Volume expansion-induced changes in renal tubular membrane protein phosphorylation
The influence of volume expansion (VE) on the in vitro phosphorylation of membrane protein in the proximal brush border membrane (BBM) of the thyroparathyroidectomized (TPTX) rat was studied in the presence and absence of cyclic AMP and the results were compared to those obtained in control TPTX and...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1987-02, Vol.143 (1), p.74-80 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Chen, Tai C. Humpierres, Jeannette Hanna, Dean Perregaux, Susan B. Puschett, Jules B. |
| description | The influence of volume expansion (VE) on the in vitro phosphorylation of membrane protein in the proximal brush border membrane (BBM) of the thyroparathyroidectomized (TPTX) rat was studied in the presence and absence of cyclic AMP and the results were compared to those obtained in control TPTX and intact animals.
The results indicate that the cyclic AMP-independent phosphorylation of a protein band (Mr = 72,000) was stimulated both by VE and by the presence of parathyroid hormone in the circulation, whereas the cyclic AMP-dependent phosphorylation of membrane proteins (Mr = 40,000, 52,000 and 87,000) was inhibited by the same maneuvers. These findings, taken together with data previously available, which demonstrate inhibition of BBM phosphate transport following VE, may provide a link between alterations in phosphate transport in renal BBM vesicles and the phosphorylation of membrane proteins. The results further suggest that membrane protein phosphorylation may be a common mechanism by which a number of agents and maneuvers induce an inhibition of renal tubular phosphate transport. |
| doi_str_mv | 10.1016/0006-291X(87)90631-0 |
| format | Article |
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The results indicate that the cyclic AMP-independent phosphorylation of a protein band (Mr = 72,000) was stimulated both by VE and by the presence of parathyroid hormone in the circulation, whereas the cyclic AMP-dependent phosphorylation of membrane proteins (Mr = 40,000, 52,000 and 87,000) was inhibited by the same maneuvers. These findings, taken together with data previously available, which demonstrate inhibition of BBM phosphate transport following VE, may provide a link between alterations in phosphate transport in renal BBM vesicles and the phosphorylation of membrane proteins. The results further suggest that membrane protein phosphorylation may be a common mechanism by which a number of agents and maneuvers induce an inhibition of renal tubular phosphate transport.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(87)90631-0</identifier><identifier>PMID: 3827931</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Animals ; Applied sciences ; Exact sciences and technology ; Female ; kidney ; Kidney Cortex - metabolism ; Kidney Tubules - metabolism ; membrane proteins ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Microvilli - metabolism ; Molecular Weight ; Other techniques and industries ; Parathyroid Glands - physiology ; Phosphorylation ; Protein Kinases - metabolism ; Rats ; Rats, Inbred Strains ; Thyroidectomy ; tubules</subject><ispartof>Biochemical and biophysical research communications, 1987-02, Vol.143 (1), p.74-80</ispartof><rights>1987</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-750e3c8349c6bcb7a9030df03eec988cf34c630e6ecbd5c3a4d0c39211a637d43</citedby><cites>FETCH-LOGICAL-c417t-750e3c8349c6bcb7a9030df03eec988cf34c630e6ecbd5c3a4d0c39211a637d43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(87)90631-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7530350$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3827931$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Tai C.</creatorcontrib><creatorcontrib>Humpierres, Jeannette</creatorcontrib><creatorcontrib>Hanna, Dean</creatorcontrib><creatorcontrib>Perregaux, Susan B.</creatorcontrib><creatorcontrib>Puschett, Jules B.</creatorcontrib><title>Volume expansion-induced changes in renal tubular membrane protein phosphorylation</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The influence of volume expansion (VE) on the in vitro phosphorylation of membrane protein in the proximal brush border membrane (BBM) of the thyroparathyroidectomized (TPTX) rat was studied in the presence and absence of cyclic AMP and the results were compared to those obtained in control TPTX and intact animals.
