, suggesting that it might function as an inhibitor of Lys-specific proteases. Although we could not show any inhibitory activities toward several known Lys-specific proteases, we detected the activity toward protease activity present in the culture supernatant of COLO 201 cells. These results suggested that the protein might influence the maturation of megakaryocytes via action as a serpin.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>CHO Cells</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Cloning, Molecular</subject><subject>Cricetinae</subject><subject>Culture Media, Conditioned</subject><subject>DNA, Complementary</subject><subject>GPI-Linked Proteins</subject><subject>Humans</subject><subject>Membrane Glycoproteins</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Proteins - genetics</subject><subject>Proteins - isolation & purification</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serpins - genetics</subject><subject>Serpins - isolation & purification</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1vEzEQxS0EKqFw54LkA-LUDR57N97lFoWPIrUFCZC4WV7vOOuSrIPtbZT-9bjdqAckxFzmML_3NDOPkJfA5sBk-fa6NXMu-ZyXc6iEFI_IDFgtClHBz8dkxhiHouFV_ZQ8i_Ga5SobOCEnDdS8WsgZWX8dg7PO6OT8cEbN-6slXW384Ib1GdVDR1e9DtokDO72nqHeUk2vcE-_Ydi5ge5d6uklrvUvHQ7eHBLSS53GMNFLk9yNS4fn5InVm4gvjv2U_Pj44fvqvLj48unzanlRmLKUqWglB9RGVExUCwGd1BVDqzWzbWlLIwQKi2AtMs7qroVaSA0gu84w3lhtxSl5M_nugv89Ykxq66LBzUYP6MeoZMMq3tTwXxAWjJdQswyyCTTBxxjQql1w23yrAqbuQlA5BJVDULxU9yFkyauj99husXsQHL-e56-nee_W_d4FVK3zpsft3zbvJgzzw24cBhWNw8FglyUmqc67f-_wB1SUouA</recordid><startdate>19970613</startdate><enddate>19970613</enddate><creator>Tsujimoto, Masafumi</creator><creator>Tsuruoka, Nobuo</creator><creator>Ishida, Nobuhiro</creator><creator>Kurihara, Tatsuya</creator><creator>Iwasa, Fuyuki</creator><creator>Yamashiro, Kyoko</creator><creator>Rogi, Tomohiro</creator><creator>Kodama, Shiho</creator><creator>Katsuragi, Naruto</creator><creator>Adachi, Mayumi</creator><creator>Katayama, Toyoko</creator><creator>Nakao, Masahiro</creator><creator>Yamaichi, Kozo</creator><creator>Hashino, Junko</creator><creator>Haruyama, Munetada</creator><creator>Miura, Kenju</creator><creator>Nakanishi, Toshihiro</creator><creator>Nakazato, Hiroshi</creator><creator>Teramura, Masanao</creator><creator>Mizoguchi, Hideaki</creator><creator>Yamaguchi, Nozomi</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19970613</creationdate><title>Purification, cDNA Cloning, and Characterization of a New Serpin with Megakaryocyte Maturation Activity</title><author>Tsujimoto, Masafumi ; 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The predicted amino acid sequence consisting of 380 residues was unique and was 38% identical to the serpin plasminogen activator inhibitor type 2 (PAI-2). The recombinant factor expressed in Chinese hamster ovary cells showed species-specific activity on the induction of megakaryocyte maturationin vitro. When injected into mice, the factor indeed elicited an increase in the number of platelets in plasma. The sequence alignment indicated that the factor possessed a lysine residue at the P1 position, suggesting that it might function as an inhibitor of Lys-specific proteases. Although we could not show any inhibitory activities toward several known Lys-specific proteases, we detected the activity toward protease activity present in the culture supernatant of COLO 201 cells. These results suggested that the protein might influence the maturation of megakaryocytes via action as a serpin.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9182567</pmid><doi>10.1074/jbc.272.24.15373</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1997-06, Vol.272 (24), p.15373-15380 |
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| subjects | Amino Acid Sequence Animals Base Sequence CHO Cells Chromatography, Gel Chromatography, Ion Exchange Cloning, Molecular Cricetinae Culture Media, Conditioned DNA, Complementary GPI-Linked Proteins Humans Membrane Glycoproteins Mice Molecular Sequence Data Proteins - genetics Proteins - isolation & purification Sequence Homology, Amino Acid Serpins - genetics Serpins - isolation & purification |
| title | Purification, cDNA Cloning, and Characterization of a New Serpin with Megakaryocyte Maturation Activity |
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