Acetoxy drug: Protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates
Polyphenolic acetates are the novel potent enhancers of intracellular nitric oxide. An enhanced intracellular level of Nitric oxide (NO) is essential to ameliorate several pathological conditions of heart and vasculature necessitating the activation of NOS. We have projected in this report the acety...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry 2006-01, Vol.14 (2), p.575-583 |
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| creator | Khurana, Pulkit Kumari, Ranju Vohra, Parag Kumar, Ajit Seema Gupta, Garima Raj, Hanumantharao G. Dwarakanath, Bilikere S. Parmar, Virinder S. Saluja, Daman Bose, Mridula Vij, Anjana Chaudhary, Nabo K. Adhikari, Jawahar S. Tyagi, Yogesh K. Kohli, Ekta |
| description | Polyphenolic acetates are the novel potent enhancers of intracellular nitric oxide.
An enhanced intracellular level of Nitric oxide (NO) is essential to ameliorate several pathological conditions of heart and vasculature necessitating the activation of NOS. We have projected in this report the acetylation of eNOS by polyphenolic peracetates (PA) catalyzed by the novel enzyme acetoxy drug: protein transacetylase (TAase) discovered in our laboratory as an unambiguous way of activating NOS which results in the manifestation of physiological action. The human platelet was chosen as the experimental system in order to validate the aforementioned proposition. PA caused profound irreversible activation of platelet NADPH cytochrome
c reductase mediated by TAase. The convincing biochemical evidences are presented to show that PA could cause acetylation of the reductase domain of NOS leading to the activation of eNOS in tune with their specificities to platelet TAase. As a result, the enhanced level of NO due to activation of platelet eNOS by PA was found to inhibit the ADP-induced platelet aggregation. The present studies highlight for the first time the role of PA as the novel potent agent for enhancing the intracellular NO levels. |
| doi_str_mv | 10.1016/j.bmc.2005.08.044 |
| format | Article |
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An enhanced intracellular level of Nitric oxide (NO) is essential to ameliorate several pathological conditions of heart and vasculature necessitating the activation of NOS. We have projected in this report the acetylation of eNOS by polyphenolic peracetates (PA) catalyzed by the novel enzyme acetoxy drug: protein transacetylase (TAase) discovered in our laboratory as an unambiguous way of activating NOS which results in the manifestation of physiological action. The human platelet was chosen as the experimental system in order to validate the aforementioned proposition. PA caused profound irreversible activation of platelet NADPH cytochrome
c reductase mediated by TAase. The convincing biochemical evidences are presented to show that PA could cause acetylation of the reductase domain of NOS leading to the activation of eNOS in tune with their specificities to platelet TAase. As a result, the enhanced level of NO due to activation of platelet eNOS by PA was found to inhibit the ADP-induced platelet aggregation. The present studies highlight for the first time the role of PA as the novel potent agent for enhancing the intracellular NO levels.</description><identifier>ISSN: 0968-0896</identifier><identifier>EISSN: 1464-3391</identifier><identifier>DOI: 10.1016/j.bmc.2005.08.044</identifier><identifier>PMID: 16214347</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Acetates - chemistry ; Acetates - pharmacology ; Acetylation ; Acyltransferases - metabolism ; Biological and medical sciences ; Blood Platelets - enzymology ; Blood. Blood coagulation. Reticuloendothelial system ; Blotting, Western ; Cardiovascular system ; Catalysis ; Cytochromes c - metabolism ; Enzyme Activation ; Flavonoids - chemistry ; Humans ; Medical sciences ; Microscopy, Confocal ; Miscellaneous ; Nitric oxide ; Nitric oxide synthase ; Nitric Oxide Synthase - metabolism ; Pharmacology. Drug treatments ; Phenols - chemistry ; Platelet aggregation ; Polyphenolic peracetate ; Polyphenols ; Protein acetylation ; Transacetylase</subject><ispartof>Bioorganic & medicinal chemistry, 2006-01, Vol.14 (2), p.575-583</ispartof><rights>2005 Elsevier Ltd</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-5904e7a2e9493a4e184abc471a57ab336a893ade2c214c58ab92ab603f549ddb3</citedby><cites>FETCH-LOGICAL-c447t-5904e7a2e9493a4e184abc471a57ab336a893ade2c214c58ab92ab603f549ddb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bmc.2005.08.044$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17322012$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16214347$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Khurana, Pulkit</creatorcontrib><creatorcontrib>Kumari, Ranju</creatorcontrib><creatorcontrib>Vohra, Parag</creatorcontrib><creatorcontrib>Kumar, Ajit</creatorcontrib><creatorcontrib>Seema</creatorcontrib><creatorcontrib>Gupta, Garima</creatorcontrib><creatorcontrib>Raj, Hanumantharao G.</creatorcontrib><creatorcontrib>Dwarakanath, Bilikere S.</creatorcontrib><creatorcontrib>Parmar, Virinder S.</creatorcontrib><creatorcontrib>Saluja, Daman</creatorcontrib><creatorcontrib>Bose, Mridula</creatorcontrib><creatorcontrib>Vij, Anjana</creatorcontrib><creatorcontrib>Chaudhary, Nabo K.</creatorcontrib><creatorcontrib>Adhikari, Jawahar S.</creatorcontrib><creatorcontrib>Tyagi, Yogesh K.</creatorcontrib><creatorcontrib>Kohli, Ekta</creatorcontrib><title>Acetoxy drug: Protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates</title><title>Bioorganic & medicinal chemistry</title><addtitle>Bioorg Med Chem</addtitle><description>Polyphenolic acetates are the novel potent enhancers of intracellular nitric oxide.
An enhanced intracellular level of Nitric oxide (NO) is essential to ameliorate several pathological conditions of heart and vasculature necessitating the activation of NOS. We have projected in this report the acetylation of eNOS by polyphenolic peracetates (PA) catalyzed by the novel enzyme acetoxy drug: protein transacetylase (TAase) discovered in our laboratory as an unambiguous way of activating NOS which results in the manifestation of physiological action. The human platelet was chosen as the experimental system in order to validate the aforementioned proposition. PA caused profound irreversible activation of platelet NADPH cytochrome
c reductase mediated by TAase. The convincing biochemical evidences are presented to show that PA could cause acetylation of the reductase domain of NOS leading to the activation of eNOS in tune with their specificities to platelet TAase. As a result, the enhanced level of NO due to activation of platelet eNOS by PA was found to inhibit the ADP-induced platelet aggregation. The present studies highlight for the first time the role of PA as the novel potent agent for enhancing the intracellular NO levels.</description><subject>Acetates - chemistry</subject><subject>Acetates - pharmacology</subject><subject>Acetylation</subject><subject>Acyltransferases - metabolism</subject><subject>Biological and medical sciences</subject><subject>Blood Platelets - enzymology</subject><subject>Blood. Blood coagulation. Reticuloendothelial system</subject><subject>Blotting, Western</subject><subject>Cardiovascular system</subject><subject>Catalysis</subject><subject>Cytochromes c - metabolism</subject><subject>Enzyme Activation</subject><subject>Flavonoids - chemistry</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Microscopy, Confocal</subject><subject>Miscellaneous</subject><subject>Nitric oxide</subject><subject>Nitric oxide synthase</subject><subject>Nitric Oxide Synthase - metabolism</subject><subject>Pharmacology. Drug treatments</subject><subject>Phenols - chemistry</subject><subject>Platelet aggregation</subject><subject>Polyphenolic peracetate</subject><subject>Polyphenols</subject><subject>Protein acetylation</subject><subject>Transacetylase</subject><issn>0968-0896</issn><issn>1464-3391</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi0EokvhB3BBvtBbgh07H4ZTVUGLVAkOcLYmzoT1yomD7VQNEv8dr3al3jiN5HneV-OHkLeclZzx5sOh7CdTVozVJetKJuUzsuOykYUQij8nO6aarmCdai7IqxgPjLFKKv6SXPCm4lLIdkf-XhtM_nGjQ1h_faTfg09oZ5oCzBHyanMQkRpI4LY_OFAwyT5Asn6mfqT7dYKZLg4SOkx0tilYQ_2jHZDGbU77Y7jf6OLdtuxx9i6vFwzH5pyJr8mLEVzEN-d5SX5--fzj5q64_3b79eb6vjBStqmoFZPYQoVKKgESeSehN7LlULfQC9FAl98HrEz-lqk76FUFfcPEWEs1DL24JFen3iX43yvGpCcbDToHM_o16pZx1Yi6ySA_gSb4GAOOegl2grBpzvTRuT7o7FwfnWvW6ew8Z96dy9d-wuEpcZacgfdnAKIBN2a3xsYnrhVVxXiVuU8nDrOKB4tBR2NxNjjYgCbpwdv_nPEPoiqiBQ</recordid><startdate>20060115</startdate><enddate>20060115</enddate><creator>Khurana, Pulkit</creator><creator>Kumari, Ranju</creator><creator>Vohra, Parag</creator><creator>Kumar, Ajit</creator><creator>Seema</creator><creator>Gupta, Garima</creator><creator>Raj, Hanumantharao G.