Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein
FK506-binding protein (FKBP12) was originally identified as the cytosolic receptor for the immunosuppressant drugs FK506 and rapamycin. The cellular function of FKBP12, a ubiquitously expressed 12,000-dalton proline isomerase, has been unknown. FKBP12 copurifies with the 565,000-dalton ryanodine rec...
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| Veröffentlicht in: | Cell 1994-05, Vol.77 (4), p.513-523 |
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| creator | Brillantes, Anne-Marie B. Ondrias, Karol Scott, Andrew Kobrinsky, Evgeny Ondriašová, Elena Moschella, Maria C. Jayaraman, Thottala Landers, Mark Ehrlich, Barbara E. Marks, Andrew R. |
| description | FK506-binding protein (FKBP12) was originally identified as the cytosolic receptor for the immunosuppressant drugs FK506 and rapamycin. The cellular function of FKBP12, a ubiquitously expressed 12,000-dalton proline isomerase, has been unknown. FKBP12 copurifies with the 565,000-dalton ryanodine receptor (RyR), four of which form intracellular Ca
2+ release channels of the sarcoplasmic and endoplasmic reticula. By coexpressing the RyR and FKBP12 in insect cells, we have demonstrated that FKBP12 modulates channel gating by increasing channels with full conductance levels (by >400%), decreasing open probability after caffeine activation (from 0.63 ± 0.09 to 0.04 ± 0.02), and increasing mean open time (from 4.4 ± 0.6 ms to 75 ± 41 ms). FK506 or rapamycin, inhibitors of FKBP12 isomerase activity, reverse these stabilizing effects. These results provide the first natural cellular function for FKBP12, and establish that the functional Ca
2+ release channel complex includes FKBP12. |
| doi_str_mv | 10.1016/0092-8674(94)90214-3 |
| format | Article |
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2+ release channels of the sarcoplasmic and endoplasmic reticula. By coexpressing the RyR and FKBP12 in insect cells, we have demonstrated that FKBP12 modulates channel gating by increasing channels with full conductance levels (by >400%), decreasing open probability after caffeine activation (from 0.63 ± 0.09 to 0.04 ± 0.02), and increasing mean open time (from 4.4 ± 0.6 ms to 75 ± 41 ms). FK506 or rapamycin, inhibitors of FKBP12 isomerase activity, reverse these stabilizing effects. These results provide the first natural cellular function for FKBP12, and establish that the functional Ca
2+ release channel complex includes FKBP12.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(94)90214-3</identifier><identifier>PMID: 7514503</identifier><identifier>CODEN: CELLB5</identifier><language>eng</language><publisher>Cambridge, MA: Elsevier Inc</publisher><subject><![CDATA[Animals ; Biological and medical sciences ; Caffeine - pharmacology ; Calcium - metabolism ; Calcium Channels - genetics ; Calcium Channels - isolation & purification ; Calcium Channels - physiology ; Carrier Proteins - antagonists & inhibitors ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Carrier Proteins - physiology ; Cell Line ; Cell physiology ; Cloning, Molecular ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Heat-Shock Proteins - antagonists & inhibitors ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - isolation & purification ; Heat-Shock Proteins - physiology ; Ion Channel Gating - drug effects ; Ion Channel Gating - physiology ; Isometric Contraction - drug effects ; Lipid Bilayers ; Membrane and intracellular transports ; Molecular and cellular biology ; Muscle Proteins - genetics ; Muscle Proteins - isolation & purification ; Muscle Proteins - physiology ; Polyenes - pharmacology ; Rabbits ; Rats ; Recombinant Proteins - isolation & purification ; RNA, Messenger - analysis ; Ruthenium Red - pharmacology ; Ryanodine - pharmacology ; Ryanodine Receptor Calcium Release Channel ; Sarcoplasmic Reticulum - metabolism ; Sirolimus ; Tacrolimus - pharmacology ; Tacrolimus Binding Proteins]]></subject><ispartof>Cell, 1994-05, Vol.77 (4), p.513-523</ispartof><rights>1994</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c432t-58473fd5329b55bcddc38c9749ec64d834ae3ed3619b52d3804fe1e6cc8ed143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0092867494902143$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4199749$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7514503$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brillantes, Anne-Marie B.</creatorcontrib><creatorcontrib>Ondrias, Karol</creatorcontrib><creatorcontrib>Scott, Andrew</creatorcontrib><creatorcontrib>Kobrinsky, Evgeny</creatorcontrib><creatorcontrib>Ondriašová, Elena</creatorcontrib><creatorcontrib>Moschella, Maria C.</creatorcontrib><creatorcontrib>Jayaraman, Thottala</creatorcontrib><creatorcontrib>Landers, Mark</creatorcontrib><creatorcontrib>Ehrlich, Barbara E.</creatorcontrib><creatorcontrib>Marks, Andrew R.</creatorcontrib><title>Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein</title><title>Cell</title><addtitle>Cell</addtitle><description>FK506-binding protein (FKBP12) was originally identified as the cytosolic receptor for the immunosuppressant drugs FK506 and rapamycin. The cellular function of FKBP12, a ubiquitously expressed 12,000-dalton proline isomerase, has been unknown. FKBP12 copurifies with the 565,000-dalton ryanodine receptor (RyR), four of which form intracellular Ca
