Purinergic regulation of anion secretion by cystic fibrosis pancreatic duct cells
H. C. Chan, W. T. Cheung, P. Y. Leung, L. J. Wu, S. B. Chew, W. H. Ko and P. Y. Wong Department of Physiology, Faculty of Medicine, Chinese University of Hong Kong, Shatin, Hong Kong. The present study explored regulation of anion secretion across cystic fibrosis pancreatic ductal epithelium by extr...
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| Veröffentlicht in: | American Journal of Physiology: Cell Physiology 1996-08, Vol.271 (2), p.C469-C477 |
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| container_title | American Journal of Physiology: Cell Physiology |
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| creator | Chan, H. C Cheung, W. T Leung, P. Y Wu, L. J Chew, S. B Ko, W. H Wong, P. Y |
| description | H. C. Chan, W. T. Cheung, P. Y. Leung, L. J. Wu, S. B. Chew, W. H. Ko and P. Y. Wong
Department of Physiology, Faculty of Medicine, Chinese University of Hong Kong, Shatin, Hong Kong.
The present study explored regulation of anion secretion across cystic
fibrosis pancreatic ductal epithelium by extracellular ATP with the
short-circuit current (Isc) technique. CFPAC-1 cells grown on Millipore
filters formed polarized monolayers with junctional complexes as revealed
by light and electron microscopy. The cultured monolayers exhibited an
increase in Isc in response to apical application of ATP in a
concentration-dependent manner (concentration eliciting 50% of maximal
response = 3 microM). Replacement of Cl- in the bathing solution or
treatment of the cells with a Cl- channel blocker,
4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS), markedly reduced
Isc, indicating that a substantial portion of ATP-activated Isc was Cl-
dependent. The effects of different adenosine nucleosides and/or
nucleotides on Isc were also studied to identify the type of purinoceptors
involved. The order of potency, ATP = UTP > ADP > adenosine, was
consistent with that for P2 purinoceptors. Reactive blue 2 (100 microM), a
P2 antagonist, was found to inhibit 86% of ATP-induced Isc. ATP-induced Isc
was also inhibited by pretreatment of the cells with a Ca2+ chelator,
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid acetoxymethyl
ester (50 microM). Confocal microscopic study also demonstrated a rise in
intracellular Ca2+ with stimulation by extracellular ATP, indicating a role
of intracellular Ca2+ in mediating the ATP response. ATP-induced Isc was
observed in monolayers whose basolateral membranes had been permeabilized
by nystatin, which was also sensitive to apical addition of DIDS,
suggesting that Isc was mediated by apical Cl- channels. The results of the
present study demonstrate the presence of a purinergic regulatory mechanism
involving P2U receptor and Ca2+ mobilization in pancreatic duct anion
secretion. |
| doi_str_mv | 10.1152/ajpcell.1996.271.2.c469 |
| format | Article |
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Department of Physiology, Faculty of Medicine, Chinese University of Hong Kong, Shatin, Hong Kong.
The present study explored regulation of anion secretion across cystic
fibrosis pancreatic ductal epithelium by extracellular ATP with the
short-circuit current (Isc) technique. CFPAC-1 cells grown on Millipore
filters formed polarized monolayers with junctional complexes as revealed
by light and electron microscopy. The cultured monolayers exhibited an
increase in Isc in response to apical application of ATP in a
concentration-dependent manner (concentration eliciting 50% of maximal
response = 3 microM). Replacement of Cl- in the bathing solution or
treatment of the cells with a Cl- channel blocker,
4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS), markedly reduced
Isc, indicating that a substantial portion of ATP-activated Isc was Cl-
dependent. The effects of different adenosine nucleosides and/or
nucleotides on Isc were also studied to identify the type of purinoceptors
involved. The order of potency, ATP = UTP > ADP > adenosine, was
consistent with that for P2 purinoceptors. Reactive blue 2 (100 microM), a
P2 antagonist, was found to inhibit 86% of ATP-induced Isc. ATP-induced Isc
was also inhibited by pretreatment of the cells with a Ca2+ chelator,
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid acetoxymethyl
ester (50 microM). Confocal microscopic study also demonstrated a rise in
intracellular Ca2+ with stimulation by extracellular ATP, indicating a role
of intracellular Ca2+ in mediating the ATP response. ATP-induced Isc was
observed in monolayers whose basolateral membranes had been permeabilized
by nystatin, which was also sensitive to apical addition of DIDS,
suggesting that Isc was mediated by apical Cl- channels. The results of the
present study demonstrate the presence of a purinergic regulatory mechanism
involving P2U receptor and Ca2+ mobilization in pancreatic duct anion
