The ATP-Mg/Pi carrier of rat liver mitochondria catalyzes a divalent electroneutral exchange
Net transport of ATP-Mg or ADP in exchange for phosphate in isolated rat liver mitochondria has been shown to be an electroneutral process mediated by the ATP-Mg/Pi carrier. We compared the steady state distribution ratios of phosphate, ATP-Mg, and ADP at a pH of 7.4 to determine whether the divalen...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-09, Vol.267 (27), p.19198-19203 |
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| creator | JOYAL, J. L APRILLE, J. R |
| description | Net transport of ATP-Mg or ADP in exchange for phosphate in isolated rat liver mitochondria has been shown to be an electroneutral
process mediated by the ATP-Mg/Pi carrier. We compared the steady state distribution ratios of phosphate, ATP-Mg, and ADP
at a pH of 7.4 to determine whether the divalent or monovalent form of these anions is the transported substrate. The log
of the divalent ATP-Mg distribution ratio (in/out) approached the log of the divalent phosphate distribution ratio (approximately
0.85), which was approximately twice the value of the delta pH (approximately 0.40) across the inner mitochondrial membrane.
This steady state relationship held under several different conditions, e.g. when the medium ATP concentration was varied
or if the phosphate gradient was modified by partial uncoupling with the proton ionophore, carbonyl cyanide p-trifluoromethoxyphenylhydrazone.
Unidirectional ADP efflux in exchange for external ADP or ATP-Mg was stimulated by an increase in matrix H+. The log of the
trivalent ADP distribution ratio (approximately 1.20) approached 3 times the value of delta pH. All these data are consistent
with the model of an electroneutral exchange of divalent phosphate (HPO2-4) for divalent ATP-Mg (ATP-Mg2-) or for divalent
protonated ADP (HADP2-). We conclude that this transport mechanism accounts for the adenine nucleotide concentration gradient
that normally exists between the matrix and external medium. |
| doi_str_mv | 10.1016/S0021-9258(18)41761-9 |
| format | Article |
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process mediated by the ATP-Mg/Pi carrier. We compared the steady state distribution ratios of phosphate, ATP-Mg, and ADP
at a pH of 7.4 to determine whether the divalent or monovalent form of these anions is the transported substrate. The log
of the divalent ATP-Mg distribution ratio (in/out) approached the log of the divalent phosphate distribution ratio (approximately
0.85), which was approximately twice the value of the delta pH (approximately 0.40) across the inner mitochondrial membrane.
This steady state relationship held under several different conditions, e.g. when the medium ATP concentration was varied
or if the phosphate gradient was modified by partial uncoupling with the proton ionophore, carbonyl cyanide p-trifluoromethoxyphenylhydrazone.
Unidirectional ADP efflux in exchange for external ADP or ATP-Mg was stimulated by an increase in matrix H+. The log of the
trivalent ADP distribution ratio (approximately 1.20) approached 3 times the value of delta pH. All these data are consistent
with the model of an electroneutral exchange of divalent phosphate (HPO2-4) for divalent ATP-Mg (ATP-Mg2-) or for divalent
protonated ADP (HADP2-). We conclude that this transport mechanism accounts for the adenine nucleotide concentration gradient
that normally exists between the matrix and external medium.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)41761-9</identifier><identifier>PMID: 1527042</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; Antiporters ; Biological and medical sciences ; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone - pharmacology ; Carrier Proteins - metabolism ; Cell Compartmentation ; Cell physiology ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Intracellular Membranes - metabolism ; Ions ; Membrane and intracellular transports ; Membrane Potentials ; Mitochondria, Liver - metabolism ; Mitochondrial Proteins ; Molecular and cellular biology ; Phosphates - metabolism ; Rats</subject><ispartof>The Journal of biological chemistry, 1992-09, Vol.267 (27), p.19198-19203</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-b0c565a460efb134d443066558636c24e14d5ebaf266dde3ae7f2b9a07d4e1643</citedby><cites>FETCH-LOGICAL-c409t-b0c565a460efb134d443066558636c24e14d5ebaf266dde3ae7f2b9a07d4e1643</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4332139$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1527042$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>JOYAL, J. L</creatorcontrib><creatorcontrib>APRILLE, J. R</creatorcontrib><title>The ATP-Mg/Pi carrier of rat liver mitochondria catalyzes a divalent electroneutral exchange</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Net transport of ATP-Mg or ADP in exchange for phosphate in isolated rat liver mitochondria has been shown to be an electroneutral
process mediated by the ATP-Mg/Pi carrier. We compared the steady state distribution ratios of phosphate, ATP-Mg, and ADP
at a pH of 7.4 to determine whether the divalent or monovalent form of these anions is the transported substrate. The log
of the divalent ATP-Mg distribution ratio (in/out) approached the log of the divalent phosphate distribution ratio (approximately
0.85), which was approximately twice the value of the delta pH (approximately 0.40) across the inner mitochondrial membrane.
This steady state relationship held under several different conditions, e.g. when the medium ATP concentration was varied
or if the phosphate gradient was modified by partial uncoupling with the proton ionophore, carbonyl cyanide p-trifluoromethoxyphenylhydrazone.
