Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments
Factor X in plasma is a gamma-carboxylated two-chain glycoprotein which, in activated form, plays a pivotal role in blood coagulation. We have utilized purified rat Factor X antibody, coupled to Sepharose, to isolate and characterize Factor X in rat liver, plasma, and hepatoma cells. Rat factor X is...
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Veröffentlicht in: | The Journal of biological chemistry 1982-11, Vol.257 (21), p.13108-13113 |
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container_title | The Journal of biological chemistry |
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creator | Graves, C B Munns, T W Willingham, A K Strauss, A W |
description | Factor X in plasma is a gamma-carboxylated two-chain glycoprotein which, in activated form, plays a pivotal role in blood coagulation. We have utilized purified rat Factor X antibody, coupled to Sepharose, to isolate and characterize Factor X in rat liver, plasma, and hepatoma cells. Rat factor X is synthesized as a single chain precursor (Mr = 63,000). It is this form which undergoes vitamin K-dependent carboxylation in rat liver microsomes. Only after secretion is Factor X converted into its two-chain mature form. Single chain X synthesis and secretion in hepatoma cells is enhanced by vitamin K. The amount of single chain X secreted by these cells is one-half that of prothrombin. The NH2-terminal gamma-carboxylated fragments of prothrombin which induce prothrombin synthesis (Graves, C. B., Munns, T. W., Carlisle, T. L., Grant, G. A., and Strauss, A. W. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 4772-4776) also induce single chain X synthesis by hepatoma cells. We propose that synthesis of all vitamin K-dependent proteins may be regulated by this common control mechanism. |
doi_str_mv | 10.1016/S0021-9258(18)33629-9 |
format | Article |
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We have utilized purified rat Factor X antibody, coupled to Sepharose, to isolate and characterize Factor X in rat liver, plasma, and hepatoma cells. Rat factor X is synthesized as a single chain precursor (Mr = 63,000). It is this form which undergoes vitamin K-dependent carboxylation in rat liver microsomes. Only after secretion is Factor X converted into its two-chain mature form. Single chain X synthesis and secretion in hepatoma cells is enhanced by vitamin K. The amount of single chain X secreted by these cells is one-half that of prothrombin. The NH2-terminal gamma-carboxylated fragments of prothrombin which induce prothrombin synthesis (Graves, C. B., Munns, T. W., Carlisle, T. L., Grant, G. A., and Strauss, A. W. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 4772-4776) also induce single chain X synthesis by hepatoma cells. We propose that synthesis of all vitamin K-dependent proteins may be regulated by this common control mechanism.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)33629-9</identifier><identifier>PMID: 7130196</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cell Line ; Electrophoresis, Polyacrylamide Gel ; Factor X - biosynthesis ; Factor X - isolation & purification ; Liver Neoplasms, Experimental - metabolism ; Peptide Fragments - metabolism ; Prothrombin - physiology ; Rats ; Tunicamycin - pharmacology ; Vitamin K - pharmacology</subject><ispartof>The Journal of biological chemistry, 1982-11, Vol.257 (21), p.13108-13113</ispartof><rights>1982 © 1982 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-c436t-248f857cae44f1e591d1a7bfa8c0333c38e82b42533526edd145c0b65304993e3</citedby><cites>FETCH-LOGICAL-c436t-248f857cae44f1e591d1a7bfa8c0333c38e82b42533526edd145c0b65304993e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7130196$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Graves, C B</creatorcontrib><creatorcontrib>Munns, T W</creatorcontrib><creatorcontrib>Willingham, A K</creatorcontrib><creatorcontrib>Strauss, A W</creatorcontrib><title>Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Factor X in plasma is a gamma-carboxylated two-chain glycoprotein which, in activated form, plays a pivotal role in blood coagulation. We have utilized purified rat Factor X antibody, coupled to Sepharose, to isolate and characterize Factor X in rat liver, plasma, and hepatoma cells. Rat factor X is synthesized as a single chain precursor (Mr = 63,000). It is this form which undergoes vitamin K-dependent carboxylation in rat liver microsomes. Only after secretion is Factor X converted into its two-chain mature form. Single chain X synthesis and secretion in hepatoma cells is enhanced by vitamin K. The amount of single chain X secreted by these cells is one-half that of prothrombin. The NH2-terminal gamma-carboxylated fragments of prothrombin which induce prothrombin synthesis (Graves, C. B., Munns, T. W., Carlisle, T. L., Grant, G. A., and Strauss, A. W. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 4772-4776) also induce single chain X synthesis by hepatoma cells. We propose that synthesis of all vitamin K-dependent proteins may be regulated by this common control mechanism.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Factor X - biosynthesis</subject><subject>Factor X - isolation & purification</subject><subject>Liver Neoplasms, Experimental - metabolism</subject><subject>Peptide Fragments - metabolism</subject><subject>Prothrombin - physiology</subject><subject>Rats</subject><subject>Tunicamycin - pharmacology</subject><subject>Vitamin K - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1r3DAQhkVoSTbb_oSADqWkBzcafdjSqYSQpoVAIUkh9CJkebxWWdupZKdsfn202SXX6CLQ-8xo9IiQE2BfgUF5dssYh8JwpU9BfxGi5KYwB2QBTItCKLh_RxavyBE5Tukvy0saOCSHFQgGplyQPzduoq3z0xjpPQ2Jps0wdZjCEzbUJepoCsNqjdR3Lgz0IaKfY8pwGJrZhzon9SYfj1MXx77OSBvdqsdhSh_I-9atE37c70vy-_vl3cWP4vrX1c-L8-vCS1FOBZe61aryDqVsAZWBBlxVt057JoTwQqPmteRKCMVLbBqQyrO6VCK_xQgUS_J51zdP8W_GNNk-JI_rtRtwnJOtpOCVkZBBtQN9HFOK2NqHGHoXNxaY3Tq1L07tVpgFbV-cWpPrTvYXzHWPzWvVXmLOP-3yLqy6_yGircPoO-wtV5XNDUFsP2VJvu0wzDIeA0abfMDBY5NL_GSbMbwxyDMRipId</recordid><startdate>19821110</startdate><enddate>19821110</enddate><creator>Graves, C B</creator><creator>Munns, T W</creator><creator>Willingham, A K</creator><creator>Strauss, A W</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>7X8</scope></search><sort><creationdate>19821110</creationdate><title>Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments</title><author>Graves, C B ; Munns, T W ; Willingham, A K ; Strauss, A W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c436t-248f857cae44f1e591d1a7bfa8c0333c38e82b42533526edd145c0b65304993e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Factor X - biosynthesis</topic><topic>Factor X - isolation & purification</topic><topic>Liver Neoplasms, Experimental - metabolism</topic><topic>Peptide Fragments - metabolism</topic><topic>Prothrombin - physiology</topic><topic>Rats</topic><topic>Tunicamycin - pharmacology</topic><topic>Vitamin K - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Graves, C B</creatorcontrib><creatorcontrib>Munns, T W</creatorcontrib><creatorcontrib>Willingham, A K</creatorcontrib><creatorcontrib>Strauss, A W</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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Graves, C B</au><au>Munns, T W</au><au>Willingham, A K</au><au>Strauss, A W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1982-11-10</date><risdate>1982</risdate><volume>257</volume><issue>21</issue><spage>13108</spage><epage>13113</epage><pages>13108-13113</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Factor X in plasma is a gamma-carboxylated two-chain glycoprotein which, in activated form, plays a pivotal role in blood coagulation. We have utilized purified rat Factor X antibody, coupled to Sepharose, to isolate and characterize Factor X in rat liver, plasma, and hepatoma cells. Rat factor X is synthesized as a single chain precursor (Mr = 63,000). It is this form which undergoes vitamin K-dependent carboxylation in rat liver microsomes. Only after secretion is Factor X converted into its two-chain mature form. Single chain X synthesis and secretion in hepatoma cells is enhanced by vitamin K. The amount of single chain X secreted by these cells is one-half that of prothrombin. The NH2-terminal gamma-carboxylated fragments of prothrombin which induce prothrombin synthesis (Graves, C. B., Munns, T. W., Carlisle, T. L., Grant, G. A., and Strauss, A. W. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 4772-4776) also induce single chain X synthesis by hepatoma cells. We propose that synthesis of all vitamin K-dependent proteins may be regulated by this common control mechanism.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7130196</pmid><doi>10.1016/S0021-9258(18)33629-9</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
subjects | Animals Cell Line Electrophoresis, Polyacrylamide Gel Factor X - biosynthesis Factor X - isolation & purification Liver Neoplasms, Experimental - metabolism Peptide Fragments - metabolism Prothrombin - physiology Rats Tunicamycin - pharmacology Vitamin K - pharmacology |
title | Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments |
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