secretion.</description><identifier>ISSN: 0363-6143</identifier><identifier>ISSN: 0002-9513</identifier><identifier>EISSN: 1522-1563</identifier><identifier>DOI: 10.1152/ajpcell.1996.271.2.c469</identifier><identifier>PMID: 8769985</identifier><language>eng</language><publisher>United States</publisher><subject>Adenosine Triphosphate - pharmacology ; Anions - metabolism ; Calcium - physiology ; Cell Line ; Cell Membrane - metabolism ; Cell Polarity ; Chloride Channels - physiology ; Cystic Fibrosis - metabolism ; Electric Conductivity ; Pancreatic Ducts - cytology ; Pancreatic Ducts - metabolism ; Pancreatic Ducts - physiology ; Purines - metabolism ; Receptors, Purinergic - physiology</subject><ispartof>American Journal of Physiology: Cell Physiology, 1996-08, Vol.271 (2), p.C469-C477</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c346t-2c84e1235d080a1d3bbbaf02459cbc9bea0254d4849562184547dba16616587c3</citedby><cites>FETCH-LOGICAL-c346t-2c84e1235d080a1d3bbbaf02459cbc9bea0254d4849562184547dba16616587c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8769985$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chan, H. C</creatorcontrib><creatorcontrib>Cheung, W. T</creatorcontrib><creatorcontrib>Leung, P. Y</creatorcontrib><creatorcontrib>Wu, L. J</creatorcontrib><creatorcontrib>Chew, S. B</creatorcontrib><creatorcontrib>Ko, W. H</creatorcontrib><creatorcontrib>Wong, P. Y</creatorcontrib><title>Purinergic regulation of anion secretion by cystic fibrosis pancreatic duct cells</title><title>American Journal of Physiology: Cell Physiology</title><addtitle>Am J Physiol</addtitle><description>H. C. Chan, W. T. Cheung, P. Y. Leung, L. J. Wu, S. B. Chew, W. H. Ko and P. Y. Wong
Department of Physiology, Faculty of Medicine, Chinese University of Hong Kong, Shatin, Hong Kong.
The present study explored regulation of anion secretion across cystic
fibrosis pancreatic ductal epithelium by extracellular ATP with the
short-circuit current (Isc) technique. CFPAC-1 cells grown on Millipore
filters formed polarized monolayers with junctional complexes as revealed
by light and electron microscopy. The cultured monolayers exhibited an
increase in Isc in response to apical application of ATP in a
concentration-dependent manner (concentration eliciting 50% of maximal
response = 3 microM). Replacement of Cl- in the bathing solution or
treatment of the cells with a Cl- channel blocker,
4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS), markedly reduced
Isc, indicating that a substantial portion of ATP-activated Isc was Cl-
dependent. The effects of different adenosine nucleosides and/or
nucleotides on Isc were also studied to identify the type of purinoceptors
involved. The order of potency, ATP = UTP > ADP > adenosine, was
consistent with that for P2 purinoceptors. Reactive blue 2 (100 microM), a
P2 antagonist, was found to inhibit 86% of ATP-induced Isc. ATP-induced Isc
was also inhibited by pretreatment of the cells with a Ca2+ chelator,
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid acetoxymethyl
ester (50 microM). Confocal microscopic study also demonstrated a rise in
intracellular Ca2+ with stimulation by extracellular ATP, indicating a role
of intracellular Ca2+ in mediating the ATP response. ATP-induced Isc was
observed in monolayers whose basolateral membranes had been permeabilized
by nystatin, which was also sensitive to apical addition of DIDS,
suggesting that Isc was mediated by apical Cl- channels. The results of the
present study demonstrate the presence of a purinergic regulatory mechanism
involving P2U receptor and Ca2+ mobilization in pancreatic duct anion
secretion.</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Anions - metabolism</subject><subject>Calcium - physiology</subject><subject>Cell Line</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Polarity</subject><subject>Chloride Channels - physiology</subject><subject>Cystic Fibrosis - metabolism</subject><subject>Electric Conductivity</subject><subject>Pancreatic Ducts - cytology</subject><subject>Pancreatic Ducts - metabolism</subject><subject>Pancreatic Ducts - physiology</subject><subject>Purines - metabolism</subject><subject>Receptors, Purinergic - physiology</subject><issn>0363-6143</issn><issn>0002-9513</issn><issn>1522-1563</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkEtLxDAUhYMo4zj6E8Su3LUmaR7NUgZfIKig65CkaSdDp61Ji_TfmzrD4CrhnnPPPXwA3CCYIUTxndr2xjZNhoRgGeYow5khTJyAZVRxiijLT8ES5ixPGSL5ObgIYQshJJiJBVgUnAlR0CX4eB-9a62vnUm8rcdGDa5rk65KVDt_gjXe_o30lJgpDNFXOe274ELSqzaqap6VoxmSuVG4BGeVaoK9Orwr8PX48Ll-Tl_fnl7W96-pyQkbUmwKYhHOaQkLqFCZa61VBTGhwmgjtFUQU1KSggjKMCoIJbzUCjGGGC24yVfgdp_b--57tGGQOxfmBqq13RgkLzCnUPBo5Hujia2Dt5XsvdspP0kE5QxTHmDKGaaMMCWW6wgzbl4fTox6Z8vj3oFe1NO9vnH15sd5K_vNFFzXdPV0DP2X9wuYn4Nm</recordid><startdate>19960801</startdate><enddate>19960801</enddate><creator>Chan, H. C</creator><creator>Cheung, W. T</creator><creator>Leung, P. Y</creator><creator>Wu, L. J</creator><creator>Chew, S. B</creator><creator>Ko, W. H</creator><creator>Wong, P. Y</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><scope>7X8</scope></search><sort><creationdate>19960801</creationdate><title>Purinergic regulation of anion secretion by cystic fibrosis pancreatic duct cells</title><author>Chan, H. C ; Cheung, W. T ; Leung, P. Y ; Wu, L. J ; Chew, S. B ; Ko, W. H ; Wong, P. Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c346t-2c84e1235d080a1d3bbbaf02459cbc9bea0254d4849562184547dba16616587c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Anions - metabolism</topic><topic>Calcium - physiology</topic><topic>Cell Line</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Polarity</topic><topic>Chloride Channels - physiology</topic><topic>Cystic Fibrosis - metabolism</topic><topic>Electric Conductivity</topic><topic>Pancreatic Ducts - cytology</topic><topic>Pancreatic Ducts - metabolism</topic><topic>Pancreatic Ducts - physiology</topic><topic>Purines - metabolism</topic><topic>Receptors, Purinergic - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chan, H. C</creatorcontrib><creatorcontrib>Cheung, W. T</creatorcontrib><creatorcontrib>Leung, P. Y</creatorcontrib><creatorcontrib>Wu, L. J</creatorcontrib><creatorcontrib>Chew, S. B</creatorcontrib><creatorcontrib>Ko, W. H</creatorcontrib><creatorcontrib>Wong, P. Y</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>American Journal of Physiology: Cell Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chan, H. C</au><au>Cheung, W. T</au><au>Leung, P. Y</au><au>Wu, L. J</au><au>Chew, S. B</au><au>Ko, W. H</au><au>Wong, P. Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purinergic regulation of anion secretion by cystic fibrosis pancreatic duct cells</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><addtitle>Am J Physiol</addtitle><date>1996-08-01</date><risdate>1996</risdate><volume>271</volume><issue>2</issue><spage>C469</spage><epage>C477</epage><pages>C469-C477</pages><issn>0363-6143</issn><issn>0002-9513</issn><eissn>1522-1563</eissn><abstract>H. C. Chan, W. T. Cheung, P. Y. Leung, L. J. Wu, S. B. Chew, W. H. Ko and P. Y. Wong
Department of Physiology, Faculty of Medicine, Chinese University of Hong Kong, Shatin, Hong Kong.
The present study explored regulation of anion secretion across cystic
fibrosis pancreatic ductal epithelium by extracellular ATP with the
short-circuit current (Isc) technique. CFPAC-1 cells grown on Millipore
filters formed polarized monolayers with junctional complexes as revealed
by light and electron microscopy. The cultured monolayers exhibited an
increase in Isc in response to apical application of ATP in a
concentration-dependent manner (concentration eliciting 50% of maximal
response = 3 microM). Replacement of Cl- in the bathing solution or
treatment of the cells with a Cl- channel blocker,
4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS), markedly reduced
Isc, indicating that a substantial portion of ATP-activated Isc was Cl-
dependent. The effects of different adenosine nucleosides and/or
nucleotides on Isc were also studied to identify the type of purinoceptors
involved. The order of potency, ATP = UTP > ADP > adenosine, was
consistent with that for P2 purinoceptors. Reactive blue 2 (100 microM), a
P2 antagonist, was found to inhibit 86% of ATP-induced Isc. ATP-induced Isc
was also inhibited by pretreatment of the cells with a Ca2+ chelator,
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid acetoxymethyl
ester (50 microM). Confocal microscopic study also demonstrated a rise in
intracellular Ca2+ with stimulation by extracellular ATP, indicating a role
of intracellular Ca2+ in mediating the ATP response. ATP-induced Isc was
observed in monolayers whose basolateral membranes had been permeabilized
by nystatin, which was also sensitive to apical addition of DIDS,
suggesting that Isc was mediated by apical Cl- channels. The results of the
present study demonstrate the presence of a purinergic regulatory mechanism
involving P2U receptor and Ca2+ mobilization in pancreatic duct anion
secretion.</abstract><cop>United States</cop><pmid>8769985</pmid><doi>10.1152/ajpcell.1996.271.2.c469</doi></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0363-6143 |
| ispartof | American Journal of Physiology: Cell Physiology, 1996-08, Vol.271 (2), p.C469-C477 |
| issn | 0363-6143 0002-9513 1522-1563 |
| language | eng |
| recordid | cdi_highwire_physiology_ajpcell_271_2_C469 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - pharmacology Anions - metabolism Calcium - physiology Cell Line Cell Membrane - metabolism Cell Polarity Chloride Channels - physiology Cystic Fibrosis - metabolism Electric Conductivity Pancreatic Ducts - cytology Pancreatic Ducts - metabolism Pancreatic Ducts - physiology Purines - metabolism Receptors, Purinergic - physiology |
| title | Purinergic regulation of anion secretion by cystic fibrosis pancreatic duct cells |
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