Arginase II Contributes to the Ca 2+ /CaMKII/eNOS Axis by Regulating Ca 2+ Concentration Between the Cytosol and Mitochondria in a p32-Dependent Manner
Background Arginase II activity contributes to reciprocal regulation of endothelial nitric oxide synthase ( eNOS ). We tested the hypotheses that arginase II activity participates in the regulation of Ca /Ca /calmodulin-dependent kinase II / eNOS activation, and this process is dependent on mitochon...
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| Veröffentlicht in: | Journal of the American Heart Association 2018-09, Vol.7 (18), p.e009579 |
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| creator | Koo, Bon-Hyeock Hwang, Hye-Mi Yi, Bong-Gu Lim, Hyun Kyo Jeon, Byeong Hwa Hoe, Kwang Lae Kwon, Young-Guen Won, Moo-Ho Kim, Young Myeong Berkowitz, Dan E Ryoo, Sungwoo |
| description | Background Arginase II activity contributes to reciprocal regulation of endothelial nitric oxide synthase ( eNOS ). We tested the hypotheses that arginase II activity participates in the regulation of Ca
/Ca
/calmodulin-dependent kinase II / eNOS activation, and this process is dependent on mitochondrial p32. Methods and Results Downregulation of arginase II increased the concentration of cytosolic Ca
([Ca
]c) and decreased mitochondrial Ca
([Ca
]m) in microscopic and fluorescence-activated cell sorting analyses, resulting in augmented eNOS Ser1177 phosphorylation and decreased eNOS Thr495 phosphorylation through Ca
/Ca
/calmodulin-dependent kinase II . These changes were observed in human umbilical vein endothelial cells treated with small interfering RNA against p32 (sip32). Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, fluorescence immunoassay, and ion chromatography, inhibition of arginase II reduced the amount of spermine, a binding molecule, and the release of Ca
from p32. In addition, arginase II gene knockdown using small interfering RNA and knockout arginase II -null mice resulted in reduced p32 protein level. In the aortas of wild-type mice, small interfering RNA against p32 induced eNOS Ser1177 phosphorylation and enhanced NO -dependent vasorelaxation. Arginase activity, p32 protein expression, spermine amount, and [Ca
]m were increased in the aortas from apolipoprotein E (ApoE
) mice fed a high-cholesterol diet, and intravenous administration of small interfering RNA against p32 restored Ca
/Ca
/calmodulin-dependent kinase II -dependent eNOS Ser1177 phosphorylation and improved endothelial dysfunction. The effects of arginase II downregulation were not associated with elevated NO production when tested in aortic endothelia from eNOS knockout mice. Conclusions These data demonstrate a novel function of arginase II in regulation of Ca
-dependent eNOS phosphorylation. This novel mechanism drives arginase activation, mitochondrial dysfunction, endothelial dysfunction, and atherogenesis. |
| doi_str_mv | 10.1161/JAHA.118.009579 |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1161_JAHA_118_009579</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>30371203</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1509-d89b646ff0f8f9a8920483bee927cefb63d121045dd8d513f0763ecc2cfabc0b3</originalsourceid><addsrcrecordid>eNpNkEtPwzAQhC0EAlQ4c0N7R2nsuHn4GMKjgRYkHufIsdclqDhRnAr6S_i7GAUQe9nRamak_Qg5YXTKWMLCm3yee5VNKRVxKnbIYURnaSBERnf_6QNy7Nwr9ZNEKY_FPjnglKcsovyQfOb9qrHSIZQlFK0d-qbeDOhgaGF4QSgkRGcQFnJ5W5Yh3t0_Qv7ROKi38ICrzVoOjV39uHxcoW_wt9bCOQ7viHZs2Q6ta9cgrYZlM7TqpbW6byQ0FiR0PAousEOrfRqW0lrsj8iekWuHxz97Qp6vLp-KebC4vy6LfBEoFlMR6EzUySwxhprMCJkJ_3XGa0QRpQpNnXDNIkZnsdaZjhk3NE04KhUpI2tFaz4h4dir-ta5Hk3V9c2b7LcVo9U35eqbsldZNVL2idMx0W3qN9R__l-m_AvYfHbU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Arginase