Studies on the turnover of protein and glycoprotein components in rabbit kidney brush borders
The kinetics of incorporation of [(3)H]lysine and [(14)C]glucosamine into kidney brush borders were studied in vivo. The patterns of incorporation and loss of radioactivity from the brush borders were similar for both radioactively labelled precursors. Maximal labelling occurred 15-20h after injecti...
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Veröffentlicht in: | Biochemical journal 1973-03, Vol.132 (3), p.501-508 |
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description | The kinetics of incorporation of [(3)H]lysine and [(14)C]glucosamine into kidney brush borders were studied in vivo. The patterns of incorporation and loss of radioactivity from the brush borders were similar for both radioactively labelled precursors. Maximal labelling occurred 15-20h after injection of the precursors, and then the radioactivity declined rapidly until 50h. The radioactivity of brush borders then remained constant until 120h and thereafter declined slowly. These results are interpreted as indicating that two processes contribute to the turnover of brush-border components, pinocytosis and a slower turnover of the components of the microvilli. Studies of the distribution of radioactivity among glycoprotein components of the brush borders, separated by polyacrylamide-gel electrophoresis, indicated that the membrane components turned over in unison. |
doi_str_mv | 10.1042/bj1320501 |
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The patterns of incorporation and loss of radioactivity from the brush borders were similar for both radioactively labelled precursors. Maximal labelling occurred 15-20h after injection of the precursors, and then the radioactivity declined rapidly until 50h. The radioactivity of brush borders then remained constant until 120h and thereafter declined slowly. These results are interpreted as indicating that two processes contribute to the turnover of brush-border components, pinocytosis and a slower turnover of the components of the microvilli. Studies of the distribution of radioactivity among glycoprotein components of the brush borders, separated by polyacrylamide-gel electrophoresis, indicated that the membrane components turned over in unison.</description><identifier>ISSN: 0264-6021</identifier><identifier>ISSN: 0306-3283</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj1320501</identifier><identifier>PMID: 4724586</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Carbon Isotopes ; Densitometry ; Electrophoresis, Polyacrylamide Gel ; Glucosamine - metabolism ; Glycoproteins - biosynthesis ; Kidney - metabolism ; Kidney Cortex - metabolism ; Lysine - metabolism ; Models, Biological ; Protein Biosynthesis ; Rabbits ; Subcellular Structures ; Time Factors ; Tritium</subject><ispartof>Biochemical journal, 1973-03, Vol.132 (3), p.501-508</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c370t-d6e4c637f0e22de394252eb2319fd4ff9c073d0575493b5f41c7cfbe1a50bf3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1177614/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1177614/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4724586$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Quirk, S J</creatorcontrib><creatorcontrib>Byrne, J</creatorcontrib><creatorcontrib>Robinson, G B</creatorcontrib><title>Studies on the turnover of protein and glycoprotein components in rabbit kidney brush borders</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>The kinetics of incorporation of [(3)H]lysine and [(14)C]glucosamine into kidney brush borders were studied in vivo. The patterns of incorporation and loss of radioactivity from the brush borders were similar for both radioactively labelled precursors. Maximal labelling occurred 15-20h after injection of the precursors, and then the radioactivity declined rapidly until 50h. The radioactivity of brush borders then remained constant until 120h and thereafter declined slowly. These results are interpreted as indicating that two processes contribute to the turnover of brush-border components, pinocytosis and a slower turnover of the components of the microvilli. Studies of the distribution of radioactivity among glycoprotein components of the brush borders, separated by polyacrylamide-gel electrophoresis, indicated that the membrane components turned over in unison.