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Poly(ADP-ribose) Polymerase (PARP)-1-independent Apoptosis-inducing Factor (AIF) Release and Cell Death Are Induced by Eleostearic Acid and Blocked by α-Tocopherol and MEK Inhibition
Poly(ADP-ribose)polymerase-1 (PARP-1) is thought to be required for apoptosis-inducing factor (AIF) release from mitochondria in caspase-independent apoptosis. The mechanism by which AIF is released through PARP-1 remains unclear. Here, we provide evidence that PARP-1-independent AIF release and cel...
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| Published in: | The Journal of biological chemistry 2010-04, Vol.285 (17), p.13079-13091 |
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| container_issue | 17 |
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| creator | Kondo, Kazunari Obitsu, Saemi Ohta, Sayaka Matsunami, Katsuyoshi Otsuka, Hideaki Teshima, Reiko |
| description | Poly(ADP-ribose)polymerase-1 (PARP-1) is thought to be required for apoptosis-inducing factor (AIF) release from mitochondria in caspase-independent apoptosis. The mechanism by which AIF is released through PARP-1 remains unclear. Here, we provide evidence that PARP-1-independent AIF release and cell death are induced by a trienoic fatty acid, α-eleostearic acid (α-ESA). α-ESA induced the caspase-independent and AIF-initiated apoptotic death of neuronal cell lines, independently of PARP-1 activation. The cell death was inhibited by the MEK inhibitor U0126 and by knockdown of MEK using small interfering RNA. However, inhibitors for JNK, p38 inhibitors, calpain, phospholipase A2, and phosphatidylinositol 3-kinase, did not block cell death. AIF was translocated to the nucleus after the induction of apoptosis by α-ESA in differentiated PC12 cells without activating caspase-3 and PARP-1. The α-ESA-mediated cell death was not inhibited by PARP inhibitor 3,4-dihydro-5-[4-(1-piperidinyl)butoxyl]-1(2H)-isoquinoline and by knockdown of PARP-1 using small interfering RNA. Unlike N-methyl-N′-nitro-N-nitrosoguanidine treatment, histone-phosphorylated histone 2AX was not phosphorylated by α-ESA, which suggests no DNA damage. Overexpression of Bcl-2 did not inhibit the cell death. α-ESA caused a small quantity of superoxide production in the mitochondria, resulting in the reduction of mitochondrial membrane potential, both of which were blocked by a trace amount of α-tocopherol localized in the mitochondria. Our results demonstrate that α-ESA induces PARP-1-independent AIF release and cell death without activating Bax, cytochrome c, and caspase-3. MEK is also a key molecule, although the link between ERK, AIF release, and cell death remains unknown. Finding molecules that regulate AIF release may be an important therapeutic target for the treatment of neuronal injury. |
| doi_str_mv | 10.1074/jbc.M109.044206 |
| format | article |
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The mechanism by which AIF is released through PARP-1 remains unclear. Here, we provide evidence that PARP-1-independent AIF release and cell death are induced by a trienoic fatty acid, α-eleostearic acid (α-ESA). α-ESA induced the caspase-independent and AIF-initiated apoptotic death of neuronal cell lines, independently of PARP-1 activation. The cell death was inhibited by the MEK inhibitor U0126 and by knockdown of MEK using small interfering RNA. However, inhibitors for JNK, p38 inhibitors, calpain, phospholipase A2, and phosphatidylinositol 3-kinase, did not block cell death. AIF was translocated to the nucleus after the induction of apoptosis by α-ESA in differentiated PC12 cells without activating caspase-3 and PARP-1. The α-ESA-mediated cell death was not inhibited