Carbonic anhydrase III in obese Zucker rats
Proteins from 5- to to 7-wk-old lean and obese Zucker rats were separated by one-dimensional sodium dodecyl sulfate (SDS) and two-dimensional SDS-isoelectric focusing-polyacrylamide gel electrophoresis. laser densitometry revealed an obesity-related decrease in the concentration of a 28-kDa cytosoli...
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| Veröffentlicht in: | American journal of physiology: endocrinology and metabolism 1993-04, Vol.264 (4), p.E621-E630 |
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| container_title | American journal of physiology: endocrinology and metabolism |
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| creator | Lynch, C. J Brennan, W. A., Jr Vary, T. C Carter, N Dodgson, S. J |
| description | Proteins from 5- to to 7-wk-old lean and obese Zucker rats were separated by one-dimensional sodium dodecyl sulfate (SDS) and two-dimensional SDS-isoelectric focusing-polyacrylamide gel electrophoresis. laser densitometry revealed an obesity-related decrease in the concentration of a 28-kDa cytosolic adipocyte protein, the most abundant protein in adipocytes from lean Zucker rats. Microsequencing revealed the identity of this protein to be carbonic anhydrase III (CA III). The identity and obesity-related decrease was further confirmed using isoform-specific antisera and CA Ill enzyme activity measurements made by 18(O) mass spectrometry. Immunoblotting studies also revealed that CA III is present in at least two charge isoforms in adipocytes. Our data indicate that lean Zucker rat adipocytes may represent the richest source of CA III in nature (24% of the cytosolic protein content). An obesity-related decrease in both the concentration and activity of CA III was observed in two lipogenic tissues, liver and white fat. but not in soleus muscle. Adipocyte CA III activity was no longer depressed when hyperinsulinemic obese rats were made insulin deficient by streptozotocin injection. This suggests that the obesity-related decrease in CA III may be related to the hyperinsulinemia as well as to the insulin hyper-responsiveness that adipocytes from obese Zucker rats of this age display. |
| doi_str_mv | 10.1152/ajpendo.1993.264.4.E621 |
| format | Article |
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J ; Brennan, W. A., Jr ; Vary, T. C ; Carter, N ; Dodgson, S. J</creator><creatorcontrib>Lynch, C. J ; Brennan, W. A., Jr ; Vary, T. C ; Carter, N ; Dodgson, S. J ; Auswertungs- und Informationsdienst fuer Ernaehrung, Landwirtschaft und Forsten, Bonn (Germany)</creatorcontrib><description>Proteins from 5- to to 7-wk-old lean and obese Zucker rats were separated by one-dimensional sodium dodecyl sulfate (SDS) and two-dimensional SDS-isoelectric focusing-polyacrylamide gel electrophoresis. laser densitometry revealed an obesity-related decrease in the concentration of a 28-kDa cytosolic adipocyte protein, the most abundant protein in adipocytes from lean Zucker rats. Microsequencing revealed the identity of this protein to be carbonic anhydrase III (CA III). The identity and obesity-related decrease was further confirmed using isoform-specific antisera and CA Ill enzyme activity measurements made by 18(O) mass spectrometry. Immunoblotting studies also revealed that CA III is present in at least two charge isoforms in adipocytes. Our data indicate that lean Zucker rat adipocytes may represent the richest source of CA III in nature (24% of the cytosolic protein content). An obesity-related decrease in both the concentration and activity of CA III was observed in two lipogenic tissues, liver and white fat. but not in soleus muscle. Adipocyte CA III activity was no longer depressed when hyperinsulinemic obese rats were made insulin deficient by streptozotocin injection. 