Loading…

Protein–Protein Interactions: Inhibition of Mammalian Carbonic Anhydrases I–XV by the Murine Inhibitor of Carbonic Anhydrase and Other Members of the Transferrin Family

The murine inhibitor of carbonic anhydrase (mICA), a member of the transferrin (TF) superfamily of proteins, together with human holo- and apoTF and lactoferrin (LF) were assessed as inhibitors of all catalytically active mammalian (h = human, m = murine) CA isoforms, from CA I to CA XV. mICA was a...

Full description

Saved in:

Bibliographic Details
Published in:	Journal of medicinal chemistry 2012-06, Vol.55 (11), p.5529-5535
Main Authors:	Durdagi, Serdar, Vullo, Daniela, Pan, Peiwen, Kähkönen, Niklas, Määttä, Juha A, Hytönen, Vesa P, Scozzafava, Andrea, Parkkila, Seppo, Supuran, Claudiu T
Format:	Article
Language:	English
Subjects:	Animals Apoproteins - metabolism Biological Assay Biosensing Techniques Calorimetry, Differential Scanning Carbonic Anhydrases - metabolism Humans Isoenzymes - antagonists & inhibitors Isoenzymes - metabolism Mice Protein Binding Protein Denaturation Protein Interaction Mapping Transferrins - metabolism
Citations:	Items that this one cites Items that cite this one
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

cited_by	cdi_FETCH-LOGICAL-a315t-7caf1a2fa4f6255fd1df2d575975b11c0341bbdb7e7b00fd1d8dd7279b1f24b23
cites	cdi_FETCH-LOGICAL-a315t-7caf1a2fa4f6255fd1df2d575975b11c0341bbdb7e7b00fd1d8dd7279b1f24b23
container_end_page	5535
container_issue	11
container_start_page	5529
container_title	Journal of medicinal chemistry
container_volume	55
creator	Durdagi, Serdar Vullo, Daniela Pan, Peiwen Kähkönen, Niklas Määttä, Juha A Hytönen, Vesa P Scozzafava, Andrea Parkkila, Seppo Supuran, Claudiu T
description	The murine inhibitor of carbonic anhydrase (mICA), a member of the transferrin (TF) superfamily of proteins, together with human holo- and apoTF and lactoferrin (LF) were assessed as inhibitors of all catalytically active mammalian (h = human, m = murine) CA isoforms, from CA I to CA XV. mICA was a low nanomolar to subnanomolar inhibitor of hCAs I, II, III, VA, VB, VII and mCAs XV (K I of 0.7–44.0 nM) and inhibited the remaining isoforms with K I of 185.5–469 nM. hTF, apoTF, and hLF were inhibitors of most of these CAs but with reduced efficiency compared to mICA (K I of 18.9–453.8 nM). Biacore surface plasmon resonance and differential scanning calorimetry experiments were also used for obtaining more insights into the interaction between these proteins, which may be useful for drug design of protein-based CA inhibitors.