</creator><creator>Dwarakanath, Bilikere S.</creator><creator>Parmar, Virinder S.</creator><creator>Saluja, Daman</creator><creator>Bose, Mridula</creator><creator>Vij, Anjana</creator><creator>Chaudhary, Nabo K.</creator><creator>Adhikari, Jawahar S.</creator><creator>Tyagi, Yogesh K.</creator><creator>Kohli, Ekta</creator><general>Elsevier Ltd</general><general>Elsevier Science</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>7X8</scope></search><sort><creationdate>20060115</creationdate><title>Acetoxy drug: Protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates</title><author>Khurana, Pulkit ; Kumari, Ranju ; Vohra, Parag ; Kumar, Ajit ; Seema ; Gupta, Garima ; Raj, Hanumantharao G. ; Dwarakanath, Bilikere S. ; Parmar, Virinder S. ; Saluja, Daman ; Bose, Mridula ; Vij, Anjana ; Chaudhary, Nabo K. ; Adhikari, Jawahar S. ; Tyagi, Yogesh K. ; Kohli, Ekta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-5904e7a2e9493a4e184abc471a57ab336a893ade2c214c58ab92ab603f549ddb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Acetates - chemistry</topic><topic>Acetates - pharmacology</topic><topic>Acetylation</topic><topic>Acyltransferases - metabolism</topic><topic>Biological and medical sciences</topic><topic>Blood Platelets - enzymology</topic><topic>Blood. 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An enhanced intracellular level of Nitric oxide (NO) is essential to ameliorate several pathological conditions of heart and vasculature necessitating the activation of NOS. We have projected in this report the acetylation of eNOS by polyphenolic peracetates (PA) catalyzed by the novel enzyme acetoxy drug: protein transacetylase (TAase) discovered in our laboratory as an unambiguous way of activating NOS which results in the manifestation of physiological action. The human platelet was chosen as the experimental system in order to validate the aforementioned proposition. PA caused profound irreversible activation of platelet NADPH cytochrome
c reductase mediated by TAase. The convincing biochemical evidences are presented to show that PA could cause acetylation of the reductase domain of NOS leading to the activation of eNOS in tune with their specificities to platelet TAase. As a result, the enhanced level of NO due to activation of platelet eNOS by PA was found to inhibit the ADP-induced platelet aggregation. The present studies highlight for the first time the role of PA as the novel potent agent for enhancing the intracellular NO levels.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>16214347</pmid><doi>10.1016/j.bmc.2005.08.044</doi><tpages>9</tpages></addata></record> |
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| ispartof | Bioorganic & medicinal chemistry, 2006-01, Vol.14 (2), p.575-583 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Acetates - chemistry Acetates - pharmacology Acetylation Acyltransferases - metabolism Biological and medical sciences Blood Platelets - enzymology Blood. Blood coagulation. Reticuloendothelial system Blotting, Western Cardiovascular system Catalysis Cytochromes c - metabolism Enzyme Activation Flavonoids - chemistry Humans Medical sciences Microscopy, Confocal Miscellaneous Nitric oxide Nitric oxide synthase Nitric Oxide Synthase - metabolism Pharmacology. Drug treatments Phenols - chemistry Platelet aggregation Polyphenolic peracetate Polyphenols Protein acetylation Transacetylase |
| title | Acetoxy drug: Protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates |
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