II Contributes to the Ca 2+ /CaMKII/eNOS Axis by Regulating Ca 2+ Concentration Between the Cytosol and Mitochondria in a p32-Dependent Manner</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Wiley Online Library (Open Access Collection)</source><source>PubMed Central</source><creator>Koo, Bon-Hyeock ; Hwang, Hye-Mi ; Yi, Bong-Gu ; Lim, Hyun Kyo ; Jeon, Byeong Hwa ; Hoe, Kwang Lae ; Kwon, Young-Guen ; Won, Moo-Ho ; Kim, Young Myeong ; Berkowitz, Dan E ; Ryoo, Sungwoo</creator><creatorcontrib>Koo, Bon-Hyeock ; Hwang, Hye-Mi ; Yi, Bong-Gu ; Lim, Hyun Kyo ; Jeon, Byeong Hwa ; Hoe, Kwang Lae ; Kwon, Young-Guen ; Won, Moo-Ho ; Kim, Young Myeong ; Berkowitz, Dan E ; Ryoo, Sungwoo</creatorcontrib><description>Background Arginase II activity contributes to reciprocal regulation of endothelial nitric oxide synthase ( eNOS ). We tested the hypotheses that arginase II activity participates in the regulation of Ca
/Ca
/calmodulin-dependent kinase II / eNOS activation, and this process is dependent on mitochondrial p32. Methods and Results Downregulation of arginase II increased the concentration of cytosolic Ca
([Ca
]c) and decreased mitochondrial Ca
([Ca
]m) in microscopic and fluorescence-activated cell sorting analyses, resulting in augmented eNOS Ser1177 phosphorylation and decreased eNOS Thr495 phosphorylation through Ca
/Ca
/calmodulin-dependent kinase II . These changes were observed in human umbilical vein endothelial cells treated with small interfering RNA against p32 (sip32). Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, fluorescence immunoassay, and ion chromatography, inhibition of arginase II reduced the amount of spermine, a binding molecule, and the release of Ca
from p32. In addition, arginase II gene knockdown using small interfering RNA and knockout arginase II -null mice resulted in reduced p32 protein level. In the aortas of wild-type mice, small interfering RNA against p32 induced eNOS Ser1177 phosphorylation and enhanced NO -dependent vasorelaxation. Arginase activity, p32 protein expression, spermine amount, and [Ca
]m were increased in the aortas from apolipoprotein E (ApoE
) mice fed a high-cholesterol diet, and intravenous administration of small interfering RNA against p32 restored Ca
/Ca
/calmodulin-dependent kinase II -dependent eNOS Ser1177 phosphorylation and improved endothelial dysfunction. The effects of arginase II downregulation were not associated with elevated NO production when tested in aortic endothelia from eNOS knockout mice. Conclusions These data demonstrate a novel function of arginase II in regulation of Ca
-dependent eNOS phosphorylation. This novel mechanism drives arginase activation, mitochondrial dysfunction, endothelial dysfunction, and atherogenesis.</description><identifier>ISSN: 2047-9980</identifier><identifier>EISSN: 2047-9980</identifier><identifier>DOI: 10.1161/JAHA.118.009579</identifier><identifier>PMID: 30371203</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Aorta, Thoracic - metabolism ; Aorta, Thoracic - pathology ; Arginase - biosynthesis ; Arginase - genetics ; Atherosclerosis - genetics ; Atherosclerosis - metabolism ; Atherosclerosis - pathology ; Calcium - metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism ; Cells, Cultured ; Cytosol - metabolism ; Endothelium, Vascular - metabolism ; Endothelium, Vascular - pathology ; Gene Expression Regulation ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mitochondria - metabolism ; Mitochondria - pathology ; Mitochondrial Proteins - metabolism ; Nitric Oxide Synthase Type III - metabolism ; Phosphorylation ; RNA - genetics ; Signal Transduction</subject><ispartof>Journal of the American Heart Association, 