doi_str_mv	10.1021/jm3004587
format	article
fullrecord	<record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1020832469</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1020832469</sourcerecordid><originalsourceid>FETCH-LOGICAL-a315t-7caf1a2fa4f6255fd1df2d575975b11c0341bbdb7e7b00fd1d8dd7279b1f24b23</originalsourceid><addsrcrecordid>eNptkbFu2zAQhomgReKkGfoCBZcCzaCWPImm3C0wmsZAjHRIi2zCUSRhGhKZktLgre_Q18hT5UlKwU6WdLo78Ps_4HiEvOfsM2fAv2z7krFK1PKIzLgAVlQ1q96QGWMABcyhPCGnKW0ZYyWH8picAAhZM5Az8vgjhsE4__Tn76GjKz-YiO3ggk9f87Rxyk0DDZause-xc-jpEqMK3rX00m92OmIyia6y5f4XVTs6bAxdj9F58ywIccq_TlH0mt5mPtK16ZWJaeKm_F1En6yJ2UKvsHfd7h15a7FL5vxQz8jPq293y-vi5vb7anl5U2DJxVDIFi1HsFjZOQhhNdcWtJBiIYXivGVlxZXSShqpGJuea60lyIXiFioF5Rn5tPc-xPB7NGloepda03XoTRhTkz-d1SVU80VGL_ZoG0NK0djmIboe4y5DE8ebl-Nk9sNBO6re6Bfy-RoZ-LgHsE3NNozR5y3_I_oHYqiaIA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1020832469</pqid></control><display><type>article</type><title>Protein–Protein Interactions: Inhibition of Mammalian Carbonic Anhydrases I–XV by the Murine Inhibitor of Carbonic Anhydrase and Other Members of the Transferrin Family</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)</source><creator>Durdagi, Serdar ; Vullo, Daniela ; Pan, Peiwen ; Kähkönen, Niklas ; Määttä, Juha A ; Hytönen, Vesa P ; Scozzafava, Andrea ; Parkkila, Seppo ; Supuran, Claudiu T</creator><creatorcontrib>Durdagi, Serdar ; Vullo, Daniela ; Pan, Peiwen ; Kähkönen, Niklas ; Määttä, Juha A ; Hytönen, Vesa P ; Scozzafava, Andrea ; Parkkila, Seppo ; Supuran, Claudiu T</creatorcontrib><description>The murine inhibitor of carbonic anhydrase (mICA), a member of the transferrin (TF) superfamily of proteins, together with human holo- and apoTF and lactoferrin (LF) were assessed as inhibitors of all catalytically active mammalian (h = human, m = murine) CA isoforms, from CA I to CA XV. mICA was a low nanomolar to subnanomolar inhibitor of hCAs I, II, III, VA, VB, VII and mCAs XV (K I of 0.7–44.0 nM) and inhibited the remaining isoforms with K I of 185.5–469 nM. hTF, apoTF, and hLF were inhibitors of most of these CAs but with reduced efficiency compared to mICA (K I of 18.9–453.8 nM). Biacore surface plasmon resonance and differential scanning calorimetry experiments were also used for obtaining more insights into the interaction between these proteins, which may be useful for drug design of protein-based CA inhibitors.</description><identifier>ISSN: 0022-2623</identifier><identifier>EISSN: 1520-4804</identifier><identifier>DOI: 10.1021/jm3004587</identifier><identifier>PMID: 22578027</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Apoproteins - metabolism ; Biological Assay ; Biosensing Techniques ; Calorimetry, Differential Scanning ; Carbonic Anhydrases - metabolism ; Humans ; Isoenzymes - antagonists & inhibitors ; Isoenzymes - metabolism ; Mice ; Protein Binding ; Protein Denaturation ; Protein Interaction Mapping ; Transferrins - metabolism</subject><ispartof>Journal of medicinal chemistry, 2012-06, Vol.55 (11), p.5529-5535</ispartof><rights>Copyright © 2012 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a315t-7caf1a2fa4f6255fd1df2d575975b11c0341bbdb7e7b00fd1d8dd7279b1f24b23</citedby><cites>FETCH-LOGICAL-a315t-7caf1a2fa4f6255fd1df2d575975b11c0341bbdb7e7b00fd1d8dd7279b1f24b23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22578027$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Durdagi, Serdar</creatorcontrib><creatorcontrib>Vullo, Daniela</creatorcontrib><creatorcontrib>Pan, Peiwen</creatorcontrib><creatorcontrib>Kähkönen, Niklas</creatorcontrib><creatorcontrib>Määttä, Juha A</creatorcontrib><creatorcontrib>Hytönen, Vesa P</creatorcontrib><creatorcontrib>Scozzafava, Andrea</creatorcontrib><creatorcontrib>Parkkila, Seppo</creatorcontrib><creatorcontrib>Supuran, Claudiu