2+ release channels of the sarcoplasmic and endoplasmic reticula. By coexpressing the RyR and FKBP12 in insect cells, we have demonstrated that FKBP12 modulates channel gating by increasing channels with full conductance levels (by >400%), decreasing open probability after caffeine activation (from 0.63 ± 0.09 to 0.04 ± 0.02), and increasing mean open time (from 4.4 ± 0.6 ms to 75 ± 41 ms). FK506 or rapamycin, inhibitors of FKBP12 isomerase activity, reverse these stabilizing effects. These results provide the first natural cellular function for FKBP12, and establish that the functional Ca
2+ release channel complex includes FKBP12.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Caffeine - pharmacology</subject><subject>Calcium - metabolism</subject><subject>Calcium Channels - genetics</subject><subject>Calcium Channels - isolation & purification</subject><subject>Calcium Channels - physiology</subject><subject>Carrier Proteins - antagonists & inhibitors</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - physiology</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>Cloning, Molecular</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Heat-Shock Proteins - antagonists & inhibitors</subject><subject>Heat-Shock Proteins - genetics</subject><subject>Heat-Shock Proteins - isolation & purification</subject><subject>Heat-Shock Proteins - physiology</subject><subject>Ion Channel Gating - drug effects</subject><subject>Ion Channel Gating - physiology</subject><subject>Isometric Contraction - drug effects</subject><subject>Lipid Bilayers</subject><subject>Membrane and intracellular transports</subject><subject>Molecular and cellular biology</subject><subject>Muscle Proteins - genetics</subject><subject>Muscle Proteins - isolation & purification</subject><subject>Muscle Proteins - physiology</subject><subject>Polyenes - pharmacology</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>RNA, Messenger - analysis</subject><subject>Ruthenium Red - pharmacology</subject><subject>Ryanodine - pharmacology</subject><subject>Ryanodine Receptor Calcium Release Channel</subject><subject>Sarcoplasmic Reticulum - metabolism</subject><subject>Sirolimus</subject><subject>Tacrolimus - pharmacology</subject><subject>Tacrolimus Binding Proteins</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1q3DAURkVpSKdp36AFL0pIFk4l68fSplBC05YEskj2Qr66blU88kSyA5Onj9wZZpmAQIvvfFdXh5BPjF4wytRXSk1Ta9WKMyPODW2YqPkbsmLUtLVgbfOWrA7IO_I-53-UUi2lPCbHrWRCUr4i9m5yXRjCk5vCGKuxr8ANEOZ1lXBAl7GCvy5GHKqztHVx9CFiiQA305jOq36O8L_Ybaura0lV3YVYmD_VJo0ThviBHPVuyPhxf5-Q-6sf95e_6pvbn78vv9_UIHgz1VKLlvde8sZ0UnbgPXANphUGQQmvuXDI0XPFSt54rqnokaEC0OiZ4CfkdDe2PPswY57sOmTAYXARxznbVgmtGilfBZkymtGGF1DsQEhjzgl7u0lh7dLWMmoX_3aRaxe51pSz-LdL7fN-_tyt0R9Ke-El_7LPXS6m--QihHzABDPLpwv2bYdhcfYYMNkMASOgD0X-ZP0YXt7jGcqvoR8</recordid><startdate>19940520</startdate><enddate>19940520</enddate><creator>Brillantes, Anne-Marie B.</creator><creator>Ondrias, Karol</creator><creator>Scott, Andrew</creator><creator>Kobrinsky, Evgeny</creator><creator>Ondriašová, Elena</creator><creator>Moschella, Maria C.</creator><creator>Jayaraman, Thottala</creator><creator>Landers, Mark</creator><creator>Ehrlich, Barbara E.</creator><creator>Marks, Andrew R.</creator><general>Elsevier Inc</general><general>Cell Press</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19940520</creationdate><title>Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein</title><author>Brillantes, Anne-Marie B. ; Ondrias, Karol ; Scott, Andrew ; Kobrinsky, Evgeny ; Ondriašová, Elena ; Moschella, Maria C. ; Jayaraman, Thottala ; Landers, Mark ; Ehrlich, Barbara E. ; Marks, Andrew R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c432t-58473fd5329b55bcddc38c9749ec64d834ae3ed3619b52d3804fe1e6cc8ed143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Caffeine - pharmacology</topic><topic>Calcium - metabolism</topic><topic>Calcium Channels - genetics</topic><topic>Calcium Channels - isolation & purification</topic><topic>Calcium Channels - physiology</topic><topic>Carrier Proteins - antagonists & inhibitors</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - physiology</topic><topic>Cell Line</topic><topic>Cell