Effects of Lipids on ATPase Activity of Purified Chinese Hamster P-Glycoprotein
Chinese hamster P-glycoprotein ("multidrug-resistance protein") was purified and reconstituted in proteoliposomes by the procedure of I. L. Urbatsch, M. K. Al-Shawl, and A. E. Senior (1994, Biochemistry 33, 7069-7076). The presence of lipid during the octylglucoside solubilization and Reac...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1995-01, Vol.316 (1), p.135-140 |
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| creator | Urbatsch, I.L. Senior, A.E. |
| description | Chinese hamster P-glycoprotein ("multidrug-resistance protein") was purified and reconstituted in proteoliposomes by the procedure of I. L. Urbatsch, M. K. Al-Shawl, and A. E. Senior (1994, Biochemistry 33, 7069-7076). The presence of lipid during the octylglucoside solubilization and Reactive Red 120 chromatography steps was found to be mandatory for retention of ATPase activity. Sheep brain or bovine liver lipid extracts could be substituted for the Escherichia coli lipids used previously, Stimulation of ATPase activity of purified, reconstituted P-glycoprotein by vinblastine, colchicine, and daunomycin was seen with sheep brain and bovine liver lipids, but not with E. coli lipids. Basal (i.e., not drug-stimulated) ATPase activity was different in the three lipids. Azidopine labeling of the drug binding sites in purified, reconstituted P-glycoprotein was carried out; vinblastine, colchicine, and daunomycin competed for labeling in all three lipids. It is therefore evident that the lipid environment can significantly influence the characteristics of purified, reconstituted P-glycoprotein ATPase activity and the apparent coupling between drug-binding and catalytic sites. |
| doi_str_mv | 10.1006/abbi.1995.1020 |
| format | Article |
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L. Urbatsch, M. K. Al-Shawl, and A. E. Senior (1994, Biochemistry 33, 7069-7076). The presence of lipid during the octylglucoside solubilization and Reactive Red 120 chromatography steps was found to be mandatory for retention of ATPase activity. Sheep brain or bovine liver lipid extracts could be substituted for the Escherichia coli lipids used previously, Stimulation of ATPase activity of purified, reconstituted P-glycoprotein by vinblastine, colchicine, and daunomycin was seen with sheep brain and bovine liver lipids, but not with E. coli lipids. Basal (i.e., not drug-stimulated) ATPase activity was different in the three lipids. Azidopine labeling of the drug binding sites in purified, reconstituted P-glycoprotein was carried out; vinblastine, colchicine, and daunomycin competed for labeling in all three lipids. It is therefore evident that the lipid environment can significantly influence the characteristics of purified, reconstituted P-glycoprotein ATPase activity and the apparent coupling between drug-binding and catalytic sites.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1006/abbi.1995.1020</identifier><identifier>PMID: 7840607</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphatases - drug effects ; Animals ; ATP-Binding Cassette, Sub-Family B, Member 1 - drug effects ; ATP-Binding Cassette, Sub-Family B, Member 1 - isolation & purification ; ATP-Binding Cassette, Sub-Family B, Member 1 - metabolism ; Azides - metabolism ; Binding, Competitive ; Brain Chemistry ; Cattle ; Cell Membrane - metabolism ; Colchicine - pharmacology ; Cricetinae ; Cricetulus ; Daunorubicin - pharmacology ; Dihydropyridines - metabolism ; Escherichia coli - chemistry ; Lipids - pharmacology ; Liver - chemistry ; Proteolipids - metabolism ; Sheep ; Verapamil - pharmacology ; Vinblastine - pharmacology</subject><ispartof>Archives of biochemistry and biophysics, 1995-01, Vol.316 (1), p.135-140</ispartof><rights>1995 Academic Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c445t-cc58ac37ecf221cbda16172bde2bcc5d8f1b6c56c03c5a0fbf27e79765962af53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/abbi.1995.1020$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7840607$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Urbatsch, I.L.</creatorcontrib><creatorcontrib>Senior, A.E.</creatorcontrib><title>Effects of Lipids on ATPase Activity of Purified Chinese Hamster P-Glycoprotein</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Chinese hamster P-glycoprotein ("multidrug-resistance protein") was purified and reconstituted in proteoliposomes by the procedure of I. L. Urbatsch, M. K. Al-Shawl, and A. E. Senior (1994, Biochemistry 33, 7069-7076). The presence of lipid during the octylglucoside solubilization and Reactive Red 120 chromatography steps was found to be mandatory for retention of ATPase activity. Sheep brain or bovine liver lipid extracts could be substituted for the Escherichia coli lipids used previously, Stimulation of ATPase activity of purified, reconstituted P-glycoprotein by vinblastine, colchicine, and daunomycin was seen with sheep brain and bovine liver lipids, but not with E. coli lipids. Basal (i.e., not drug-stimulated) ATPase activity was different in the three lipids. Azidopine labeling of the drug binding sites in purified, reconstituted P-glycoprotein was carried out; vinblastine, colchicine, and daunomycin competed for labeling in all three lipids. It is therefore evident that the lipid environment can significantly influence the characteristics of purified, reconstituted P-glycoprotein ATPase activity and the apparent coupling between drug-binding and catalytic sites.