Immunochemical evidence for a unique GPI-anchored carbonic anhydrase isozyme in human cardiomyocytes
1 Vegetative Physiologie, Zentrum Physiologie, Medizinische Hochschule Hannover, and 2 Division of Thoracic and Cardiovascular Surgery, Hannover Medical School, D-30623 Hannover, Germany To clarify the controversial question of cell-specific distribution of carbonic anhydrase (CA) in the heart, en...
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| Veröffentlicht in: | American journal of physiology. Heart and circulatory physiology 2000-04, Vol.278 (4), p.H1335-H1344 |
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| container_title | American journal of physiology. Heart and circulatory physiology |
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| creator | Knuppel-Ruppert, Anja Sylvia Gros, Gerolf Harringer, Wolfgang Kubis, Hans-Peter |
| description | 1 Vegetative Physiologie, Zentrum Physiologie,
Medizinische Hochschule Hannover, and 2 Division
of Thoracic and Cardiovascular Surgery, Hannover Medical School,
D-30623 Hannover, Germany
To clarify the
controversial question of cell-specific distribution of carbonic
anhydrase (CA) in the heart, endothelial cells and cardiomyocytes were
isolated from porcine and human hearts and were characterized with
cell-specific markers. CA activity was found in the microsomal fraction
of both cell types. It was shown by Triton X-114 phase separation that
both cell types possess a membrane-bound form of CA. These CAs share
the same mechanism of membrane-anchoring via
glycosylphosphatidylinositol (GPI), which excludes identity with
transmembrane isoforms CA IX or CA XII. Western blotting analysis of
human microsomes with anti-human CA IV antibodies revealed a marked
difference in immunoreactivity. Endothelial CA activity resulted in
11-fold stronger CA IV bands compared with identical amounts of
myocytic CA activity, indicating that cardiac endothelium and
cardiomyocytes possess immunologically distinct forms of CA. We
conclude that in human hearts CA IV is associated with the endothelium,
whereas most of the CA in myocytes is not identical with one of the
known CA isozymes. This suggests that cardiomyocytic CA is a novel isozyme.
carbonic anhydrase activity; membrane-bound isozyme; porcine heart; human heart |
| doi_str_mv | 10.1152/ajpheart.2000.278.4.H1335 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_10749731</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71007796</sourcerecordid><originalsourceid>FETCH-LOGICAL-c456t-cd83d8e6996f4204624cfbfab8f5eb88d8fa5c2013cabfcad7d9c47cc7cb997d3</originalsourceid><addsrcrecordid>eNp1kMFu1DAQhi0EokvhFZC5cEtqx0kcixOqaLtSJTiUs-WM7cZVbAc7oYSnJ8sWtBw4zWG-_5_Rh9A7SkpKm-pCPUyDUWkuK0JIWfGurMsbyljzDO22fVXQhonnaEdYy4qWsuYMvcr5YYMb3rKX6IwSXgvO6A7pvfdLiDAY70CN2Hx32gQw2MaEFV6C-7YYfP1lX6gAQ0xGY1Cpj8EBVmFYdVLZYJfjz9VvM-Bh8SocGO2iXyOss8mv0QurxmzePM1z9PXq093lTXH7-Xp_-fG2gLpp5wJ0x3RnWiFaW1ekbqsabG9V39nG9F2nO6saqAhloHoLSnMtoOYAHHohuGbn6P2xd0pxezvP0rsMZhxVMHHJklNCOBftBoojCCnmnIyVU3JepVVSIg-K5R_F8qBYboplLX8r3rJvn44svTf6JHl0ugEXR2Bw98OjS0ZOw5pdHOP9etL7T-WH_yeulnG8Mz_mv9GTpJy0Zb8Aqj2kJg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71007796</pqid></control><display><type>article</type><title>Immunochemical evidence for a unique GPI-anchored carbonic anhydrase isozyme in human cardiomyocytes</title><source>MEDLINE</source><source>American Physiological Society</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Knuppel-Ruppert, Anja Sylvia ; Gros, Gerolf ; Harringer, Wolfgang ; Kubis, Hans-Peter</creator><creatorcontrib>Knuppel-Ruppert, Anja Sylvia ; Gros, Gerolf ; Harringer, Wolfgang ; Kubis, Hans-Peter</creatorcontrib><description>1 Vegetative Physiologie, Zentrum Physiologie,
Medizinische Hochschule Hannover, and 2 Division
of Thoracic and Cardiovascular Surgery, Hannover Medical School,
D-30623 Hannover, Germany
To clarify the
controversial question of cell-specific distribution of carbonic
anhydrase (CA) in the heart, endothelial cells and cardiomyocytes were
isolated from porcine and human hearts and were characterized with
cell-specific markers. CA activity was found in the microsomal fraction
of both cell types. It was shown by Triton X-114 phase separation that
both cell types possess a membrane-bound form of CA. These CAs share
the same mechanism of membrane-anchoring via
glycosylphosphatidylinositol (GPI), which excludes identity with
transmembrane isoforms CA IX or CA XII. Western blotting analysis of
human microsomes with anti-human CA IV antibodies revealed a marked
difference in immunoreactivity. Endothelial CA activity resulted in
11-fold stronger CA IV bands compared with identical amounts of
myocytic CA activity, indicating that cardiac endothelium and
cardiomyocytes possess immunologically distinct forms of CA. We
conclude that in human hearts CA IV is associated with the endothelium,
whereas most of the CA in myocytes is not identical with one of the
known CA isozymes. This suggests that cardiomyocytic CA is a novel isozyme.
