Identification of a selective inhibitor of murine intestinal alkaline phosphatase (ML260) by concurrent ultra-high throughput screening against human and mouse isozymes
Alkaline phosphatase (AP) isozymes are present in a wide range of species from bacteria to man and are capable of dephosphorylation and transphosphorylation of a wide spectrum of substrates in vitro. In humans, four AP isozymes have been identified—one tissue-nonspecific (TNAP) and three tissue-spec...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry letters 2014-02, Vol.24 (3), p.1000-1004 |
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| creator | Ardecky, Robert J. Bobkova, Ekaterina V. Kiffer-Moreira, Tina Brown, Brock Ganji, Santhi Zou, Jiwen Pass, Ian Narisawa, Sonoko Iano, Flávia Godoy Rosenstein, Craig Cheltsov, Anton Rascon, Justin Hedrick, Michael Gasior, Carlton Forster, Anita Shi, Shenghua Dahl, Russell Vasile, Stefan Su, Ying Sergienko, Eduard Chung, Thomas D.Y. Kaunitz, Jonathan Hoylaerts, Marc F. Pinkerton, Anthony B. Millán, José Luis |
| description | Alkaline phosphatase (AP) isozymes are present in a wide range of species from bacteria to man and are capable of dephosphorylation and transphosphorylation of a wide spectrum of substrates in vitro. In humans, four AP isozymes have been identified—one tissue-nonspecific (TNAP) and three tissue-specific—named according to the tissue of their predominant expression: intestinal (IAP), placental (PLAP) and germ cell (GCAP) APs. Modulation of activity of the different AP isozymes may have therapeutic implications in distinct diseases and cellular processes. For instance, changes in the level of IAP activity can affect gut mucosa tolerance to microbial invasion due to the ability of IAP to detoxify bacterial endotoxins, alter the absorption of fatty acids and affect ectopurinergic regulation of duodenal bicarbonate secretion. To identify isozyme selective modulators of the human and mouse IAPs, we developed a series of murine duodenal IAP (Akp3-encoded dIAP isozyme), human IAP (hIAP), PLAP, and TNAP assays. High throughput screening and subsequent SAR efforts generated a potent inhibitor of dIAP, ML260, with specificity for the Akp3-, compared to the Akp5- and Akp6-encoded mouse isozymes. |
| doi_str_mv | 10.1016/j.bmcl.2013.12.043 |
| format | Article |
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In humans, four AP isozymes have been identified—one tissue-nonspecific (TNAP) and three tissue-specific—named according to the tissue of their predominant expression: intestinal (IAP), placental (PLAP) and germ cell (GCAP) APs. Modulation of activity of the different AP isozymes may have therapeutic implications in distinct diseases and cellular processes. For instance, changes in the level of IAP activity can affect gut mucosa tolerance to microbial invasion due to the ability of IAP to detoxify bacterial endotoxins, alter the absorption of fatty acids and affect ectopurinergic regulation of duodenal bicarbonate secretion. To identify isozyme selective modulators of the human and mouse IAPs, we developed a series of murine duodenal IAP (Akp3-encoded dIAP isozyme), human IAP (hIAP), PLAP, and TNAP assays. High throughput screening and subsequent SAR efforts generated a potent inhibitor of dIAP, ML260, with specificity for the Akp3-, compared to the Akp5- and Akp6-encoded mouse isozymes.