The results indicate that the cyclic AMP-independent phosphorylation of a protein band (Mr = 72,000) was stimulated both by VE and by the presence of parathyroid hormone in the circulation, whereas the cyclic AMP-dependent phosphorylation of membrane proteins (Mr = 40,000, 52,000 and 87,000) was inhibited by the same maneuvers. These findings, taken together with data previously available, which demonstrate inhibition of BBM phosphate transport following VE, may provide a link between alterations in phosphate transport in renal BBM vesicles and the phosphorylation of membrane proteins. The results further suggest that membrane protein phosphorylation may be a common mechanism by which a number of agents and maneuvers induce an inhibition of renal tubular phosphate transport.</description><subject>Animals</subject><subject>Applied sciences</subject><subject>Exact sciences and technology</subject><subject>Female</subject><subject>kidney</subject><subject>Kidney Cortex - metabolism</subject><subject>Kidney Tubules - metabolism</subject><subject>membrane proteins</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Microvilli - metabolism</subject><subject>Molecular Weight</subject><subject>Other techniques and industries</subject><subject>Parathyroid Glands - physiology</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Thyroidectomy</subject><subject>tubules</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9LHTEUxUNR9PnsN6gwCym6GL2Z5CWTjVCkrYIgiC3dhcydOzVl_rwmM1K_vZm-x1vqImRxzj059xfGPnG44MDVJQCovDD811mpzw0owXP4wBYcDOQFB7nHFjvLITuK8Q8A51KZA3YgykIbwRfs4efQTh1l9G_t-uiHPvd9PSHVGT65_jfFzPdZoN612ThVU-tC1lFXBddTtg7DSElePw0xnfDSujElHLP9xrWRPm7vJfvx7evj9U1-d__99vrLXY6S6zHXKyCBpZAGVYWVdgYE1A0IIjRliY2QqASQIqzqFQona0BhCs6dErqWYsk-b3JTj78TxdF2PiK1beo2TNFqLQuVVn7XyKUuuEzPL5ncGDEMMQZq7Dr4zoUXy8HOzO0M1M5Abantf-Z2HjvZ5k9VR_VuaAs56adb3UV0bZPgoY87m14JEKs55mpjowTt2VOwET316S98IBxtPfi3e7wCqOueZQ</recordid><startdate>19870227</startdate><enddate>19870227</enddate><creator>Chen, Tai C.</creator><creator>Humpierres, Jeannette</creator><creator>Hanna, Dean</creator><creator>Perregaux, Susan B.</creator><creator>Puschett, Jules B.</creator><general>Elsevier Inc</general><general>Elsevier</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19870227</creationdate><title>Volume expansion-induced changes in renal tubular membrane protein phosphorylation</title><author>Chen, Tai C. ; Humpierres, Jeannette ; Hanna, Dean ; Perregaux, Susan B. ; Puschett, Jules B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-750e3c8349c6bcb7a9030df03eec988cf34c630e6ecbd5c3a4d0c39211a637d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Animals</topic><topic>Applied sciences</topic><topic>Exact sciences and technology</topic><topic>Female</topic><topic>kidney</topic><topic>Kidney Cortex - metabolism</topic><topic>Kidney Tubules - metabolism</topic><topic>membrane proteins</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Microvilli - metabolism</topic><topic>Molecular Weight</topic><topic>Other techniques and industries</topic><topic>Parathyroid Glands - physiology</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Thyroidectomy</topic><topic>tubules</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Tai C.</creatorcontrib><creatorcontrib>Humpierres, Jeannette</creatorcontrib><creatorcontrib>Hanna, Dean</creatorcontrib><creatorcontrib>Perregaux, Susan B.</creatorcontrib><creatorcontrib>Puschett, Jules B.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Tai C.</au><au>Humpierres, Jeannette</au><au>Hanna, Dean</au><au>Perregaux, Susan B.</au><au>Puschett, Jules B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Volume expansion-induced changes in renal tubular membrane protein phosphorylation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1987-02-27</date><risdate>1987</risdate><volume>143</volume><issue>1</issue><spage>74</spage><epage>80</epage><pages>74-80</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The influence of volume expansion (VE) on the in vitro phosphorylation of membrane protein in the proximal brush border membrane (BBM) of the thyroparathyroidectomized (TPTX) rat was studied in the presence and absence of cyclic AMP and the results were compared to those obtained in control TPTX and intact animals.
The results indicate that the cyclic AMP-independent phosphorylation of a protein band (Mr = 72,000) was stimulated both by VE and by the presence of parathyroid hormone in the circulation, whereas the cyclic AMP-dependent phosphorylation of membrane proteins (Mr = 40,000, 52,000 and 87,000) was inhibited by the same maneuvers. These findings, taken together with data previously available, which demonstrate inhibition of BBM phosphate transport following VE, may provide a link between alterations in phosphate transport in renal BBM vesicles and the phosphorylation of membrane proteins. The results further suggest that membrane protein phosphorylation may be a common mechanism by which a number of agents and maneuvers induce an inhibition of renal tubular phosphate transport.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3827931</pmid><doi>10.1016/0006-291X(87)90631-0</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1987-02, Vol.143 (1), p.74-80 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Applied sciences Exact sciences and technology Female kidney Kidney Cortex - metabolism Kidney Tubules - metabolism membrane proteins Membrane Proteins - isolation & purification Membrane Proteins - metabolism Microvilli - metabolism Molecular Weight Other techniques and industries Parathyroid Glands - physiology Phosphorylation Protein Kinases - metabolism Rats Rats, Inbred Strains Thyroidectomy tubules |
| title | Volume expansion-induced changes in renal tubular membrane protein phosphorylation |
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