A new role of Pro-73 of p47phox in the activation of neutrophil NADPH oxidase
The PX domain of p47phox is thought to be involved in autoinhibition. However, when the domain was deleted, the ability to activate the phagocyte NADPH oxidase was markedly diminished. We have mutated the proline-rich region of the PX domain and examined the mutants for the ability to activate. Subs...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2003-08, Vol.416 (1), p.92-100 |
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| creator | Nagasawa, Teruaki Ebisu, Kentaro Inoue, Yasuyuki Miyano, Kei Tamura, Minoru |
| description | The PX domain of p47phox is thought to be involved in autoinhibition. However, when the domain was deleted, the ability to activate the phagocyte NADPH oxidase was markedly diminished. We have mutated the proline-rich region of the PX domain and examined the mutants for the ability to activate. Substitution of Gln for Pro-73 of p47phox(1-286) (P73Q) resulted in a considerably lower activity than the wild type and P73Q had a much lower affinity for the oxidase complex. Whereas, Gln substitution for Pro-76 (P76Q) showed a slightly enhanced activation and the mutant had a slightly higher affinity for the complex than the wild type. Affinity for p67phox(1-210) was slightly decreased either by P73Q or P76Q. Optimal SDS concentration for the activation was lowered by these mutations. Binding of PX domain with phosphatidylinositol-3,4-bisphosphate was diminished by P73Q mutation. The results in this study suggest that Pro-73 has a role in interaction with the catalytic component cytochrome b558. |
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However, when the domain was deleted, the ability to activate the phagocyte NADPH oxidase was markedly diminished. We have mutated the proline-rich region of the PX domain and examined the mutants for the ability to activate. Substitution of Gln for Pro-73 of p47phox(1-286) (P73Q) resulted in a considerably lower activity than the wild type and P73Q had a much lower affinity for the oxidase complex. Whereas, Gln substitution for Pro-76 (P76Q) showed a slightly enhanced activation and the mutant had a slightly higher affinity for the complex than the wild type. Affinity for p67phox(1-210) was slightly decreased either by P73Q or P76Q. Optimal SDS concentration for the activation was lowered by these mutations. Binding of PX domain with phosphatidylinositol-3,4-bisphosphate was diminished by P73Q mutation. The results in this study suggest that Pro-73 has a role in interaction with the catalytic component cytochrome b558.</description><identifier>ISSN: 0003-9861</identifier><identifier>PMID: 12859985</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Motifs ; Cells, Cultured ; Circular Dichroism ; Cytochrome b Group - metabolism ; Enzyme Activation - physiology ; Humans ; Kinetics ; Mutation ; NADPH Oxidases - metabolism ; Neutrophils - enzymology ; Neutrophils - metabolism ; Phosphatidylinositol Phosphates - metabolism ; Phospholipids - metabolism ; Phosphoproteins - chemistry ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Proline - genetics ; Proline - metabolism ; Protein Structure, Tertiary ; rac GTP-Binding Proteins - genetics ; rac GTP-Binding Proteins - metabolism ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Sodium Dodecyl Sulfate - chemistry</subject><ispartof>Archives of biochemistry and biophysics, 2003-08, Vol.416 (1), p.92-100</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12859985$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nagasawa, Teruaki</creatorcontrib><creatorcontrib>Ebisu, Kentaro</creatorcontrib><creatorcontrib>Inoue, Yasuyuki</creatorcontrib><creatorcontrib>Miyano, Kei</creatorcontrib><creatorcontrib>Tamura, Minoru</creatorcontrib><title>A new role of Pro-73 of p47phox in the activation of neutrophil NADPH oxidase</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The PX domain of p47phox is thought to be involved in autoinhibition. However, when the domain was deleted, the ability to activate the phagocyte NADPH oxidase was markedly diminished. We have mutated the proline-rich region of the PX domain and examined the mutants for the ability to activate. Substitution of Gln for Pro-73 of p47phox(1-286) (P73Q) resulted in a considerably lower activity than the wild type and P73Q had a much lower affinity for the oxidase complex. Whereas, Gln substitution for Pro-76 (P76Q) showed a slightly enhanced activation and the mutant had a slightly higher affinity for the complex than the wild type. Affinity for p67phox(1-210) was slightly decreased either by P73Q or P76Q. Optimal SDS concentration for the activation was lowered by these mutations. Binding of PX domain with phosphatidylinositol-3,4-bisphosphate was diminished by P73Q mutation. The results in this study suggest that Pro-73 has a role in interaction with the catalytic component cytochrome b558.