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/j.bmcl.2013.12.043</identifier><identifier>PMID: 24412070</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Acetanilides - chemistry ; Acetanilides - isolation & purification ; Acetanilides - pharmacology ; Alkaline phosphatase ; Alkaline Phosphatase - antagonists & inhibitors ; Animals ; Enzyme Activation - drug effects ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - isolation & purification ; Enzyme Inhibitors - pharmacology ; Enzymes ; Humans ; Inflammatory bowel disease ; Inhibitors ; Intestinal alkaline phosphatase ; Mice ; Protein Isoforms - chemistry ; Sulfonamides - chemistry ; Sulfonamides - isolation & purification ; Sulfonamides - pharmacology</subject><ispartof>Bioorganic & medicinal chemistry letters, 2014-02, Vol.24 (3), p.1000-1004</ispartof><rights>2013 Elsevier Ltd</rights><rights>Copyright © 2013 Elsevier Ltd. All rights reserved.</rights><rights>2013 Elsevier Ltd. All rights reserved. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c488t-dd8188ce7313f01d7b29c77f5efa5b979645cc1cdc83d6b85de9e73ebb5a3db63</citedby><cites>FETCH-LOGICAL-c488t-dd8188ce7313f01d7b29c77f5efa5b979645cc1cdc83d6b85de9e73ebb5a3db63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bmcl.2013.12.043$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,315,782,786,887,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24412070$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ardecky, Robert J.</creatorcontrib><creatorcontrib>Bobkova, Ekaterina V.</creatorcontrib><creatorcontrib>Kiffer-Moreira, Tina</creatorcontrib><creatorcontrib>Brown, Brock</creatorcontrib><creatorcontrib>Ganji, Santhi</creatorcontrib><creatorcontrib>Zou, Jiwen</creatorcontrib><creatorcontrib>Pass, Ian</creatorcontrib><creatorcontrib>Narisawa, Sonoko</creatorcontrib><creatorcontrib>Iano, Flávia Godoy</creatorcontrib><creatorcontrib>Rosenstein, Craig</creatorcontrib><creatorcontrib>Cheltsov, Anton</creatorcontrib><creatorcontrib>Rascon, Justin</creatorcontrib><creatorcontrib>Hedrick, Michael</creatorcontrib><creatorcontrib>Gasior, Carlton</creatorcontrib><creatorcontrib>Forster, Anita</creatorcontrib><creatorcontrib>Shi, Shenghua</creatorcontrib><creatorcontrib>Dahl, Russell</creatorcontrib><creatorcontrib>Vasile, Stefan</creatorcontrib><creatorcontrib>Su, Ying</creatorcontrib><creatorcontrib>Sergienko, Eduard</creatorcontrib><creatorcontrib>Chung, Thomas D.Y.</creatorcontrib><creatorcontrib>Kaunitz, Jonathan</creatorcontrib><creatorcontrib>Hoylaerts, Marc F.</creatorcontrib><creatorcontrib>Pinkerton, Anthony B.</creatorcontrib><creatorcontrib>Millán, José Luis</creatorcontrib><title>Identification of a selective inhibitor of murine intestinal alkaline phosphatase (ML260) by concurrent ultra-high throughput screening against human and mouse isozymes</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>Alkaline phosphatase (AP) isozymes are present in a wide range of species from bacteria to man and are capable of dephosphorylation and transphosphorylation of a wide spectrum of substrates in vitro. 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High throughput screening and subsequent SAR efforts generated a potent inhibitor of dIAP, ML260, with specificity for the Akp3-, compared to the Akp5- and Akp6-encoded mouse isozymes.</description><subject>Acetanilides - chemistry</subject><subject>Acetanilides - isolation & purification</subject><subject>Acetanilides - pharmacology</subject><subject>Alkaline phosphatase</subject><subject>Alkaline Phosphatase - antagonists & inhibitors</subject><subject>Animals</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - isolation & purification</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzymes</subject><subject>Humans</subject><subject>Inflammatory bowel disease</subject><subject>Inhibitors</subject><subject>Intestinal alkaline phosphatase</subject><subject>Mice</subject><subject>Protein Isoforms - chemistry</subject><subject>Sulfonamides - chemistry</subject><subject>Sulfonamides - isolation & purification</subject><subject>Sulfonamides - pharmacology</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFksuKFDEUhgtRnHb0BVxIluOiytzqEhBhGLwMtLhRcBdSyamutFVJm6Qa2ifyMU3R46AbXQXO-c6fc_mL4jnBFcGkebWv-llPFcWEVYRWmLMHxYbwhpeM4_phscGiwWUn-NeL4kmMe4wJx5w_Li4o54TiFm-Kn7cGXLKD1SpZ75AfkEIRJtDJHgFZN9reJh_WxLwE69ZYgpisUxNS0zc1rbHD6ONhVElFQFcft7TBL1F_Qto7vYSQf0DLlIIqR7sbURqDX3bjYUko6gDgrNshtVPWxYTGZVYOKWfQ7JesZqP_cZohPi0eDWqK8OzuvSy-vHv7-eZDuf30_vbmeltq3nWpNKYjXaehZYQNmJi2p0K37VDDoOpetKLhtdZEG90x0_RdbUBkGPq-Vsz0Dbss3px1D0s_g9G596AmeQh2VuEkvbLy74yzo9z5o2SCM0pwFri6Ewj--5I3JWcbNUyTcpAnkqQmTcvbltX_R7mgjeioEBmlZ1QHH2OA4b4jguXqBrmXqxvk6gZJqMxuyEUv_pzlvuT3-TPw-gxA3ujRQpBRW3AajA3ZAdJ4-y_9Xy6MzAg</recordid><startdate>20140201</startdate><enddate>20140201</enddate><creator>Ardecky, Robert J.