2018-09, Vol.7 (18), p.e009579</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1509-d89b646ff0f8f9a8920483bee927cefb63d121045dd8d513f0763ecc2cfabc0b3</citedby><cites>FETCH-LOGICAL-c1509-d89b646ff0f8f9a8920483bee927cefb63d121045dd8d513f0763ecc2cfabc0b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,865,27928,27929</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30371203$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Koo, Bon-Hyeock</creatorcontrib><creatorcontrib>Hwang, Hye-Mi</creatorcontrib><creatorcontrib>Yi, Bong-Gu</creatorcontrib><creatorcontrib>Lim, Hyun Kyo</creatorcontrib><creatorcontrib>Jeon, Byeong Hwa</creatorcontrib><creatorcontrib>Hoe, Kwang Lae</creatorcontrib><creatorcontrib>Kwon, Young-Guen</creatorcontrib><creatorcontrib>Won, Moo-Ho</creatorcontrib><creatorcontrib>Kim, Young Myeong</creatorcontrib><creatorcontrib>Berkowitz, Dan E</creatorcontrib><creatorcontrib>Ryoo, Sungwoo</creatorcontrib><title>Arginase II Contributes to the Ca 2+ /CaMKII/eNOS Axis by Regulating Ca 2+ Concentration Between the Cytosol and Mitochondria in a p32-Dependent Manner</title><title>Journal of the American Heart Association</title><addtitle>J Am Heart Assoc</addtitle><description>Background Arginase II activity contributes to reciprocal regulation of endothelial nitric oxide synthase ( eNOS ). We tested the hypotheses that arginase II activity participates in the regulation of Ca
/Ca
/calmodulin-dependent kinase II / eNOS activation, and this process is dependent on mitochondrial p32. Methods and Results Downregulation of arginase II increased the concentration of cytosolic Ca
([Ca
]c) and decreased mitochondrial Ca
([Ca
]m) in microscopic and fluorescence-activated cell sorting analyses, resulting in augmented eNOS Ser1177 phosphorylation and decreased eNOS Thr495 phosphorylation through Ca
/Ca
/calmodulin-dependent kinase II . These changes were observed in human umbilical vein endothelial cells treated with small interfering RNA against p32 (sip32). Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, fluorescence immunoassay, and ion chromatography, inhibition of arginase II reduced the amount of spermine, a binding molecule, and the release of Ca
from p32. In addition, arginase II gene knockdown using small interfering RNA and knockout arginase II -null mice resulted in reduced p32 protein level. In the aortas of wild-type mice, small interfering RNA against p32 induced eNOS Ser1177 phosphorylation and enhanced NO -dependent vasorelaxation. Arginase activity, p32 protein expression, spermine amount, and [Ca
]m were increased in the aortas from apolipoprotein E (ApoE
) mice fed a high-cholesterol diet, and intravenous administration of small interfering RNA against p32 restored Ca
/Ca
/calmodulin-dependent kinase II -dependent eNOS Ser1177 phosphorylation and improved endothelial dysfunction. The effects of arginase II downregulation were not associated with elevated NO production when tested in aortic endothelia from eNOS knockout mice. Conclusions These data demonstrate a novel function of arginase II in regulation of Ca
-dependent eNOS phosphorylation. This novel mechanism drives arginase activation, mitochondrial dysfunction, endothelial dysfunction, and atherogenesis.