</description><subject>Adenosine Triphosphatases - drug effects</subject><subject>Animals</subject><subject>ATP-Binding Cassette, Sub-Family B, Member 1 - drug effects</subject><subject>ATP-Binding Cassette, Sub-Family B, Member 1 - isolation & purification</subject><subject>ATP-Binding Cassette, Sub-Family B, Member 1 - metabolism</subject><subject>Azides - metabolism</subject><subject>Binding, Competitive</subject><subject>Brain Chemistry</subject><subject>Cattle</subject><subject>Cell Membrane - metabolism</subject><subject>Colchicine - pharmacology</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Daunorubicin - pharmacology</subject><subject>Dihydropyridines - metabolism</subject><subject>Escherichia coli - chemistry</subject><subject>Lipids - pharmacology</subject><subject>Liver - chemistry</subject><subject>Proteolipids - metabolism</subject><subject>Sheep</subject><subject>Verapamil - pharmacology</subject><subject>Vinblastine - pharmacology</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEtLAzEURoMotVa37oRZuZt6M49kZllKbYVCu6jrkGRuMDKPmswU-u_N0OLOVW443_1CDiHPFOYUgL1JpeyclmUergnckCmFksWQFtktmQJAGpcFo_fkwftvAEozlkzIhBcZMOBTslsZg7r3UWeirT3aKkxttDjspcdooXt7sv15hPvBWWOxipZftsUAN7LxPbpoH6_rs-6OruvRto_kzsja49P1nJHP99VhuYm3u_XHcrGNdZblfax1XkidctQmSahWlaSM8kRVmKjAqsJQxXTONKQ6l2CUSTjykrO8ZIk0eTojr5fe8O7PgL4XjfUa61q22A1ecE7TnGUQgvNLULvOe4dGHJ1tpDsLCmI0KEaDYjQoRoNh4eXaPKgGq7_4VVngxYVj-N7JohNeW2w1VtYFk6Lq7H_Vv8BZf5s</recordid><startdate>19950110</startdate><enddate>19950110</enddate><creator>Urbatsch, I.L.</creator><creator>Senior, A.E.</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>19950110</creationdate><title>Effects of Lipids on ATPase Activity of Purified Chinese Hamster P-Glycoprotein</title><author>Urbatsch, I.L. ; Senior, A.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c445t-cc58ac37ecf221cbda16172bde2bcc5d8f1b6c56c03c5a0fbf27e79765962af53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adenosine Triphosphatases - drug effects</topic><topic>Animals</topic><topic>ATP-Binding Cassette, Sub-Family B, Member 1 - drug effects</topic><topic>ATP-Binding Cassette, Sub-Family B, Member 1 - isolation & purification</topic><topic>ATP-Binding Cassette, Sub-Family B, Member 1 - metabolism</topic><topic>Azides - metabolism</topic><topic>Binding, Competitive</topic><topic>Brain Chemistry</topic><topic>Cattle</topic><topic>Cell Membrane - metabolism</topic><topic>Colchicine - pharmacology</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>Daunorubicin - pharmacology</topic><topic>Dihydropyridines - metabolism</topic><topic>Escherichia coli - chemistry</topic><topic>Lipids - pharmacology</topic><topic>Liver - chemistry</topic><topic>Proteolipids - metabolism</topic><topic>Sheep</topic><topic>Verapamil - pharmacology</topic><topic>Vinblastine - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Urbatsch, I.L.</creatorcontrib><creatorcontrib>Senior, A.E.</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>Urbatsch, I.L.</au><au>Senior, A.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of Lipids on ATPase Activity of Purified Chinese Hamster P-Glycoprotein</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1995-01-10</date><risdate>1995</risdate><volume>316</volume><issue>1</issue><spage>135</spage><epage>140</epage><pages>135-140</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Chinese hamster P-glycoprotein ("multidrug-resistance protein") was purified and reconstituted in proteoliposomes by the procedure of I. L. Urbatsch, M. K. Al-Shawl, and A. E. Senior (1994, Biochemistry 33, 7069-7076). The presence of lipid during the octylglucoside solubilization and Reactive Red 120 chromatography steps was found to be mandatory for retention of ATPase activity. Sheep brain or bovine liver lipid extracts could be substituted for the Escherichia coli lipids used previously, Stimulation of ATPase activity of purified, reconstituted P-glycoprotein by vinblastine, colchicine, and daunomycin was seen with sheep brain and bovine liver lipids, but not with E. coli lipids. Basal (i.e., not drug-stimulated) ATPase activity was different in the three lipids. Azidopine labeling of the drug binding sites in purified, reconstituted P-glycoprotein was carried out; vinblastine, colchicine, and daunomycin competed for labeling in all three lipids. It is therefore evident that the lipid environment can significantly influence the characteristics of purified, reconstituted P-glycoprotein ATPase activity and the apparent coupling between drug-binding and catalytic sites.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7840607</pmid><doi>10.1006/abbi.1995.1020</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Triphosphatases - drug effects Animals ATP-Binding Cassette, Sub-Family B, Member 1 - drug effects ATP-Binding Cassette, Sub-Family B, Member 1 - isolation & purification ATP-Binding Cassette, Sub-Family B, Member 1 - metabolism Azides - metabolism Binding, Competitive Brain Chemistry Cattle Cell Membrane - metabolism Colchicine - pharmacology Cricetinae Cricetulus Daunorubicin - pharmacology Dihydropyridines - metabolism Escherichia coli - chemistry Lipids - pharmacology Liver - chemistry Proteolipids - metabolism Sheep Verapamil - pharmacology Vinblastine - pharmacology |
| title | Effects of Lipids on ATPase Activity of Purified Chinese Hamster P-Glycoprotein |
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