Identification and Possible Localization of cGMP-Dependent Protein Kinase in Bovine Aortic Endothelial Cells
Endothelial-derived nitric oxide (NO) is an important intercellular messenger. Although endothelial cells contain both nitric oxide synthase and soluble guanylate cyclase, the nature of receptor proteins for cGMP is uncertain. Based on previous work in vascular smooth muscle cells which indicates th...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1994-06, Vol.201 (2), p.531-537 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Macmillancrow, L.A. Murphyullrich, J.E. Lincoln, T.M. |
| description | Endothelial-derived nitric oxide (NO) is an important intercellular messenger. Although endothelial cells contain both nitric oxide synthase and soluble guanylate cyclase, the nature of receptor proteins for cGMP is uncertain. Based on previous work in vascular smooth muscle cells which indicates that the cGMP-dependent protein kinase (cGK) is partially associated with the cytoskeleton, we determined that cGK was present in non-cytosolic fractions of endothelial cells. The data reveal that cGK is found only in Triton-soluble extracts of particulate fractions from bovine aortic endothelial cells and provide the first evidence for the existence of cGK in this cell type based on immunoreactivity, immunofluorescence microscopy and phosphotransferase activity. The limited distribution of endothelial cell cGK may explain why this kinase has not been heretofore identified in endothelial cells. |
| doi_str_mv | 10.1006/bbrc.1994.1734 |
| format | Article |
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Although endothelial cells contain both nitric oxide synthase and soluble guanylate cyclase, the nature of receptor proteins for cGMP is uncertain. Based on previous work in vascular smooth muscle cells which indicates that the cGMP-dependent protein kinase (cGK) is partially associated with the cytoskeleton, we determined that cGK was present in non-cytosolic fractions of endothelial cells. The data reveal that cGK is found only in Triton-soluble extracts of particulate fractions from bovine aortic endothelial cells and provide the first evidence for the existence of cGK in this cell type based on immunoreactivity, immunofluorescence microscopy and phosphotransferase activity. The limited distribution of endothelial cell cGK may explain why this kinase has not been heretofore identified in endothelial cells.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1994.1734</identifier><identifier>PMID: 8002983</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Aorta ; Blotting, Western ; Cattle ; Cell Membrane - enzymology ; Cell Membrane - ultrastructure ; Cells, Cultured ; Cyclic GMP-Dependent Protein Kinases - analysis ; Cyclic GMP-Dependent Protein Kinases - metabolism ; Cytoskeleton - enzymology ; Cytoskeleton - ultrastructure ; Electrophoresis, Polyacrylamide Gel ; Endothelium, Vascular - cytology ; Endothelium, Vascular - enzymology ; Fluorescent Antibody Technique ; Immunohistochemistry ; Molecular Weight ; Phosphorylation ; Phosphotransferases - analysis ; Phosphotransferases - metabolism ; Subcellular Fractions - enzymology</subject><ispartof>Biochemical and biophysical research communications, 1994-06, Vol.201 (2), p.531-537</ispartof><rights>1994 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-d0047840e8ef7f79353a4dd1299d5acd0450b4d464d1dc28d1d0e7ba6a2aaec43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.1994.1734$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8002983$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Macmillancrow, L.A.</creatorcontrib><creatorcontrib>Murphyullrich, J.E.</creatorcontrib><creatorcontrib>Lincoln, T.M.</creatorcontrib><title>Identification and Possible Localization of cGMP-Dependent Protein Kinase in Bovine Aortic Endothelial Cells</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Endothelial-derived nitric oxide (NO) is an important intercellular messenger. Although endothelial cells contain both nitric oxide synthase and soluble guanylate cyclase, the nature of receptor proteins for cGMP is uncertain. Based on previous work in vascular smooth muscle cells which indicates that the cGMP-dependent protein kinase (cGK) is partially associated with the cytoskeleton, we determined that cGK was present in non-cytosolic fractions of endothelial cells. The data reveal that cGK is found only in Triton-soluble extracts of particulate fractions from bovine aortic endothelial cells and provide the first evidence for the existence of cGK in this cell type based on immunoreactivity, immunofluorescence microscopy and phosphotransferase activity. The limited distribution of endothelial cell cGK may explain why this kinase has not been heretofore identified in endothelial cells.