</creator><creator>Bobkova, Ekaterina V.</creator><creator>Kiffer-Moreira, Tina</creator><creator>Brown, Brock</creator><creator>Ganji, Santhi</creator><creator>Zou, Jiwen</creator><creator>Pass, Ian</creator><creator>Narisawa, Sonoko</creator><creator>Iano, Flávia Godoy</creator><creator>Rosenstein, Craig</creator><creator>Cheltsov, Anton</creator><creator>Rascon, Justin</creator><creator>Hedrick, Michael</creator><creator>Gasior, Carlton</creator><creator>Forster, Anita</creator><creator>Shi, Shenghua</creator><creator>Dahl, Russell</creator><creator>Vasile, Stefan</creator><creator>Su, Ying</creator><creator>Sergienko, Eduard</creator><creator>Chung, Thomas D.Y.</creator><creator>Kaunitz, Jonathan</creator><creator>Hoylaerts, Marc F.</creator><creator>Pinkerton, Anthony B.</creator><creator>Millán, José Luis</creator><general>Elsevier Ltd</general><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>5PM</scope></search><sort><creationdate>20140201</creationdate><title>Identification of a selective inhibitor of murine intestinal alkaline phosphatase (ML260) by concurrent ultra-high throughput screening against human and mouse isozymes</title><author>Ardecky, Robert J. ; 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In humans, four AP isozymes have been identified—one tissue-nonspecific (TNAP) and three tissue-specific—named according to the tissue of their predominant expression: intestinal (IAP), placental (PLAP) and germ cell (GCAP) APs. Modulation of activity of the different AP isozymes may have therapeutic implications in distinct diseases and cellular processes. For instance, changes in the level of IAP activity can affect gut mucosa tolerance to microbial invasion due to the ability of IAP to detoxify bacterial endotoxins, alter the absorption of fatty acids and affect ectopurinergic regulation of duodenal bicarbonate secretion. To identify isozyme selective modulators of the human and mouse IAPs, we developed a series of murine duodenal IAP (Akp3-encoded dIAP isozyme), human IAP (hIAP), PLAP, and TNAP assays. High throughput screening and subsequent SAR efforts generated a potent inhibitor of dIAP, ML260, with specificity for the Akp3-, compared to the Akp5- and Akp6-encoded mouse isozymes.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>24412070</pmid><doi>10.1016/j.bmcl.2013.12.043</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Bioorganic & medicinal chemistry letters, 2014-02, Vol.24 (3), p.1000-1004 |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Acetanilides - chemistry Acetanilides - isolation & purification Acetanilides - pharmacology Alkaline phosphatase Alkaline Phosphatase - antagonists & inhibitors Animals Enzyme Activation - drug effects Enzyme Inhibitors - chemistry Enzyme Inhibitors - isolation & purification Enzyme Inhibitors - pharmacology Enzymes Humans Inflammatory bowel disease Inhibitors Intestinal alkaline phosphatase Mice Protein Isoforms - chemistry Sulfonamides - chemistry Sulfonamides - isolation & purification Sulfonamides - pharmacology |
| title | Identification of a selective inhibitor of murine intestinal alkaline phosphatase (ML260) by concurrent ultra-high throughput screening against human and mouse isozymes |
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