Unidirectional ADP efflux in exchange for external ADP or ATP-Mg was stimulated by an increase in matrix H+. The log of the
trivalent ADP distribution ratio (approximately 1.20) approached 3 times the value of delta pH. All these data are consistent
with the model of an electroneutral exchange of divalent phosphate (HPO2-4) for divalent ATP-Mg (ATP-Mg2-) or for divalent
protonated ADP (HADP2-). We conclude that this transport mechanism accounts for the adenine nucleotide concentration gradient
that normally exists between the matrix and external medium.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Antiporters</subject><subject>Biological and medical sciences</subject><subject>Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone - pharmacology</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Compartmentation</subject><subject>Cell physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Intracellular Membranes - metabolism</subject><subject>Ions</subject><subject>Membrane and intracellular transports</subject><subject>Membrane Potentials</subject><subject>Mitochondria, Liver - metabolism</subject><subject>Mitochondrial Proteins</subject><subject>Molecular and cellular biology</subject><subject>Phosphates - metabolism</subject><subject>Rats</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1r3DAQhkVpSLdpf0JAh1LagxONvmwdQ0g_ICWBbKGHgpDl8VpFtlPJmzb99VWySzKXYXifmYGHkGNgJ8BAn94wxqEyXDUfoPkoodZlekFWwBpRCQU_XpLVE_KKvM75FyslDRySQ1C8ZpKvyM_1gPRsfV1925xeB-pdSgETnXua3EJjuCvDGJbZD_PUpeAKsbh4_w8zdbQLdy7itFCM6Jc0T7hdkosU__rBTRt8Qw56FzO-3fcj8v3Txfr8S3V59fnr-dll5SUzS9Uyr7RyUjPsWxCyk1IwrZVqtNCeSwTZKWxdz7XuOhQO6563xrG6K5mW4oi83929TfPvLebFjiF7jNFNOG-zrQUYUY4WUO1An-acE_b2NoXRpXsLzD5YtY9W7YMyC419tGpN2TveP9i2I3bPWzuNJX-3z132LvbJTT7kJ6x85iDMMzaEzfAnJLRtKGZxtFzXltcWDJhG_AfPG4s5</recordid><startdate>19920925</startdate><enddate>19920925</enddate><creator>JOYAL, J. L</creator><creator>APRILLE, J. R</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>19920925</creationdate><title>The ATP-Mg/Pi carrier of rat liver mitochondria catalyzes a divalent electroneutral exchange</title><author>JOYAL, J. L ; APRILLE, J. R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-b0c565a460efb134d443066558636c24e14d5ebaf266dde3ae7f2b9a07d4e1643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Antiporters</topic><topic>Biological and medical sciences</topic><topic>Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone - pharmacology</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Compartmentation</topic><topic>Cell physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Intracellular Membranes - metabolism</topic><topic>Ions</topic><topic>Membrane and intracellular transports</topic><topic>Membrane Potentials</topic><topic>Mitochondria, Liver - metabolism</topic><topic>Mitochondrial Proteins</topic><topic>Molecular and cellular biology</topic><topic>Phosphates - metabolism</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>JOYAL, J. L</creatorcontrib><creatorcontrib>APRILLE, J. R</creatorcontrib><collection>Pascal-Francis</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>JOYAL, J. L</au><au>APRILLE, J. R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ATP-Mg/Pi carrier of rat liver mitochondria catalyzes a divalent electroneutral exchange</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-09-25</date><risdate>1992</risdate><volume>267</volume><issue>27</issue><spage>19198</spage><epage>19203</epage><pages>19198-19203</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Net transport of ATP-Mg or ADP in exchange for phosphate in isolated rat liver mitochondria has been shown to be an electroneutral
process mediated by the ATP-Mg/Pi carrier. We compared the steady state distribution ratios of phosphate, ATP-Mg, and ADP
at a pH of 7.4 to determine whether the divalent or monovalent form of these anions is the transported substrate. The log
of the divalent ATP-Mg distribution ratio (in/out) approached the log of the divalent phosphate distribution ratio (approximately
0.85), which was approximately twice the value of the delta pH (approximately 0.40) across the inner mitochondrial membrane.
This steady state relationship held under several different conditions, e.g. when the medium ATP concentration was varied
or if the phosphate gradient was modified by partial uncoupling with the proton ionophore, carbonyl cyanide p-trifluoromethoxyphenylhydrazone.
Unidirectional ADP efflux in exchange for external ADP or ATP-Mg was stimulated by an increase in matrix H+. The log of the
trivalent ADP distribution ratio (approximately 1.20) approached 3 times the value of delta pH. All these data are consistent
with the model of an electroneutral exchange of divalent phosphate (HPO2-4) for divalent ATP-Mg (ATP-Mg2-) or for divalent
protonated ADP (HADP2-). We conclude that this transport mechanism accounts for the adenine nucleotide concentration gradient
that normally exists between the matrix and external medium.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1527042</pmid><doi>10.1016/S0021-9258(18)41761-9</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-09, Vol.267 (27), p.19198-19203 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73193443 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Adenosine Triphosphate - metabolism Animals Antiporters Biological and medical sciences Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone - pharmacology Carrier Proteins - metabolism Cell Compartmentation Cell physiology Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Intracellular Membranes - metabolism Ions Membrane and intracellular transports Membrane Potentials Mitochondria, Liver - metabolism Mitochondrial Proteins Molecular and cellular biology Phosphates - metabolism Rats |
| title | The ATP-Mg/Pi carrier of rat liver mitochondria catalyzes a divalent electroneutral exchange |
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