Stimulation of Canine Kidney BBMV ATPase Activity by Acidic pH in the Presence of Zn2+: An ATPase Activity Distinct from Transport ATPases and Alkaline Phosphatase That May Be an Ecto-ATPase
Renal brush border membrane vesicles (BBMV) of the dog possess at least two ATPase activities. In the present study, we have examined the effect of pH, ions, and inhibitors on the activity of ATPase in BBMV. Two different sets of conditions were identified that produced stimulation of ATPase activit...
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| Veröffentlicht in: | Membrane biochemistry 1990, Vol.9 (1), p.69-81 |
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| creator | Hilden, Shirley A. Madias, Nicolaos E. |
| description | Renal brush border membrane vesicles (BBMV) of the dog possess at least two ATPase activities. In the present study, we have examined the effect of pH, ions, and inhibitors on the activity of ATPase in BBMV. Two different sets of conditions were identified that produced stimulation of ATPase activity. A unique stimulation of BBMV ATPase activity occurred at acidic pH in the presence of 1 mM ZnCl2. In the absence of Zn2+, a second ATPase activity was stimulated by alkaline pH values with peak stimulation occurring between pH 8.5 and 9.0. The results suggest that the alkaline pH-stimulated hydrolysis of ATP probably represents the activity of BBMV alkaline phosphatase. The unique acidic pH + Zn2+-stimulated ATPase activity must represent the activity of a second protein other than the alkaline phosphatase, since purified alkaline phosphatase did not show this activity. The biochemical identity and physiological function of this renal BBMV ATPase activity remain to be determined, but it may be an ecto-ATPase |
| doi_str_mv | 10.3109/09687689009026824 |
| format | Article |
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In the present study, we have examined the effect of pH, ions, and inhibitors on the activity of ATPase in BBMV. Two different sets of conditions were identified that produced stimulation of ATPase activity. A unique stimulation of BBMV ATPase activity occurred at acidic pH in the presence of 1 mM ZnCl2. In the absence of Zn2+, a second ATPase activity was stimulated by alkaline pH values with peak stimulation occurring between pH 8.5 and 9.0. The results suggest that the alkaline pH-stimulated hydrolysis of ATP probably represents the activity of BBMV alkaline phosphatase. The unique acidic pH + Zn2+-stimulated ATPase activity must represent the activity of a second protein other than the alkaline phosphatase, since purified alkaline phosphatase did not show this activity. The biochemical identity and physiological function of this renal BBMV ATPase activity remain to be determined, but it may be an ecto-ATPase</description><identifier>ISSN: 0968-7688</identifier><identifier>ISSN: 0149-046X</identifier><identifier>EISSN: 1464-5203</identifier><identifier>DOI: 10.3109/09687689009026824</identifier><identifier>PMID: 2150216</identifier><language>eng</language><publisher>United States: Informa UK Ltd</publisher><subject>Adenosine Triphosphatases - antagonists & inhibitors ; Adenosine Triphosphatases - metabolism ; Alkaline Phosphatase - metabolism ; Animals ; ATPase ; Biological Transport ; brush border membrane vesicles ; Dogs ; ecto-ATPase ; Enzyme Activation ; Hydrogen-Ion Concentration ; Kidney - enzymology ; Kidney - ultrastructure ; Microvilli - enzymology ; Substrate Specificity ; Type C Phospholipases - metabolism ; Zinc ; Zinc - pharmacology</subject><ispartof>Membrane biochemistry, 1990, Vol.9 (1), p.69-81</ispartof><rights>1990 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 1990</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.3109/09687689009026824$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.3109/09687689009026824$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>314,776,780,4010,27900,27901,27902,59620,60409,61194,61375</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2150216$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hilden, Shirley A.</creatorcontrib><creatorcontrib>Madias, Nicolaos E.</creatorcontrib><title>Stimulation of Canine Kidney BBMV ATPase Activity by Acidic pH in the Presence of Zn2+: An ATPase Activity Distinct from Transport ATPases and Alkaline Phosphatase That May Be an Ecto-ATPase</title><title>Membrane biochemistry</title><addtitle>Membr Biochem</addtitle><description>Renal brush border membrane vesicles (BBMV) of the dog possess at least two ATPase activities. In the present study, we have examined the effect of pH, ions, and inhibitors on the activity of ATPase in BBMV. Two different sets of conditions were identified that produced stimulation of ATPase activity. A unique stimulation of BBMV ATPase activity occurred at acidic pH in the presence of 1 mM ZnCl2. In the absence of Zn2+, a second ATPase activity was stimulated by alkaline pH values with peak stimulation occurring between pH 8.5 and 9.0. The results suggest that the alkaline pH-stimulated hydrolysis of ATP probably represents the activity of BBMV alkaline phosphatase. The unique acidic pH + Zn2+-stimulated ATPase activity must represent the activity of a second protein other than the alkaline phosphatase, since purified alkaline phosphatase did not show this activity. The biochemical identity and physiological function of this renal BBMV ATPase activity remain to be determined, but it may be an ecto-ATPase</description><subject>Adenosine Triphosphatases - antagonists & inhibitors</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Alkaline Phosphatase - metabolism</subject><subject>Animals</subject><subject>ATPase</subject><subject>Biological Transport</subject><subject>brush border membrane vesicles</subject><subject>Dogs</subject><subject>ecto-ATPase</subject><subject>Enzyme Activation</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kidney - enzymology</subject><subject>Kidney - ultrastructure</subject><subject>Microvilli - enzymology</subject><subject>Substrate Specificity</subject><subject>Type C Phospholipases - metabolism</subject><subject>Zinc</subject><subject>Zinc - pharmacology</subject><issn>0968-7688</issn><issn>0149-046X</issn><issn>1464-5203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUFv1DAQhSMEKkvhB3BA8okLCjheO3GAS7oUimjFSiwcuEQTZ6K4JHawHVD-HL8NR7sXVHGwxtL73tPoTZI8zejLbUbLV7TMZZHLktKSslwyfi_ZZDznqWB0ez_ZrHoaAfkweeT9LaWU5zk_S85YJijL8k3y50vQ4zxA0NYQ25EdGG2QfNKtwYVcXNx8I9VhDx5JpYL-pcNCmiX-dasVma6INiT0SPYOPRqFa8R3w168JpW5Y3ynfdBGBdI5O5KDA-Mn68KJ8wRMS6rhBwzrBvve-qmHsCYc4iQ3EPfBCJFLFWx6ND1OHnQweHxymufJ1_eXh91Vev35w8dddZ3qTMg83RZNkRVMUi55DgVDEJ1A5JxT7FQmAFqUnDalyEDGMoWQhWKNYKXoACHbnifPj7mTsz9n9KEetVc4DGDQzr6WlJUFoyyCz07g3IzY1pPTI7ilPhUe9bdHXZvOuhF-Wze0dYBlsK6LjSjt63ja9ZX1nfNG-5t_7D3CEHoFDutbOzsTO6j_7_4LtLCndA</recordid><startdate>1990</startdate><enddate>1990</enddate><creator>Hilden, Shirley A.</creator><creator>Madias, Nicolaos E.</creator><general>Informa UK Ltd</general><general>Taylor & Francis</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>1990</creationdate><title>Stimulation of Canine Kidney BBMV ATPase Activity by Acidic pH in the Presence of Zn2+: An ATPase Activity Distinct from Transport ATPases and Alkaline Phosphatase That May Be an Ecto-ATPase</title><author>Hilden, Shirley A. ; Madias, Nicolaos E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i1586-37b7172804846a72ea5f5ee4440efc15aade840b951a80095587c2b5295faea13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Adenosine Triphosphatases - antagonists & inhibitors</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Alkaline Phosphatase - metabolism</topic><topic>Animals</topic><topic>ATPase</topic><topic>Biological Transport</topic><topic>brush border membrane vesicles</topic><topic>Dogs</topic><topic>ecto-ATPase</topic><topic>Enzyme Activation</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kidney - enzymology</topic><topic>Kidney - ultrastructure</topic><topic>Microvilli - enzymology</topic><topic>Substrate Specificity</topic><topic>Type C Phospholipases - metabolism</topic><topic>Zinc</topic><topic>Zinc - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hilden, Shirley A.</creatorcontrib><creatorcontrib>Madias, Nicolaos E.</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>Membrane biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hilden, Shirley A.</au><au>Madias, Nicolaos E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stimulation of Canine Kidney BBMV ATPase Activity by Acidic pH in the Presence of Zn2+: An ATPase Activity Distinct from Transport ATPases and Alkaline Phosphatase That May Be an Ecto-ATPase</atitle><jtitle>Membrane biochemistry</jtitle><addtitle>Membr Biochem</addtitle><date>1990</date><risdate>1990</risdate><volume>9</volume><issue>1</issue><spage>69</spage><epage>81</epage><pages>69-81</pages><issn>0968-7688</issn><issn>0149-046X</issn><eissn>1464-5203</eissn><abstract>Renal brush border membrane vesicles (BBMV) of the dog possess at least two ATPase activities. In the present study, we have examined the effect of pH, ions, and inhibitors on the activity of ATPase in BBMV. Two different sets of conditions were identified that produced stimulation of ATPase activity. A unique stimulation of BBMV ATPase activity occurred at acidic pH in the presence of 1 mM ZnCl2. In the absence of Zn2+, a second ATPase activity was stimulated by alkaline pH values with peak stimulation occurring between pH 8.5 and 9.0. The results suggest that the alkaline pH-stimulated hydrolysis of ATP probably represents the activity of BBMV alkaline phosphatase. The unique acidic pH + Zn2+-stimulated ATPase activity must represent the activity of a second protein other than the alkaline phosphatase, since purified alkaline phosphatase did not show this activity. The biochemical identity and physiological function of this renal BBMV ATPase activity remain to be determined, but it may be an ecto-ATPase</abstract><cop>United States</cop><pub>Informa UK Ltd</pub><pmid>2150216</pmid><doi>10.3109/09687689009026824</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0968-7688 |
| ispartof | Membrane biochemistry, 1990, Vol.9 (1), p.69-81 |
| issn | 0968-7688 0149-046X 1464-5203 |
| language | eng |
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| source | Taylor & Francis:Master (3349 titles); MEDLINE |
| subjects | Adenosine Triphosphatases - antagonists & inhibitors Adenosine Triphosphatases - metabolism Alkaline Phosphatase - metabolism Animals ATPase Biological Transport brush border membrane vesicles Dogs ecto-ATPase Enzyme Activation Hydrogen-Ion Concentration Kidney - enzymology Kidney - ultrastructure Microvilli - enzymology Substrate Specificity Type C Phospholipases - metabolism Zinc Zinc - pharmacology |
| title | Stimulation of Canine Kidney BBMV ATPase Activity by Acidic pH in the Presence of Zn2+: An ATPase Activity Distinct from Transport ATPases and Alkaline Phosphatase That May Be an Ecto-ATPase |
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