</description><subject>Animals</subject><subject>Aorta, Thoracic - metabolism</subject><subject>Aorta, Thoracic - pathology</subject><subject>Arginase - biosynthesis</subject><subject>Arginase - genetics</subject><subject>Atherosclerosis - genetics</subject><subject>Atherosclerosis - metabolism</subject><subject>Atherosclerosis - pathology</subject><subject>Calcium - metabolism</subject><subject>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism</subject><subject>Cells, Cultured</subject><subject>Cytosol - metabolism</subject><subject>Endothelium, Vascular - metabolism</subject><subject>Endothelium, Vascular - pathology</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Knockout</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondria - pathology</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Nitric Oxide Synthase Type III - metabolism</subject><subject>Phosphorylation</subject><subject>RNA - genetics</subject><subject>Signal Transduction</subject><issn>2047-9980</issn><issn>2047-9980</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkEtPwzAQhC0EAlQ4c0N7R2nsuHn4GMKjgRYkHufIsdclqDhRnAr6S_i7GAUQe9nRamak_Qg5YXTKWMLCm3yee5VNKRVxKnbIYURnaSBERnf_6QNy7Nwr9ZNEKY_FPjnglKcsovyQfOb9qrHSIZQlFK0d-qbeDOhgaGF4QSgkRGcQFnJ5W5Yh3t0_Qv7ROKi38ICrzVoOjV39uHxcoW_wt9bCOQ7viHZs2Q6ta9cgrYZlM7TqpbW6byQ0FiR0PAousEOrfRqW0lrsj8iekWuHxz97Qp6vLp-KebC4vy6LfBEoFlMR6EzUySwxhprMCJkJ_3XGa0QRpQpNnXDNIkZnsdaZjhk3NE04KhUpI2tFaz4h4dir-ta5Hk3V9c2b7LcVo9U35eqbsldZNVL2idMx0W3qN9R__l-m_AvYfHbU</recordid><startdate>20180918</startdate><enddate>20180918</enddate><creator>Koo, Bon-Hyeock</creator><creator>Hwang, Hye-Mi</creator><creator>Yi, Bong-Gu</creator><creator>Lim, Hyun Kyo</creator><creator>Jeon, Byeong Hwa</creator><creator>Hoe, Kwang Lae</creator><creator>Kwon, Young-Guen</creator><creator>Won, Moo-Ho</creator><creator>Kim, Young Myeong</creator><creator>Berkowitz, Dan E</creator><creator>Ryoo, Sungwoo</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20180918</creationdate><title>Arginase II Contributes to the Ca 2+ /CaMKII/eNOS Axis by Regulating Ca 2+ Concentration Between the Cytosol and Mitochondria in a p32-Dependent Manner</title><author>Koo, Bon-Hyeock ; Hwang, Hye-Mi ; Yi, Bong-Gu ; Lim, Hyun Kyo ; Jeon, Byeong Hwa ; Hoe, Kwang Lae ; Kwon, Young-Guen ; Won, Moo-Ho ; Kim, Young Myeong ; Berkowitz, Dan E ; Ryoo, Sungwoo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1509-d89b646ff0f8f9a8920483bee927cefb63d121045dd8d513f0763ecc2cfabc0b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Animals</topic><topic>Aorta, Thoracic - metabolism</topic><topic>Aorta, Thoracic - pathology</topic><topic>Arginase - biosynthesis</topic><topic>Arginase - genetics</topic><topic>Atherosclerosis - genetics</topic><topic>Atherosclerosis - metabolism</topic><topic>Atherosclerosis - pathology</topic><topic>Calcium - metabolism</topic><topic>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism</topic><topic>Cells, Cultured</topic><topic>Cytosol - metabolism</topic><topic>Endothelium, Vascular - metabolism</topic><topic>Endothelium, Vascular - pathology</topic><topic>Gene Expression Regulation</topic><topic>Humans</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondria - pathology</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Nitric Oxide Synthase Type III - metabolism</topic><topic>Phosphorylation</topic><topic>RNA - genetics</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koo, Bon-Hyeock</creatorcontrib><creatorcontrib>Hwang, Hye-Mi</creatorcontrib><creatorcontrib>Yi, Bong-Gu</creatorcontrib><creatorcontrib>Lim, Hyun Kyo</creatorcontrib><creatorcontrib>Jeon, Byeong Hwa</creatorcontrib><creatorcontrib>Hoe, Kwang Lae</creatorcontrib><creatorcontrib>Kwon, Young-Guen</creatorcontrib><creatorcontrib>Won, Moo-Ho</creatorcontrib><creatorcontrib>Kim, Young Myeong</creatorcontrib><creatorcontrib>Berkowitz, Dan E</creatorcontrib><creatorcontrib>Ryoo, Sungwoo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Journal of the American Heart Association</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koo, Bon-Hyeock</au><au>Hwang, Hye-Mi</au><au>Yi, Bong-Gu</au><au>Lim, Hyun Kyo</au><au>Jeon, Byeong Hwa</au><au>Hoe, Kwang