T</creatorcontrib><title>Protein–Protein Interactions: Inhibition of Mammalian Carbonic Anhydrases I–XV by the Murine Inhibitor of Carbonic Anhydrase and Other Members of the Transferrin Family</title><title>Journal of medicinal chemistry</title><addtitle>J. Med. Chem</addtitle><description>The murine inhibitor of carbonic anhydrase (mICA), a member of the transferrin (TF) superfamily of proteins, together with human holo- and apoTF and lactoferrin (LF) were assessed as inhibitors of all catalytically active mammalian (h = human, m = murine) CA isoforms, from CA I to CA XV. mICA was a low nanomolar to subnanomolar inhibitor of hCAs I, II, III, VA, VB, VII and mCAs XV (K I of 0.7–44.0 nM) and inhibited the remaining isoforms with K I of 185.5–469 nM. hTF, apoTF, and hLF were inhibitors of most of these CAs but with reduced efficiency compared to mICA (K I of 18.9–453.8 nM). Biacore surface plasmon resonance and differential scanning calorimetry experiments were also used for obtaining more insights into the interaction between these proteins, which may be useful for drug design of protein-based CA inhibitors.</description><subject>Animals</subject><subject>Apoproteins - metabolism</subject><subject>Biological Assay</subject><subject>Biosensing Techniques</subject><subject>Calorimetry, Differential Scanning</subject><subject>Carbonic Anhydrases - metabolism</subject><subject>Humans</subject><subject>Isoenzymes - antagonists & inhibitors</subject><subject>Isoenzymes - metabolism</subject><subject>Mice</subject><subject>Protein Binding</subject><subject>Protein Denaturation</subject><subject>Protein Interaction Mapping</subject><subject>Transferrins - metabolism</subject><issn>0022-2623</issn><issn>1520-4804</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNptkbFu2zAQhomgReKkGfoCBZcCzaCWPImm3C0wmsZAjHRIi2zCUSRhGhKZktLgre_Q18hT5UlKwU6WdLo78Ps_4HiEvOfsM2fAv2z7krFK1PKIzLgAVlQ1q96QGWMABcyhPCGnKW0ZYyWH8picAAhZM5Az8vgjhsE4__Tn76GjKz-YiO3ggk9f87Rxyk0DDZause-xc-jpEqMK3rX00m92OmIyia6y5f4XVTs6bAxdj9F58ywIccq_TlH0mt5mPtK16ZWJaeKm_F1En6yJ2UKvsHfd7h15a7FL5vxQz8jPq293y-vi5vb7anl5U2DJxVDIFi1HsFjZOQhhNdcWtJBiIYXivGVlxZXSShqpGJuea60lyIXiFioF5Rn5tPc-xPB7NGloepda03XoTRhTkz-d1SVU80VGL_ZoG0NK0djmIboe4y5DE8ebl-Nk9sNBO6re6Bfy-RoZ-LgHsE3NNozR5y3_I_oHYqiaIA</recordid><startdate>20120614</startdate><enddate>20120614</enddate><creator>Durdagi, Serdar</creator><creator>Vullo, Daniela</creator><creator>Pan, Peiwen</creator><creator>Kähkönen, Niklas</creator><creator>Määttä, Juha A</creator><creator>Hytönen, Vesa P</creator><creator>Scozzafava, Andrea</creator><creator>Parkkila, Seppo</creator><creator>Supuran, Claudiu T</creator><general>American Chemical Society</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></search><sort><creationdate>20120614</creationdate><title>Protein–Protein Interactions: Inhibition of Mammalian Carbonic Anhydrases I–XV by the Murine Inhibitor of Carbonic Anhydrase and Other Members of the Transferrin Family</title><author>Durdagi, Serdar ; Vullo, Daniela ; Pan, Peiwen ; Kähkönen, Niklas ; Määttä, Juha A ; Hytönen, Vesa P ; Scozzafava, Andrea ; Parkkila, Seppo ; Supuran, Claudiu T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a315t-7caf1a2fa4f6255fd1df2d575975b11c0341bbdb7e7b00fd1d8dd7279b1f24b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Apoproteins - metabolism</topic><topic>Biological Assay</topic><topic>Biosensing Techniques</topic><topic>Calorimetry, Differential Scanning</topic><topic>Carbonic Anhydrases - metabolism</topic><topic>Humans</topic><topic>Isoenzymes - antagonists & inhibitors</topic><topic>Isoenzymes - metabolism</topic><topic>Mice</topic><topic>Protein Binding</topic><topic>Protein Denaturation</topic><topic>Protein Interaction