by PARP inhibitor 3,4-dihydro-5-[4-(1-piperidinyl)butoxyl]-1(2H)-isoquinoline and by knockdown of PARP-1 using small interfering RNA. Unlike N-methyl-N′-nitro-N-nitrosoguanidine treatment, histone-phosphorylated histone 2AX was not phosphorylated by α-ESA, which suggests no DNA damage. Overexpression of Bcl-2 did not inhibit the cell death. α-ESA caused a small quantity of superoxide production in the mitochondria, resulting in the reduction of mitochondrial membrane potential, both of which were blocked by a trace amount of α-tocopherol localized in the mitochondria. Our results demonstrate that α-ESA induces PARP-1-independent AIF release and cell death without activating Bax, cytochrome c, and caspase-3. MEK is also a key molecule, although the link between ERK, AIF release, and cell death remains unknown. Finding molecules that regulate AIF release may be an important therapeutic target for the treatment of neuronal injury.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M109.044206</identifier><identifier>PMID: 20177052</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Active Transport, Cell Nucleus - drug effects ; AIF ; alpha-Tocopherol - pharmacology ; Animals ; Antioxidants - pharmacology ; Apoptosis ; Apoptosis - drug effects ; Apoptosis Inducing Factor - genetics ; Apoptosis Inducing Factor - metabolism ; bcl-2-Associated X Protein - genetics ; bcl-2-Associated X Protein - metabolism ; Caspase 3 - genetics ; Caspase 3 - metabolism ; Cell Biology ; Cell Nucleus - genetics ; Cell Nucleus - metabolism ; DNA/Damage ; Eleostearic Acid ; Enzyme Inhibitors - pharmacology ; ERK ; Humans ; Linolenic Acids - pharmacology ; Lipid/Fatty Acid ; Lipids ; MAP Kinase Kinase Kinases - antagonists & inhibitors ; MAP Kinase Kinase Kinases - genetics ; MAP Kinase Kinase Kinases - metabolism ; Mice ; Neurochemistry ; Neurons - metabolism ; PARP-1 ; PC12 Cells ; Phosphorylation - drug effects ; Poly (ADP-Ribose) Polymerase-1 ; Poly(ADP-ribose) Polymerases - genetics ; Poly(ADP-ribose) Polymerases - metabolism ; Rats</subject><ispartof>The Journal of biological chemistry, 2010-04, Vol.285 (17), p.13079-13091</ispartof><rights>2010 © 2010 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2010 by The American Society for Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466t-61f6ac746af16b2041fdcf29af5de2d672565ead82c76005f69dca0c90a06e4d3</citedby><cites>FETCH-LOGICAL-c466t-61f6ac746af16b2041fdcf29af5de2d672565ead82c76005f69dca0c90a06e4d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2857103/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2857103/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,733,786,790,891,27957,27958,53827,53829</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20177052$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kondo, Kazunari</creatorcontrib><creatorcontrib>Obitsu, Saemi</creatorcontrib><creatorcontrib>Ohta, Sayaka</creatorcontrib><creatorcontrib>Matsunami, Katsuyoshi</creatorcontrib><creatorcontrib>Otsuka, Hideaki</creatorcontrib><creatorcontrib>Teshima, Reiko</creatorcontrib><title>Poly(ADP-ribose) Polymerase (PARP)-1-independent Apoptosis-inducing Factor (AIF) Release and Cell Death Are Induced by Eleostearic Acid and Blocked by α-Tocopherol and MEK Inhibition</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Poly(ADP-ribose)polymerase-1 (PARP-1) is thought to be required for apoptosis-inducing factor (AIF) release from mitochondria in caspase-independent apoptosis. The mechanism by which AIF is released through PARP-1 remains unclear. Here, we provide evidence that PARP-1-independent AIF release and cell death are induced by a trienoic fatty acid, α-eleostearic acid (α-ESA). α-ESA induced the caspase-independent