carbonic anhydrase activity; membrane-bound isozyme; porcine heart; human heart</description><identifier>ISSN: 0363-6135</identifier><identifier>EISSN: 1522-1539</identifier><identifier>DOI: 10.1152/ajpheart.2000.278.4.H1335</identifier><identifier>PMID: 10749731</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Antibody Specificity ; Biomarkers ; Carbonic Anhydrases - analysis ; Carbonic Anhydrases - immunology ; Carbonic Anhydrases - metabolism ; Cell Separation ; Detergents ; Endothelium - chemistry ; Endothelium - cytology ; Endothelium - enzymology ; Glycosylation ; Glycosylphosphatidylinositols - analysis ; Heart Ventricles - chemistry ; Heart Ventricles - cytology ; Heart Ventricles - enzymology ; Humans ; Isoenzymes - analysis ; Isoenzymes - immunology ; Isoenzymes - metabolism ; Male ; Middle Aged ; Muscle Fibers, Skeletal - chemistry ; Muscle Fibers, Skeletal - cytology ; Muscle Fibers, Skeletal - enzymology ; Myocardium - chemistry ; Myocardium - cytology ; Myocardium - enzymology ; Myosin Heavy Chains - analysis ; Nitric Oxide Synthase - analysis ; Nitric Oxide Synthase Type III ; Polyethylene Glycols ; Sarcolemma - enzymology ; Swine</subject><ispartof>American journal of physiology. Heart and circulatory physiology, 2000-04, Vol.278 (4), p.H1335-H1344</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-cd83d8e6996f4204624cfbfab8f5eb88d8fa5c2013cabfcad7d9c47cc7cb997d3</citedby><cites>FETCH-LOGICAL-c456t-cd83d8e6996f4204624cfbfab8f5eb88d8fa5c2013cabfcad7d9c47cc7cb997d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3026,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10749731$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Knuppel-Ruppert, Anja Sylvia</creatorcontrib><creatorcontrib>Gros, Gerolf</creatorcontrib><creatorcontrib>Harringer, Wolfgang</creatorcontrib><creatorcontrib>Kubis, Hans-Peter</creatorcontrib><title>Immunochemical evidence for a unique GPI-anchored carbonic anhydrase isozyme in human cardiomyocytes</title><title>American journal of physiology. Heart and circulatory physiology</title><addtitle>Am J Physiol Heart Circ Physiol</addtitle><description>1 Vegetative Physiologie, Zentrum Physiologie,
Medizinische Hochschule Hannover, and 2 Division
of Thoracic and Cardiovascular Surgery, Hannover Medical School,
D-30623 Hannover, Germany
To clarify the
controversial question of cell-specific distribution of carbonic
anhydrase (CA) in the heart, endothelial cells and cardiomyocytes were
isolated from porcine and human hearts and were characterized with
cell-specific markers. CA activity was found in the microsomal fraction
of both cell types. It was shown by Triton X-114 phase separation that
both cell types possess a membrane-bound form of CA. These CAs share
the same mechanism of membrane-anchoring via
glycosylphosphatidylinositol (GPI), which excludes identity with
transmembrane isoforms CA IX or CA XII. Western blotting analysis of
human microsomes with anti-human CA IV antibodies revealed a marked
difference in immunoreactivity. Endothelial CA activity resulted in
11-fold stronger CA IV bands compared with identical amounts of
myocytic CA activity, indicating that cardiac endothelium and
cardiomyocytes possess immunologically distinct forms of CA. We
conclude that in human hearts CA IV is associated with the endothelium,
whereas most of the CA in myocytes is not identical with one of the
known CA isozymes. This suggests that cardiomyocytic CA is a novel isozyme.