</description><subject>Animals</subject><subject>Carbon Isotopes</subject><subject>Densitometry</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Glucosamine - metabolism</subject><subject>Glycoproteins - biosynthesis</subject><subject>Kidney - metabolism</subject><subject>Kidney Cortex - metabolism</subject><subject>Lysine - metabolism</subject><subject>Models, Biological</subject><subject>Protein Biosynthesis</subject><subject>Rabbits</subject><subject>Subcellular Structures</subject><subject>Time Factors</subject><subject>Tritium</subject><issn>0264-6021</issn><issn>0306-3283</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkU1LJDEQhoMoOs7uwR8g5LTgobXy0Z3uiyDiFwx40KuETlJxWnuS2aRbmH9vi7PDeiqq6uGtl3oJOWFwzkDyC_PGBIcS2B6ZMamgqBWv98kMeCWLCjg7Isc5vwEwCRIOyaFUXJZ1NSMvT8PoOsw0BjoskQ5jCvEDE42erlMcsAu0DY6-9hsb_w1sXK1jwDBkOnWpNaYb6HvnAm6oSWNeUhOTw5R_kQPf9hl_b-ucPN3ePF_fF4vHu4frq0VhhYKhcBVKWwnlATl3KBrJS46GC9Z4J71vLCjhoFSlbIQpvWRWWW-QtSUYL-bk8lt1PZoVOjsZS22v16lbtWmjY9vpn5vQLfVr_NCMKVUxOQn82Qqk-HfEPOhVly32fRswjlnXrKlrKfkEnn2DNsWcE_rdEQb6Kwm9S2JiT_93tSO3rxefRMeGeg</recordid><startdate>19730301</startdate><enddate>19730301</enddate><creator>Quirk, S J</creator><creator>Byrne, J</creator><creator>Robinson, G B</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><scope>5PM</scope></search><sort><creationdate>19730301</creationdate><title>Studies on the turnover of protein and glycoprotein components in rabbit kidney brush borders</title><author>Quirk, S J ; Byrne, J ; Robinson, G B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c370t-d6e4c637f0e22de394252eb2319fd4ff9c073d0575493b5f41c7cfbe1a50bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Animals</topic><topic>Carbon Isotopes</topic><topic>Densitometry</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Glucosamine - metabolism</topic><topic>Glycoproteins - biosynthesis</topic><topic>Kidney - metabolism</topic><topic>Kidney Cortex - metabolism</topic><topic>Lysine - metabolism</topic><topic>Models, Biological</topic><topic>Protein Biosynthesis</topic><topic>Rabbits</topic><topic>Subcellular Structures</topic><topic>Time Factors</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Quirk, S J</creatorcontrib><creatorcontrib>Byrne, J</creatorcontrib><creatorcontrib>Robinson, G B</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Quirk, S J</au><au>Byrne, J</au><au>Robinson, G B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on the turnover of protein and glycoprotein components in rabbit kidney brush borders</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1973-03-01</date><risdate>1973</risdate><volume>132</volume><issue>3</issue><spage>501</spage><epage>508</epage><pages>501-508</pages><issn>0264-6021</issn><issn>0306-3283</issn><eissn>1470-8728</eissn><abstract>The kinetics of incorporation of [(3)H]lysine and [(14)C]glucosamine into kidney brush borders were studied in vivo. The patterns of incorporation and loss of radioactivity from the brush borders were similar for both radioactively labelled precursors. Maximal labelling occurred 15-20h after injection of the precursors, and then the radioactivity declined rapidly until 50h. The radioactivity of brush borders then remained constant until 120h and thereafter declined slowly. These results are interpreted as indicating that two processes contribute to the turnover of brush-border components, pinocytosis and a slower turnover of the components of the microvilli. Studies of the distribution of radioactivity among glycoprotein components of the brush borders, separated by polyacrylamide-gel electrophoresis, indicated that the membrane components turned over in unison.</abstract><cop>England</cop><pmid>4724586</pmid><doi>10.1042/bj1320501</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Carbon Isotopes Densitometry Electrophoresis, Polyacrylamide Gel Glucosamine - metabolism Glycoproteins - biosynthesis Kidney - metabolism Kidney Cortex - metabolism Lysine - metabolism Models, Biological Protein Biosynthesis Rabbits Subcellular Structures Time Factors Tritium |
title | Studies on the turnover of protein and glycoprotein components in rabbit kidney brush borders |
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