and AIF-initiated apoptotic death of neuronal cell lines, independently of PARP-1 activation. The cell death was inhibited by the MEK inhibitor U0126 and by knockdown of MEK using small interfering RNA. However, inhibitors for JNK, p38 inhibitors, calpain, phospholipase A2, and phosphatidylinositol 3-kinase, did not block cell death. AIF was translocated to the nucleus after the induction of apoptosis by α-ESA in differentiated PC12 cells without activating caspase-3 and PARP-1. The α-ESA-mediated cell death was not inhibited by PARP inhibitor 3,4-dihydro-5-[4-(1-piperidinyl)butoxyl]-1(2H)-isoquinoline and by knockdown of PARP-1 using small interfering RNA. Unlike N-methyl-N′-nitro-N-nitrosoguanidine treatment, histone-phosphorylated histone 2AX was not phosphorylated by α-ESA, which suggests no DNA damage. Overexpression of Bcl-2 did not inhibit the cell death. α-ESA caused a small quantity of superoxide production in the mitochondria, resulting in the reduction of mitochondrial membrane potential, both of which were blocked by a trace amount of α-tocopherol localized in the mitochondria. Our results demonstrate that α-ESA induces PARP-1-independent AIF release and cell death without activating Bax, cytochrome c, and caspase-3. MEK is also a key molecule, although the link between ERK, AIF release, and cell death remains unknown. Finding molecules that regulate AIF release may be an important therapeutic target for the treatment of neuronal injury.</description><subject>Active Transport, Cell Nucleus - drug effects</subject><subject>AIF</subject><subject>alpha-Tocopherol - pharmacology</subject><subject>Animals</subject><subject>Antioxidants - pharmacology</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis Inducing Factor - genetics</subject><subject>Apoptosis Inducing Factor - metabolism</subject><subject>bcl-2-Associated X Protein - genetics</subject><subject>bcl-2-Associated X Protein - metabolism</subject><subject>Caspase 3 - genetics</subject><subject>Caspase 3 - metabolism</subject><subject>Cell Biology</subject><subject>Cell Nucleus - genetics</subject><subject>Cell Nucleus - metabolism</subject><subject>DNA/Damage</subject><subject>Eleostearic Acid</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>ERK</subject><subject>Humans</subject><subject>Linolenic Acids - pharmacology</subject><subject>Lipid/Fatty Acid</subject><subject>Lipids</subject><subject>MAP Kinase Kinase Kinases - antagonists & inhibitors</subject><subject>MAP Kinase Kinase Kinases - genetics</subject><subject>MAP Kinase Kinase Kinases - metabolism</subject><subject>Mice</subject><subject>Neurochemistry</subject><subject>Neurons - metabolism</subject><subject>PARP-1</subject><subject>PC12 Cells</subject><subject>Phosphorylation - drug effects</subject><subject>Poly (ADP-Ribose) Polymerase-1</subject><subject>Poly(ADP-ribose) Polymerases - genetics</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Rats</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNp1kUFv0zAUxy0EYmVw5ga-0R7S2U7iJJdJoWuhYhPV2CRulmO_tB5pHOx00j4WJ74FnwlnGRMc8MGW3v_3_s96f4ReUzKnJEtObio1v6CkmJMkYYQ_QRNK8jiKU_r1KZoQwmhUsDQ_Qi-8vyHhJAV9jo4YoVlGUjZBPze2uZuWZ5vImcp6mOGhsAcnPeDpprzczCIamVZDB-Fqe1x2tuutN36oHpRpt3glVW8dnpbr1QxfQgNDs2w1XkDT4DOQ_Q6XDvB6aACNqzu8bMD6HqQzCpfK6Hv8fWPVt1H_9SO6ssp2O3C2uRcvlp-Cwc5Upje2fYme1bLx8OrhPUbXq-XV4mN0_vnDelGeRyrhvI84rblUWcJlTXnFSEJrrWpWyDrVwDTPWMpTkDpnKuOEpDUvtJJEFUQSDomOj9Hp6Nsdqj1oFTbgZCM6Z_bS3QkrjfhXac1ObO2tYHmaURIHg3cPBs5-P4Dvxd54FfYiW7AHL7I4TpOsSLJAnoykctZ7B_XjFErEkLYIaYshbTGmHTre_P25R_5PvAF4OwK1tEJunfHi-ktQY0Jzlsc8DUQxEhCWeGvACa8MtCEl40D1Qlvz3_G_AbNzxHg</recordid><startdate>20100423</startdate><enddate>20100423</enddate><creator>Kondo, Kazunari</creator><creator>Obitsu, Saemi</creator><creator>Ohta, Sayaka</creator><creator>Matsunami, Katsuyoshi</creator><creator>Otsuka, Hideaki</creator><creator>Teshima, Reiko</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</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><scope>5PM</scope></search><sort><creationdate>20100423</creationdate><title>Poly(ADP-ribose) Polymerase (PARP)-1-independent Apoptosis-inducing Factor (AIF) Release and Cell Death Are Induced by Eleostearic Acid and Blocked by α-Tocopherol and MEK Inhibition</title><author>Kondo, Kazunari ; 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The mechanism by which AIF is released through PARP-1 remains unclear. Here, we provide evidence that PARP-1-independent AIF release and cell death are induced by a trienoic fatty acid, α-eleostearic acid (α-ESA). α-ESA induced the caspase-independent and AIF-initiated apoptotic death of neuronal cell lines, independently of PARP-1 activation. The cell death was inhibited by the MEK inhibitor U0126 and by knockdown of MEK using small interfering RNA. However, inhibitors for JNK, p38 inhibitors, calpain, phospholipase A2, and phosphatidylinositol 3-kinase, did not block cell death. AIF was translocated to the nucleus after the induction of apoptosis by α-ESA in differentiated PC12 cells without activating caspase-3 and PARP-1. The α-ESA-mediated cell death was not inhibited by PARP inhibitor 3,4-dihydro-5-[4-(1-piperidinyl)butoxyl]-1(2H)-isoquinoline and by knockdown of PARP-1 using small interfering RNA. Unlike N-methyl-N′-nitro-N-nitrosoguanidine treatment, histone-phosphorylated histone 2AX was not phosphorylated by α-ESA, which suggests no DNA damage. Overexpression of Bcl-2 did not inhibit the cell death. α-ESA caused a small quantity of superoxide production in the mitochondria, resulting in the reduction of mitochondrial membrane potential, both of which were blocked by a trace amount of α-tocopherol localized in the mitochondria. Our results demonstrate that α-ESA induces PARP-1-independent AIF release and cell death without activating Bax, cytochrome c, and caspase-3. MEK is also a key molecule, although the link between ERK, AIF release, and cell death remains unknown. Finding molecules that regulate AIF release may be an important therapeutic target for the treatment of neuronal injury.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20177052</pmid><doi>10.1074/jbc.M109.044206</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2010-04, Vol.285 (17), p.13079-13091 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS; PubMed Central |
| subjects | Active Transport, Cell Nucleus - drug effects AIF alpha-Tocopherol - pharmacology Animals Antioxidants - pharmacology Apoptosis Apoptosis - drug effects Apoptosis Inducing Factor - genetics Apoptosis Inducing Factor - metabolism bcl-2-Associated X Protein - genetics bcl-2-Associated X Protein - metabolism Caspase 3 - genetics Caspase 3 - metabolism Cell Biology Cell Nucleus - genetics Cell Nucleus - metabolism DNA/Damage Eleostearic Acid Enzyme Inhibitors - pharmacology ERK Humans Linolenic Acids - pharmacology Lipid/Fatty Acid Lipids MAP Kinase Kinase Kinases - antagonists & inhibitors MAP Kinase Kinase Kinases - genetics MAP Kinase Kinase Kinases - metabolism Mice Neurochemistry Neurons - metabolism PARP-1 PC12 Cells Phosphorylation - drug effects Poly (ADP-Ribose) Polymerase-1 Poly(ADP-ribose) Polymerases - genetics Poly(ADP-ribose) Polymerases - metabolism Rats |
| title | Poly(ADP-ribose) Polymerase (PARP)-1-independent Apoptosis-inducing Factor (AIF) Release and Cell Death Are Induced by Eleostearic Acid and Blocked by α-Tocopherol and MEK Inhibition |
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