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J</creatorcontrib><creatorcontrib>Brennan, W. A., Jr</creatorcontrib><creatorcontrib>Vary, T. C</creatorcontrib><creatorcontrib>Carter, N</creatorcontrib><creatorcontrib>Dodgson, S. J</creatorcontrib><creatorcontrib>Auswertungs- und Informationsdienst fuer Ernaehrung, Landwirtschaft und Forsten, Bonn (Germany)</creatorcontrib><title>Carbonic anhydrase III in obese Zucker rats</title><title>American journal of physiology: endocrinology and metabolism</title><addtitle>Am J Physiol</addtitle><description>Proteins from 5- to to 7-wk-old lean and obese Zucker rats were separated by one-dimensional sodium dodecyl sulfate (SDS) and two-dimensional SDS-isoelectric focusing-polyacrylamide gel electrophoresis. laser densitometry revealed an obesity-related decrease in the concentration of a 28-kDa cytosolic adipocyte protein, the most abundant protein in adipocytes from lean Zucker rats. Microsequencing revealed the identity of this protein to be carbonic anhydrase III (CA III). The identity and obesity-related decrease was further confirmed using isoform-specific antisera and CA Ill enzyme activity measurements made by 18(O) mass spectrometry. Immunoblotting studies also revealed that CA III is present in at least two charge isoforms in adipocytes. Our data indicate that lean Zucker rat adipocytes may represent the richest source of CA III in nature (24% of the cytosolic protein content). An obesity-related decrease in both the concentration and activity of CA III was observed in two lipogenic tissues, liver and white fat. but not in soleus muscle. Adipocyte CA III activity was no longer depressed when hyperinsulinemic obese rats were made insulin deficient by streptozotocin injection. This suggests that the obesity-related decrease in CA III may be related to the hyperinsulinemia as well as to the insulin hyper-responsiveness that adipocytes from obese Zucker rats of this age display.</description><subject>actividad enzimatica</subject><subject>activite enzymatique</subject><subject>Adipose Tissue - enzymology</subject><subject>adipose tissues</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>carbonate dehydratase</subject><subject>carbonate deshydratase</subject><subject>carbonato deshidratasa</subject><subject>Carbonic Anhydrases - genetics</subject><subject>Carbonic Anhydrases - isolation & purification</subject><subject>cells</subject><subject>cellule</subject><subject>celulas</subject><subject>Diabetes Mellitus - enzymology</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>enzymic activity</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - isolation & purification</subject><subject>Male</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Obesity - enzymology</subject><subject>Obesity - genetics</subject><subject>overweight</subject><subject>rat</subject><subject>rata</subject><subject>Rats</subject><subject>Rats, Zucker - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>sobrepeso</subject><subject>surpoids</subject><subject>tejido adiposo</subject><subject>tissu adipeux</subject><issn>0002-9513</issn><issn>0193-1849</issn><issn>2163-5773</issn><issn>1522-1555</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkM1Kw0AUhQdRaq0-gpqVG0mcyfxmKaVqoOBCu3EzTJKZJjXN1JkGydubkFBwdbmcc8_hfgDcIxghROMntTvoprARShIcxYxEJFqxGJ2BeYwYDinn-BzMIYRxmFCEL8GV97t-RRSTGZgJwhkkaA4el8pltqnyQDVlVzjldZCmaVA1gc10v3y1-bd2gVNHfw0ujKq9vpnmAmxeVp_Lt3D9_poun9dhjllyDJkxEClKOKECalyoXMSxMH0zokLRAvM8h4VBwvAiQYSQRFHMdMY1zrTgFC_Aw5h7cPan1f4o95XPdV2rRtvWS06ZgMOHC8BHY-6s904beXDVXrlOIigHTHLCJAdMssckiRww9Ze3U0Wb7XVxupu49Ho46mW1LX8rp-Wh7Hxla7vtTqH_8u5Gv1FWqq2rvNx89KUEwgQTwvEfvo58yA</recordid><startdate>19930401</startdate><enddate>19930401</enddate><creator>Lynch, C. 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J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c369t-6ff01a5474580e3dac8228f153158a5d37cc0df18f7d914449a536eb7e3be8753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>actividad enzimatica</topic><topic>activite enzymatique</topic><topic>Adipose Tissue - enzymology</topic><topic>adipose tissues</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>carbonate dehydratase</topic><topic>carbonate deshydratase</topic><topic>carbonato deshidratasa</topic><topic>Carbonic Anhydrases - genetics</topic><topic>Carbonic Anhydrases - isolation & purification</topic><topic>cells</topic><topic>cellule</topic><topic>celulas</topic><topic>Diabetes