carbonic anhydrase activity; membrane-bound isozyme; porcine heart; human heart</description><subject>Animals</subject><subject>Antibody Specificity</subject><subject>Biomarkers</subject><subject>Carbonic Anhydrases - analysis</subject><subject>Carbonic Anhydrases - immunology</subject><subject>Carbonic Anhydrases - metabolism</subject><subject>Cell Separation</subject><subject>Detergents</subject><subject>Endothelium - chemistry</subject><subject>Endothelium - cytology</subject><subject>Endothelium - enzymology</subject><subject>Glycosylation</subject><subject>Glycosylphosphatidylinositols - analysis</subject><subject>Heart Ventricles - chemistry</subject><subject>Heart Ventricles - cytology</subject><subject>Heart Ventricles - enzymology</subject><subject>Humans</subject><subject>Isoenzymes - analysis</subject><subject>Isoenzymes - immunology</subject><subject>Isoenzymes - metabolism</subject><subject>Male</subject><subject>Middle Aged</subject><subject>Muscle Fibers, Skeletal - chemistry</subject><subject>Muscle Fibers, Skeletal - cytology</subject><subject>Muscle Fibers, Skeletal - enzymology</subject><subject>Myocardium - chemistry</subject><subject>Myocardium - cytology</subject><subject>Myocardium - enzymology</subject><subject>Myosin Heavy Chains - analysis</subject><subject>Nitric Oxide Synthase - analysis</subject><subject>Nitric Oxide Synthase Type III</subject><subject>Polyethylene Glycols</subject><subject>Sarcolemma - enzymology</subject><subject>Swine</subject><issn>0363-6135</issn><issn>1522-1539</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMFu1DAQhi0EokvhFZC5cEtqx0kcixOqaLtSJTiUs-WM7cZVbAc7oYSnJ8sWtBw4zWG-_5_Rh9A7SkpKm-pCPUyDUWkuK0JIWfGurMsbyljzDO22fVXQhonnaEdYy4qWsuYMvcr5YYMb3rKX6IwSXgvO6A7pvfdLiDAY70CN2Hx32gQw2MaEFV6C-7YYfP1lX6gAQ0xGY1Cpj8EBVmFYdVLZYJfjz9VvM-Bh8SocGO2iXyOss8mv0QurxmzePM1z9PXq093lTXH7-Xp_-fG2gLpp5wJ0x3RnWiFaW1ekbqsabG9V39nG9F2nO6saqAhloHoLSnMtoOYAHHohuGbn6P2xd0pxezvP0rsMZhxVMHHJklNCOBftBoojCCnmnIyVU3JepVVSIg-K5R_F8qBYboplLX8r3rJvn44svTf6JHl0ugEXR2Bw98OjS0ZOw5pdHOP9etL7T-WH_yeulnG8Mz_mv9GTpJy0Zb8Aqj2kJg</recordid><startdate>20000401</startdate><enddate>20000401</enddate><creator>Knuppel-Ruppert, Anja Sylvia</creator><creator>Gros, Gerolf</creator><creator>Harringer, Wolfgang</creator><creator>Kubis, Hans-Peter</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>20000401</creationdate><title>Immunochemical evidence for a unique GPI-anchored carbonic anhydrase isozyme in human cardiomyocytes</title><author>Knuppel-Ruppert, Anja Sylvia ; Gros, Gerolf ; Harringer, Wolfgang ; Kubis, Hans-Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-cd83d8e6996f4204624cfbfab8f5eb88d8fa5c2013cabfcad7d9c47cc7cb997d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Antibody Specificity</topic><topic>Biomarkers</topic><topic>Carbonic Anhydrases - analysis</topic><topic>Carbonic Anhydrases - immunology</topic><topic>Carbonic Anhydrases - metabolism</topic><topic>Cell Separation</topic><topic>Detergents</topic><topic>Endothelium - chemistry</topic><topic>Endothelium - cytology</topic><topic>Endothelium - enzymology</topic><topic>Glycosylation</topic><topic>Glycosylphosphatidylinositols - analysis</topic><topic>Heart Ventricles - chemistry</topic><topic>Heart Ventricles - cytology</topic><topic>Heart Ventricles - enzymology</topic><topic>Humans</topic><topic>Isoenzymes - analysis</topic><topic>Isoenzymes - immunology</topic><topic>Isoenzymes - metabolism</topic><topic>Male</topic><topic>Middle Aged</topic><topic>Muscle Fibers, Skeletal - chemistry</topic><topic>Muscle Fibers, Skeletal - cytology</topic><topic>Muscle Fibers, Skeletal - enzymology</topic><topic>Myocardium - chemistry</topic><topic>Myocardium - cytology</topic><topic>Myocardium - enzymology</topic><topic>Myosin Heavy Chains - analysis</topic><topic>Nitric Oxide Synthase - analysis</topic><topic>Nitric Oxide Synthase Type