Protective effect of magnesium and potassium ions on the permeability of the external mitochondrial membrane
The data reported are fully consistent with the well-known observation that exogenous cytochrome c (cyto- c) molecules do not permeate through the outer membrane of mitochondria (MOM) incubated in isotonic medium (250 mM sucrose). Cyto- c is unable to accept electrons from the sulfite/cyto- c oxido-...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2007-05, Vol.461 (1), p.13-23 |
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| creator | Gorgoglione, Vincenza Laraspata, Daniela La Piana, Gianluigi Marzulli, Domenico Lofrumento, Nicola Elio |
| description | The data reported are fully consistent with the well-known observation that exogenous cytochrome
c (cyto-
c) molecules do not permeate through the outer membrane of mitochondria (MOM) incubated in isotonic medium (250
mM sucrose). Cyto-
c is unable to accept electrons from the sulfite/cyto-
c oxido-reductase (Sox) present in the intermembrane space, unless mitochondria are solubilized. Mitochondria incubated in a very high hypotonic medium (25
mM sucrose), in contrast to any expectation, continue to be not permeable to added cyto-
c even if Sox and adenylate kinase are released into the medium. The succinate/exogenous cyto-
c reductase activity, very low in isotonic medium, is greatly increased decreasing the osmolarity of the medium but in both cases remains insensitive to proteolysis by added trypsin. In hypotonic medium, magnesium and potassium ions have a protective effect on the release of enzymes and on the reactivity of cyto-
c as electron acceptor from both sulfite and succinate; results which are consistent with the view that MOM preserves its identity and remains not permeable to exogenous cyto-
c. This report strengthens the proposal, supported by previously published data that in isotonic medium the exogenous NADH/cyto-
c electron transport system is catalyzed by intact mitochondria, not permeable to added cyto-
c. |
| doi_str_mv | 10.1016/j.abb.2007.01.007 |
| format | Article |
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c (cyto-
c) molecules do not permeate through the outer membrane of mitochondria (MOM) incubated in isotonic medium (250
mM sucrose). Cyto-
c is unable to accept electrons from the sulfite/cyto-
c oxido-reductase (Sox) present in the intermembrane space, unless mitochondria are solubilized. Mitochondria incubated in a very high hypotonic medium (25
mM sucrose), in contrast to any expectation, continue to be not permeable to added cyto-
c even if Sox and adenylate kinase are released into the medium. The succinate/exogenous cyto-
c reductase activity, very low in isotonic medium, is greatly increased decreasing the osmolarity of the medium but in both cases remains insensitive to proteolysis by added trypsin. In hypotonic medium, magnesium and potassium ions have a protective effect on the release of enzymes and on the reactivity of cyto-
c as electron acceptor from both sulfite and succinate; results which are consistent with the view that MOM preserves its identity and remains not permeable to exogenous cyto-
c. This report strengthens the proposal, supported by previously published data that in isotonic medium the exogenous NADH/cyto-
c electron transport system is catalyzed by intact mitochondria, not permeable to added cyto-
c.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2007.01.007</identifier><identifier>PMID: 17320039</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenylate kinase ; Animals ; Biological Transport - physiology ; Cations, Divalent ; Cations, Monovalent ; Contact sites ; Cytochrome c ; Cytochromes c - metabolism ; Cytosolic NADH oxidation ; Horses ; Magnesium - physiology ; Mitochondria ; Mitochondria, Liver - enzymology ; Mitochondria, Liver - metabolism ; Mitochondrial Membranes - enzymology ; Mitochondrial Membranes - metabolism ; Mitochondrial membranes permeability ; Permeability ; Potassium - physiology ; Rats ; Respiratory chain ; Succinate/cytochrome- c reductase ; Sulfite oxidase</subject><ispartof>Archives of biochemistry and biophysics, 2007-05, Vol.461 (1), p.13-23</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c351t-e2786051163f2263df0465b809b09d8b5398926fbc3c4601b9e4f274950a20fe3</citedby><cites>FETCH-LOGICAL-c351t-e2786051163f2263df0465b809b09d8b5398926fbc3c4601b9e4f274950a20fe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0003986107000185$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17320039$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gorgoglione, Vincenza</creatorcontrib><creatorcontrib>Laraspata, Daniela</creatorcontrib><creatorcontrib>La Piana, Gianluigi</creatorcontrib><creatorcontrib>Marzulli, Domenico</creatorcontrib><creatorcontrib>Lofrumento, Nicola Elio</creatorcontrib><title>Protective effect of magnesium and potassium ions on the permeability of the external mitochondrial membrane</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The data reported are fully consistent with the well-known observation that exogenous cytochrome
c (cyto-
c) molecules do not permeate through the outer membrane of mitochondria (MOM) incubated in isotonic medium (250
mM sucrose). Cyto-
c is unable to accept electrons from the sulfite/cyto-
c oxido-reductase (Sox) present in the intermembrane space, unless mitochondria are solubilized. Mitochondria incubated in a very high hypotonic medium (25
mM sucrose), in contrast to any expectation, continue to be not permeable to added cyto-
c even if Sox and adenylate kinase are released into the medium. The succinate/exogenous cyto-
c reductase activity, very low in isotonic medium, is greatly increased decreasing the osmolarity of the medium but in both cases remains insensitive to proteolysis by added trypsin. In hypotonic medium, magnesium and potassium ions have a protective effect on the release of enzymes and on the reactivity of cyto-
c as electron acceptor from both sulfite and succinate; results which are consistent with the view that MOM preserves its identity and remains not permeable to exogenous cyto-
c. This report strengthens the proposal, supported by previously published data that in isotonic medium the exogenous NADH/cyto-
c electron transport system is catalyzed by intact mitochondria, not permeable to added cyto-
c.</description><subject>Adenylate kinase</subject><subject>Animals</subject><subject>Biological Transport - physiology</subject><subject>Cations, Divalent</subject><subject>Cations, Monovalent</subject><subject>Contact sites</subject><subject>Cytochrome c</subject><subject>Cytochromes c - metabolism</subject><subject>Cytosolic NADH oxidation</subject><subject>Horses</subject><subject>Magnesium - physiology</subject><subject>Mitochondria</subject><subject>Mitochondria, Liver - enzymology</subject><subject>Mitochondria, Liver - metabolism</subject><subject>Mitochondrial Membranes - enzymology</subject><subject>Mitochondrial Membranes - metabolism</subject><subject>Mitochondrial membranes permeability</subject><subject>Permeability</subject><subject>Potassium - physiology</subject><subject>Rats</subject><subject>Respiratory chain</subject><subject>Succinate/cytochrome- c reductase</subject><subject>Sulfite oxidase</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEFP3DAQhS3UqizQH9BL5VNvCeM4cWL1VCFokZDgUM6W7YzBqyTe2l4E_x6nu1JvPb2Z0XtP9kfIFwY1AyYut7U2pm4A-hpYXeSEbBhIUQEf2g9kAwC8koNgp-QspS0AY61oPpFT1vOS4nJDpocYMtrsX5Cic2WiwdFZPy2Y_H6mehnpLmSd_m4-LImGheZnpDuMM2rjJ5_f1sx6w9eMcdETnX0O9jksY_TrhrOJesEL8tHpKeHno56Tx5vr31e_qrv7n7dXP-4qyzuWK2z6QUDHmOCuaQQfHbSiMwNIA3IcTMflIBvhjOW2FcCMxNY1fSs70A045Ofk26F3F8OfPaasZp8sTlN5Q9gn1UPbAnRDMbKD0caQUkSndtHPOr4pBmpFrLaqIFYrYgVMFSmZr8fyvZlx_Jc4Mi2G7wcDli--eIwqWY-LxdHHwleNwf-n_h21PYyf</recordid><startdate>20070501</startdate><enddate>20070501</enddate><creator>Gorgoglione, Vincenza</creator><creator>Laraspata, Daniela</creator><creator>La Piana, Gianluigi</creator><creator>Marzulli, Domenico</creator><creator>Lofrumento, Nicola Elio</creator><general>Elsevier Inc</general><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>20070501</creationdate><title>Protective effect of magnesium and potassium ions on the permeability of the external mitochondrial membrane</title><author>Gorgoglione, Vincenza ; Laraspata, Daniela ; La Piana, Gianluigi ; Marzulli, Domenico ; Lofrumento, Nicola