Mellitus - enzymology</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>enzymic activity</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - isolation & purification</topic><topic>Male</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Obesity - enzymology</topic><topic>Obesity - genetics</topic><topic>overweight</topic><topic>rat</topic><topic>rata</topic><topic>Rats</topic><topic>Rats, Zucker - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>sobrepeso</topic><topic>surpoids</topic><topic>tejido adiposo</topic><topic>tissu adipeux</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lynch, C. J</creatorcontrib><creatorcontrib>Brennan, W. A., Jr</creatorcontrib><creatorcontrib>Vary, T. C</creatorcontrib><creatorcontrib>Carter, N</creatorcontrib><creatorcontrib>Dodgson, S. J</creatorcontrib><creatorcontrib>Auswertungs- und Informationsdienst fuer Ernaehrung, Landwirtschaft und Forsten, Bonn (Germany)</creatorcontrib><collection>AGRIS</collection><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: endocrinology and metabolism</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lynch, C. J</au><au>Brennan, W. A., Jr</au><au>Vary, T. C</au><au>Carter, N</au><au>Dodgson, S. J</au><aucorp>Auswertungs- und Informationsdienst fuer Ernaehrung, Landwirtschaft und Forsten, Bonn (Germany)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Carbonic anhydrase III in obese Zucker rats</atitle><jtitle>American journal of physiology: endocrinology and metabolism</jtitle><addtitle>Am J Physiol</addtitle><date>1993-04-01</date><risdate>1993</risdate><volume>264</volume><issue>4</issue><spage>E621</spage><epage>E630</epage><pages>E621-E630</pages><issn>0002-9513</issn><issn>0193-1849</issn><eissn>2163-5773</eissn><eissn>1522-1555</eissn><abstract>Proteins from 5- to to 7-wk-old lean and obese Zucker rats were separated by one-dimensional sodium dodecyl sulfate (SDS) and two-dimensional SDS-isoelectric focusing-polyacrylamide gel electrophoresis. laser densitometry revealed an obesity-related decrease in the concentration of a 28-kDa cytosolic adipocyte protein, the most abundant protein in adipocytes from lean Zucker rats. Microsequencing revealed the identity of this protein to be carbonic anhydrase III (CA III). The identity and obesity-related decrease was further confirmed using isoform-specific antisera and CA Ill enzyme activity measurements made by 18(O) mass spectrometry. Immunoblotting studies also revealed that CA III is present in at least two charge isoforms in adipocytes. Our data indicate that lean Zucker rat adipocytes may represent the richest source of CA III in nature (24% of the cytosolic protein content). An obesity-related decrease in both the concentration and activity of CA III was observed in two lipogenic tissues, liver and white fat. but not in soleus muscle. Adipocyte CA III activity was no longer depressed when hyperinsulinemic obese rats were made insulin deficient by streptozotocin injection. This suggests that the obesity-related decrease in CA III may be related to the hyperinsulinemia as well as to the insulin hyper-responsiveness that adipocytes from obese Zucker rats of this age display.</abstract><cop>United States</cop><pmid>8476041</pmid><doi>10.1152/ajpendo.1993.264.4.E621</doi></addata></record> |
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| subjects | actividad enzimatica activite enzymatique Adipose Tissue - enzymology adipose tissues Amino Acid Sequence Animals carbonate dehydratase carbonate deshydratase carbonato deshidratasa Carbonic Anhydrases - genetics Carbonic Anhydrases - isolation & purification cells cellule celulas Diabetes Mellitus - enzymology Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel enzymic activity Isoenzymes - genetics Isoenzymes - isolation & purification Male Mice Molecular Sequence Data Molecular Weight Obesity - enzymology Obesity - genetics overweight rat rata Rats Rats, Zucker - metabolism Sequence Homology, Amino Acid sobrepeso surpoids tejido adiposo tissu adipeux |
| title | Carbonic anhydrase III in obese Zucker rats |
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