III</topic><topic>Polyethylene Glycols</topic><topic>Sarcolemma - enzymology</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Knuppel-Ruppert, Anja Sylvia</creatorcontrib><creatorcontrib>Gros, Gerolf</creatorcontrib><creatorcontrib>Harringer, Wolfgang</creatorcontrib><creatorcontrib>Kubis, Hans-Peter</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. Heart and circulatory physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Knuppel-Ruppert, Anja Sylvia</au><au>Gros, Gerolf</au><au>Harringer, Wolfgang</au><au>Kubis, Hans-Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunochemical evidence for a unique GPI-anchored carbonic anhydrase isozyme in human cardiomyocytes</atitle><jtitle>American journal of physiology. Heart and circulatory physiology</jtitle><addtitle>Am J Physiol Heart Circ Physiol</addtitle><date>2000-04-01</date><risdate>2000</risdate><volume>278</volume><issue>4</issue><spage>H1335</spage><epage>H1344</epage><pages>H1335-H1344</pages><issn>0363-6135</issn><eissn>1522-1539</eissn><abstract>1 Vegetative Physiologie, Zentrum Physiologie,
Medizinische Hochschule Hannover, and 2 Division
of Thoracic and Cardiovascular Surgery, Hannover Medical School,
D-30623 Hannover, Germany
To clarify the
controversial question of cell-specific distribution of carbonic
anhydrase (CA) in the heart, endothelial cells and cardiomyocytes were
isolated from porcine and human hearts and were characterized with
cell-specific markers. CA activity was found in the microsomal fraction
of both cell types. It was shown by Triton X-114 phase separation that
both cell types possess a membrane-bound form of CA. These CAs share
the same mechanism of membrane-anchoring via
glycosylphosphatidylinositol (GPI), which excludes identity with
transmembrane isoforms CA IX or CA XII. Western blotting analysis of
human microsomes with anti-human CA IV antibodies revealed a marked
difference in immunoreactivity. Endothelial CA activity resulted in
11-fold stronger CA IV bands compared with identical amounts of
myocytic CA activity, indicating that cardiac endothelium and
cardiomyocytes possess immunologically distinct forms of CA. We
conclude that in human hearts CA IV is associated with the endothelium,
whereas most of the CA in myocytes is not identical with one of the
known CA isozymes. This suggests that cardiomyocytic CA is a novel isozyme.
carbonic anhydrase activity; membrane-bound isozyme; porcine heart; human heart</abstract><cop>United States</cop><pmid>10749731</pmid><doi>10.1152/ajpheart.2000.278.4.H1335</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0363-6135 |
| ispartof | American journal of physiology. Heart and circulatory physiology, 2000-04, Vol.278 (4), p.H1335-H1344 |
| issn | 0363-6135 1522-1539 |
| language | eng |
| recordid | cdi_pubmed_primary_10749731 |
| source | MEDLINE; American Physiological Society; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Antibody Specificity Biomarkers Carbonic Anhydrases - analysis Carbonic Anhydrases - immunology Carbonic Anhydrases - metabolism Cell Separation Detergents Endothelium - chemistry Endothelium - cytology Endothelium - enzymology Glycosylation Glycosylphosphatidylinositols - analysis Heart Ventricles - chemistry Heart Ventricles - cytology Heart Ventricles - enzymology Humans Isoenzymes - analysis Isoenzymes - immunology Isoenzymes - metabolism Male Middle Aged Muscle Fibers, Skeletal - chemistry Muscle Fibers, Skeletal - cytology Muscle Fibers, Skeletal - enzymology Myocardium - chemistry Myocardium - cytology Myocardium - enzymology Myosin Heavy Chains - analysis Nitric Oxide Synthase - analysis Nitric Oxide Synthase Type III Polyethylene Glycols Sarcolemma - enzymology Swine |
| title | Immunochemical evidence for a unique GPI-anchored carbonic anhydrase isozyme in human cardiomyocytes |
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