Lae</au><au>Kwon, Young-Guen</au><au>Won, Moo-Ho</au><au>Kim, Young Myeong</au><au>Berkowitz, Dan E</au><au>Ryoo, Sungwoo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Arginase II Contributes to the Ca 2+ /CaMKII/eNOS Axis by Regulating Ca 2+ Concentration Between the Cytosol and Mitochondria in a p32-Dependent Manner</atitle><jtitle>Journal of the American Heart Association</jtitle><addtitle>J Am Heart Assoc</addtitle><date>2018-09-18</date><risdate>2018</risdate><volume>7</volume><issue>18</issue><spage>e009579</spage><pages>e009579-</pages><issn>2047-9980</issn><eissn>2047-9980</eissn><abstract>Background Arginase II activity contributes to reciprocal regulation of endothelial nitric oxide synthase ( eNOS ). We tested the hypotheses that arginase II activity participates in the regulation of Ca
/Ca
/calmodulin-dependent kinase II / eNOS activation, and this process is dependent on mitochondrial p32. Methods and Results Downregulation of arginase II increased the concentration of cytosolic Ca
([Ca
]c) and decreased mitochondrial Ca
([Ca
]m) in microscopic and fluorescence-activated cell sorting analyses, resulting in augmented eNOS Ser1177 phosphorylation and decreased eNOS Thr495 phosphorylation through Ca
/Ca
/calmodulin-dependent kinase II . These changes were observed in human umbilical vein endothelial cells treated with small interfering RNA against p32 (sip32). Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, fluorescence immunoassay, and ion chromatography, inhibition of arginase II reduced the amount of spermine, a binding molecule, and the release of Ca
from p32. In addition, arginase II gene knockdown using small interfering RNA and knockout arginase II -null mice resulted in reduced p32 protein level. In the aortas of wild-type mice, small interfering RNA against p32 induced eNOS Ser1177 phosphorylation and enhanced NO -dependent vasorelaxation. Arginase activity, p32 protein expression, spermine amount, and [Ca
]m were increased in the aortas from apolipoprotein E (ApoE
) mice fed a high-cholesterol diet, and intravenous administration of small interfering RNA against p32 restored Ca
/Ca
/calmodulin-dependent kinase II -dependent eNOS Ser1177 phosphorylation and improved endothelial dysfunction. The effects of arginase II downregulation were not associated with elevated NO production when tested in aortic endothelia from eNOS knockout mice. Conclusions These data demonstrate a novel function of arginase II in regulation of Ca
-dependent eNOS phosphorylation. This novel mechanism drives arginase activation, mitochondrial dysfunction, endothelial dysfunction, and atherogenesis.</abstract><cop>England</cop><pmid>30371203</pmid><doi>10.1161/JAHA.118.009579</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Online Library (Open Access Collection); PubMed Central |
| subjects | Animals Aorta, Thoracic - metabolism Aorta, Thoracic - pathology Arginase - biosynthesis Arginase - genetics Atherosclerosis - genetics Atherosclerosis - metabolism Atherosclerosis - pathology Calcium - metabolism Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism Cells, Cultured Cytosol - metabolism Endothelium, Vascular - metabolism Endothelium, Vascular - pathology Gene Expression Regulation Humans Male Mice Mice, Inbred C57BL Mice, Knockout Mitochondria - metabolism Mitochondria - pathology Mitochondrial Proteins - metabolism Nitric Oxide Synthase Type III - metabolism Phosphorylation RNA - genetics Signal Transduction |
| title | Arginase II Contributes to the Ca 2+ /CaMKII/eNOS Axis by Regulating Ca 2+ Concentration Between the Cytosol and Mitochondria in a p32-Dependent Manner |
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