physiology</topic><topic>Cloning, Molecular</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Heat-Shock Proteins - antagonists & inhibitors</topic><topic>Heat-Shock Proteins - genetics</topic><topic>Heat-Shock Proteins - isolation & purification</topic><topic>Heat-Shock Proteins - physiology</topic><topic>Ion Channel Gating - drug effects</topic><topic>Ion Channel Gating - physiology</topic><topic>Isometric Contraction - drug effects</topic><topic>Lipid Bilayers</topic><topic>Membrane and intracellular transports</topic><topic>Molecular and cellular biology</topic><topic>Muscle Proteins - genetics</topic><topic>Muscle Proteins - isolation & purification</topic><topic>Muscle Proteins - physiology</topic><topic>Polyenes - pharmacology</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>RNA, Messenger - analysis</topic><topic>Ruthenium Red - pharmacology</topic><topic>Ryanodine - pharmacology</topic><topic>Ryanodine Receptor Calcium Release Channel</topic><topic>Sarcoplasmic Reticulum - metabolism</topic><topic>Sirolimus</topic><topic>Tacrolimus - pharmacology</topic><topic>Tacrolimus Binding Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brillantes, Anne-Marie B.</creatorcontrib><creatorcontrib>Ondrias, Karol</creatorcontrib><creatorcontrib>Scott, Andrew</creatorcontrib><creatorcontrib>Kobrinsky, Evgeny</creatorcontrib><creatorcontrib>Ondriašová, Elena</creatorcontrib><creatorcontrib>Moschella, Maria C.</creatorcontrib><creatorcontrib>Jayaraman, Thottala</creatorcontrib><creatorcontrib>Landers, Mark</creatorcontrib><creatorcontrib>Ehrlich, Barbara E.</creatorcontrib><creatorcontrib>Marks, Andrew 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>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brillantes, Anne-Marie B.</au><au>Ondrias, Karol</au><au>Scott, Andrew</au><au>Kobrinsky, Evgeny</au><au>Ondriašová, Elena</au><au>Moschella, Maria C.</au><au>Jayaraman, Thottala</au><au>Landers, Mark</au><au>Ehrlich, Barbara E.</au><au>Marks, Andrew R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1994-05-20</date><risdate>1994</risdate><volume>77</volume><issue>4</issue><spage>513</spage><epage>523</epage><pages>513-523</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><abstract>FK506-binding protein (FKBP12) was originally identified as the cytosolic receptor for the immunosuppressant drugs FK506 and rapamycin. The cellular function of FKBP12, a ubiquitously expressed 12,000-dalton proline isomerase, has been unknown. FKBP12 copurifies with the 565,000-dalton ryanodine receptor (RyR), four of which form intracellular Ca
2+ release channels of the sarcoplasmic and endoplasmic reticula. By coexpressing the RyR and FKBP12 in insect cells, we have demonstrated that FKBP12 modulates channel gating by increasing channels with full conductance levels (by >400%), decreasing open probability after caffeine activation (from 0.63 ± 0.09 to 0.04 ± 0.02), and increasing mean open time (from 4.4 ± 0.6 ms to 75 ± 41 ms). FK506 or rapamycin, inhibitors of FKBP12 isomerase activity, reverse these stabilizing effects. These results provide the first natural cellular function for FKBP12, and establish that the functional Ca
2+ release channel complex includes FKBP12.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>7514503</pmid><doi>10.1016/0092-8674(94)90214-3</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Cell, 1994-05, Vol.77 (4), p.513-523 |
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| subjects | Animals Biological and medical sciences Caffeine - pharmacology Calcium - metabolism Calcium Channels - genetics Calcium Channels - isolation & purification Calcium Channels - physiology Carrier Proteins - antagonists & inhibitors Carrier Proteins - genetics Carrier Proteins - isolation & purification Carrier Proteins - physiology Cell Line Cell physiology Cloning, Molecular Fundamental and applied biological sciences. Psychology Gene Expression Heat-Shock Proteins - antagonists & inhibitors Heat-Shock Proteins - genetics Heat-Shock Proteins - isolation & purification Heat-Shock Proteins - physiology Ion Channel Gating - drug effects Ion Channel Gating - physiology Isometric Contraction - drug effects Lipid Bilayers Membrane and intracellular transports Molecular and cellular biology Muscle Proteins - genetics Muscle Proteins - isolation & purification Muscle Proteins - physiology Polyenes - pharmacology Rabbits Rats Recombinant Proteins - isolation & purification RNA, Messenger - analysis Ruthenium Red - pharmacology Ryanodine - pharmacology Ryanodine Receptor Calcium Release Channel Sarcoplasmic Reticulum - metabolism Sirolimus Tacrolimus - pharmacology Tacrolimus Binding Proteins |
| title | Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein |
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