</description><subject>Amino Acid Motifs</subject><subject>Cells, Cultured</subject><subject>Circular Dichroism</subject><subject>Cytochrome b Group - metabolism</subject><subject>Enzyme Activation - physiology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Mutation</subject><subject>NADPH Oxidases - metabolism</subject><subject>Neutrophils - enzymology</subject><subject>Neutrophils - metabolism</subject><subject>Phosphatidylinositol Phosphates - metabolism</subject><subject>Phospholipids - metabolism</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Proline - genetics</subject><subject>Proline - metabolism</subject><subject>Protein Structure, Tertiary</subject><subject>rac GTP-Binding Proteins - genetics</subject><subject>rac GTP-Binding Proteins - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sodium Dodecyl Sulfate - chemistry</subject><issn>0003-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1jz1PwzAYhD2AaCn8BeSJLdLr2G_sjFH5KFKBDt0jx7EVoyQOcQLl39OKMt1J99xJd0GWAMCTXGVsQa5j_ABgTGTpFVmwVGGeK1yS14L29puOobU0OLobQyL5yQ1CDk04UN_TqbFUm8l_6cmH_hT2dp7GMDS-pW_Fw25Dw8HXOtobcul0G-3tWVdk__S4X2-S7fvzy7rYJgMKTBhCbpxESHV-9LyWiEY7kKgwM6moGNRGCQUoQTpuqqoG5AIytE6l4PiK3P_NDmP4nG2cys5HY9tW9zbMsZQcOTsWjuDdGZyrztblMPpOjz_l_3_-C8_jUss</recordid><startdate>20030801</startdate><enddate>20030801</enddate><creator>Nagasawa, Teruaki</creator><creator>Ebisu, Kentaro</creator><creator>Inoue, Yasuyuki</creator><creator>Miyano, Kei</creator><creator>Tamura, Minoru</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20030801</creationdate><title>A new role of Pro-73 of p47phox in the activation of neutrophil NADPH oxidase</title><author>Nagasawa, Teruaki ; Ebisu, Kentaro ; Inoue, Yasuyuki ; Miyano, Kei ; Tamura, Minoru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p545-1509cf7502a91503d755caf075856c24b10dc84805707f3cbbd0534065ef820f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Motifs</topic><topic>Cells, Cultured</topic><topic>Circular Dichroism</topic><topic>Cytochrome b Group - metabolism</topic><topic>Enzyme Activation - physiology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Mutation</topic><topic>NADPH Oxidases - metabolism</topic><topic>Neutrophils - enzymology</topic><topic>Neutrophils - metabolism</topic><topic>Phosphatidylinositol Phosphates - metabolism</topic><topic>Phospholipids - metabolism</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Proline - genetics</topic><topic>Proline - metabolism</topic><topic>Protein Structure, Tertiary</topic><topic>rac GTP-Binding Proteins - genetics</topic><topic>rac GTP-Binding Proteins - metabolism</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sodium Dodecyl Sulfate - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagasawa, Teruaki</creatorcontrib><creatorcontrib>Ebisu, Kentaro</creatorcontrib><creatorcontrib>Inoue, Yasuyuki</creatorcontrib><creatorcontrib>Miyano, Kei</creatorcontrib><creatorcontrib>Tamura, Minoru</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</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>Nagasawa, Teruaki</au><au>Ebisu, Kentaro</au><au>Inoue, Yasuyuki</au><au>Miyano, Kei</au><au>Tamura, Minoru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A new role of Pro-73 of p47phox in the activation of neutrophil NADPH oxidase</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2003-08-01</date><risdate>2003</risdate><volume>416</volume><issue>1</issue><spage>92</spage><epage>100</epage><pages>92-100</pages><issn>0003-9861</issn><abstract>The PX domain of p47phox is thought to be involved in autoinhibition. However, when the domain was deleted, the ability to activate the phagocyte NADPH oxidase was markedly diminished. We have mutated the proline-rich region of the PX domain and examined the mutants for the ability to activate. Substitution of Gln for Pro-73 of p47phox(1-286) (P73Q) resulted in a considerably lower activity than the wild type and P73Q had a much lower affinity for the oxidase complex. Whereas, Gln substitution for Pro-76 (P76Q) showed a slightly enhanced activation and the mutant had a slightly higher affinity for the complex than the wild type. Affinity for p67phox(1-210) was slightly decreased either by P73Q or P76Q. Optimal SDS concentration for the activation was lowered by these mutations. Binding of PX domain with phosphatidylinositol-3,4-bisphosphate was diminished by P73Q mutation. The results in this study suggest that Pro-73 has a role in interaction with the catalytic component cytochrome b558.</abstract><cop>United States</cop><pmid>12859985</pmid><tpages>9</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Motifs Cells, Cultured Circular Dichroism Cytochrome b Group - metabolism Enzyme Activation - physiology Humans Kinetics Mutation NADPH Oxidases - metabolism Neutrophils - enzymology Neutrophils - metabolism Phosphatidylinositol Phosphates - metabolism Phospholipids - metabolism Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - metabolism Proline - genetics Proline - metabolism Protein Structure, Tertiary rac GTP-Binding Proteins - genetics rac GTP-Binding Proteins - metabolism Recombinant Proteins - genetics Recombinant Proteins - metabolism Sodium Dodecyl Sulfate - chemistry |
| title | A new role of Pro-73 of p47phox in the activation of neutrophil NADPH oxidase |
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