Elio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-e2786051163f2263df0465b809b09d8b5398926fbc3c4601b9e4f274950a20fe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adenylate kinase</topic><topic>Animals</topic><topic>Biological Transport - physiology</topic><topic>Cations, Divalent</topic><topic>Cations, Monovalent</topic><topic>Contact sites</topic><topic>Cytochrome c</topic><topic>Cytochromes c - metabolism</topic><topic>Cytosolic NADH oxidation</topic><topic>Horses</topic><topic>Magnesium - physiology</topic><topic>Mitochondria</topic><topic>Mitochondria, Liver - enzymology</topic><topic>Mitochondria, Liver - metabolism</topic><topic>Mitochondrial Membranes - enzymology</topic><topic>Mitochondrial Membranes - metabolism</topic><topic>Mitochondrial membranes permeability</topic><topic>Permeability</topic><topic>Potassium - physiology</topic><topic>Rats</topic><topic>Respiratory chain</topic><topic>Succinate/cytochrome- c reductase</topic><topic>Sulfite oxidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gorgoglione, Vincenza</creatorcontrib><creatorcontrib>Laraspata, Daniela</creatorcontrib><creatorcontrib>La Piana, Gianluigi</creatorcontrib><creatorcontrib>Marzulli, Domenico</creatorcontrib><creatorcontrib>Lofrumento, Nicola Elio</creatorcontrib><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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gorgoglione, Vincenza</au><au>Laraspata, Daniela</au><au>La Piana, Gianluigi</au><au>Marzulli, Domenico</au><au>Lofrumento, Nicola Elio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protective effect of magnesium and potassium ions on the permeability of the external mitochondrial membrane</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2007-05-01</date><risdate>2007</risdate><volume>461</volume><issue>1</issue><spage>13</spage><epage>23</epage><pages>13-23</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The data reported are fully consistent with the well-known observation that exogenous cytochrome
c (cyto-
c) molecules do not permeate through the outer membrane of mitochondria (MOM) incubated in isotonic medium (250
mM sucrose). Cyto-
c is unable to accept electrons from the sulfite/cyto-
c oxido-reductase (Sox) present in the intermembrane space, unless mitochondria are solubilized. Mitochondria incubated in a very high hypotonic medium (25
mM sucrose), in contrast to any expectation, continue to be not permeable to added cyto-
c even if Sox and adenylate kinase are released into the medium. The succinate/exogenous cyto-
c reductase activity, very low in isotonic medium, is greatly increased decreasing the osmolarity of the medium but in both cases remains insensitive to proteolysis by added trypsin. In hypotonic medium, magnesium and potassium ions have a protective effect on the release of enzymes and on the reactivity of cyto-
c as electron acceptor from both sulfite and succinate; results which are consistent with the view that MOM preserves its identity and remains not permeable to exogenous cyto-
c. This report strengthens the proposal, supported by previously published data that in isotonic medium the exogenous NADH/cyto-
c electron transport system is catalyzed by intact mitochondria, not permeable to added cyto-
c.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17320039</pmid><doi>10.1016/j.abb.2007.01.007</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 2007-05, Vol.461 (1), p.13-23 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70440058 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenylate kinase Animals Biological Transport - physiology Cations, Divalent Cations, Monovalent Contact sites Cytochrome c Cytochromes c - metabolism Cytosolic NADH oxidation Horses Magnesium - physiology Mitochondria Mitochondria, Liver - enzymology Mitochondria, Liver - metabolism Mitochondrial Membranes - enzymology Mitochondrial Membranes - metabolism Mitochondrial membranes permeability Permeability Potassium - physiology Rats Respiratory chain Succinate/cytochrome- c reductase Sulfite oxidase |
| title | Protective effect of magnesium and potassium ions on the permeability of the external mitochondrial membrane |
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