Mapping</topic><topic>Transferrins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Durdagi, Serdar</creatorcontrib><creatorcontrib>Vullo, Daniela</creatorcontrib><creatorcontrib>Pan, Peiwen</creatorcontrib><creatorcontrib>Kähkönen, Niklas</creatorcontrib><creatorcontrib>Määttä, Juha A</creatorcontrib><creatorcontrib>Hytönen, Vesa P</creatorcontrib><creatorcontrib>Scozzafava, Andrea</creatorcontrib><creatorcontrib>Parkkila, Seppo</creatorcontrib><creatorcontrib>Supuran, Claudiu T</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Durdagi, Serdar</au><au>Vullo, Daniela</au><au>Pan, Peiwen</au><au>Kähkönen, Niklas</au><au>Määttä, Juha A</au><au>Hytönen, Vesa P</au><au>Scozzafava, Andrea</au><au>Parkkila, Seppo</au><au>Supuran, Claudiu T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein–Protein Interactions: Inhibition of Mammalian Carbonic Anhydrases I–XV by the Murine Inhibitor of Carbonic Anhydrase and Other Members of the Transferrin Family</atitle><jtitle>Journal of medicinal chemistry</jtitle><addtitle>J. Med. Chem</addtitle><date>2012-06-14</date><risdate>2012</risdate><volume>55</volume><issue>11</issue><spage>5529</spage><epage>5535</epage><pages>5529-5535</pages><issn>0022-2623</issn><eissn>1520-4804</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>The murine inhibitor of carbonic anhydrase (mICA), a member of the transferrin (TF) superfamily of proteins, together with human holo- and apoTF and lactoferrin (LF) were assessed as inhibitors of all catalytically active mammalian (h = human, m = murine) CA isoforms, from CA I to CA XV. mICA was a low nanomolar to subnanomolar inhibitor of hCAs I, II, III, VA, VB, VII and mCAs XV (K I of 0.7–44.0 nM) and inhibited the remaining isoforms with K I of 185.5–469 nM. hTF, apoTF, and hLF were inhibitors of most of these CAs but with reduced efficiency compared to mICA (K I of 18.9–453.8 nM). Biacore surface plasmon resonance and differential scanning calorimetry experiments were also used for obtaining more insights into the interaction between these proteins, which may be useful for drug design of protein-based CA inhibitors.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>22578027</pmid><doi>10.1021/jm3004587</doi><tpages>7</tpages></addata></record>
fulltext	fulltext
identifier	ISSN: 0022-2623
ispartof	Journal of medicinal chemistry, 2012-06, Vol.55 (11), p.5529-5535
issn	0022-2623 1520-4804
language	eng
recordid	cdi_proquest_miscellaneous_1020832469
source	American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)
subjects	Animals Apoproteins - metabolism Biological Assay Biosensing Techniques Calorimetry, Differential Scanning Carbonic Anhydrases - metabolism Humans Isoenzymes - antagonists & inhibitors Isoenzymes - metabolism Mice Protein Binding Protein Denaturation Protein Interaction Mapping Transferrins - metabolism
title	Protein–Protein Interactions: Inhibition of Mammalian Carbonic Anhydrases I–XV by the Murine Inhibitor of Carbonic Anhydrase and Other Members of the Transferrin Family
url	http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-09-23T05%3A30%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Protein%E2%80%93Protein%20Interactions:%20Inhibition%20of%20Mammalian%20Carbonic%20Anhydrases%20I%E2%80%93XV%20by%20the%20Murine%20Inhibitor%20of%20Carbonic%20Anhydrase%20and%20Other%20Members%20of%20the%20Transferrin%20Family&rft.jtitle=Journal%20of%20medicinal%20chemistry&rft.au=Durdagi,%20Serdar&rft.date=2012-06-14&rft.volume=55&rft.issue=11&rft.spage=5529&rft.epage=5535&rft.pages=5529-5535&rft.issn=0022-2623&rft.eissn=1520-4804&rft_id=info:doi/10.1021/jm3004587&rft_dat=%3Cproquest_cross%3E1020832469%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a315t-7caf1a2fa4f6255fd1df2d575975b11c0341bbdb7e7b00fd1d8dd7279b1f24b23%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1020832469&rft_id=info:pmid/22578027&rfr_iscdi=true