</description><subject>Animals</subject><subject>Aorta</subject><subject>Blotting, Western</subject><subject>Cattle</subject><subject>Cell Membrane - enzymology</subject><subject>Cell Membrane - ultrastructure</subject><subject>Cells, Cultured</subject><subject>Cyclic GMP-Dependent Protein Kinases - analysis</subject><subject>Cyclic GMP-Dependent Protein Kinases - metabolism</subject><subject>Cytoskeleton - enzymology</subject><subject>Cytoskeleton - ultrastructure</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endothelium, Vascular - cytology</subject><subject>Endothelium, Vascular - enzymology</subject><subject>Fluorescent Antibody Technique</subject><subject>Immunohistochemistry</subject><subject>Molecular Weight</subject><subject>Phosphorylation</subject><subject>Phosphotransferases - analysis</subject><subject>Phosphotransferases - metabolism</subject><subject>Subcellular Fractions - enzymology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kL1PwzAQxS0EKuVjZUPyxJZyTtwkHkv5FEV0AInNcuyLMErtYqdI8NfjqBUby91J793T3Y-QMwYTBlBeNk3QEyYEn7Cq4HtkzEBAljPg-2QMyZHlgr0dkqMYPwAY46UYkVENkIu6GJPuwaDrbWu16q13VDlDlz5G23RIF16rzv5sFd9Sffe0zK5xjW5Yosvge7SOPlqnItI0Xfkv65DOfOitpjfO-P4dO6s6OseuiyfkoFVdxNNdPyavtzcv8_ts8Xz3MJ8tMl0Uos8MAK9qDlhjW7WVKKaF4sawXAgzVdoAn0LDDS-5YUbndaqAVaNKlSuFmhfH5GKbuw7-c4OxlysbdbpAOfSbKKtyymte1Mk42Rp1SD8HbOU62JUK35KBHPDKAa8c8MoBb1o43yVvmhWaP_uOZ9LrrY7pvS-LQUZt0Wk0NqDupfH2v-hffP2KgQ</recordid><startdate>19940615</startdate><enddate>19940615</enddate><creator>Macmillancrow, L.A.</creator><creator>Murphyullrich, J.E.</creator><creator>Lincoln, T.M.</creator><general>Elsevier Inc</general><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>19940615</creationdate><title>Identification and Possible Localization of cGMP-Dependent Protein Kinase in Bovine Aortic Endothelial Cells</title><author>Macmillancrow, L.A. ; Murphyullrich, J.E. ; Lincoln, T.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-d0047840e8ef7f79353a4dd1299d5acd0450b4d464d1dc28d1d0e7ba6a2aaec43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Aorta</topic><topic>Blotting, Western</topic><topic>Cattle</topic><topic>Cell Membrane - enzymology</topic><topic>Cell Membrane - ultrastructure</topic><topic>Cells, Cultured</topic><topic>Cyclic GMP-Dependent Protein Kinases - analysis</topic><topic>Cyclic GMP-Dependent Protein Kinases - metabolism</topic><topic>Cytoskeleton - enzymology</topic><topic>Cytoskeleton - ultrastructure</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endothelium, Vascular - cytology</topic><topic>Endothelium, Vascular - enzymology</topic><topic>Fluorescent Antibody Technique</topic><topic>Immunohistochemistry</topic><topic>Molecular Weight</topic><topic>Phosphorylation</topic><topic>Phosphotransferases - analysis</topic><topic>Phosphotransferases - metabolism</topic><topic>Subcellular Fractions - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Macmillancrow, L.A.</creatorcontrib><creatorcontrib>Murphyullrich, J.E.</creatorcontrib><creatorcontrib>Lincoln, T.M.</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Macmillancrow, L.A.</au><au>Murphyullrich, J.E.</au><au>Lincoln, T.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and Possible Localization of cGMP-Dependent Protein Kinase in Bovine Aortic Endothelial Cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1994-06-15</date><risdate>1994</risdate><volume>201</volume><issue>2</issue><spage>531</spage><epage>537</epage><pages>531-537</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Endothelial-derived nitric oxide (NO) is an important intercellular messenger. Although endothelial cells contain both nitric oxide synthase and soluble guanylate cyclase, the nature of receptor proteins for cGMP is uncertain. Based on previous work in vascular smooth muscle cells which indicates that the cGMP-dependent protein kinase (cGK) is partially associated with the cytoskeleton, we determined that cGK was present in non-cytosolic fractions of endothelial cells. The data reveal that cGK is found only in Triton-soluble extracts of particulate fractions from bovine aortic endothelial cells and provide the first evidence for the existence of cGK in this cell type based on immunoreactivity, immunofluorescence microscopy and phosphotransferase activity. The limited distribution of endothelial cell cGK may explain why this kinase has not been heretofore identified in endothelial cells.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8002983</pmid><doi>10.1006/bbrc.1994.1734</doi><tpages>7</tpages></addata></record> |
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| subjects | Animals Aorta Blotting, Western Cattle Cell Membrane - enzymology Cell Membrane - ultrastructure Cells, Cultured Cyclic GMP-Dependent Protein Kinases - analysis Cyclic GMP-Dependent Protein Kinases - metabolism Cytoskeleton - enzymology Cytoskeleton - ultrastructure Electrophoresis, Polyacrylamide Gel Endothelium, Vascular - cytology Endothelium, Vascular - enzymology Fluorescent Antibody Technique Immunohistochemistry Molecular Weight Phosphorylation Phosphotransferases - analysis Phosphotransferases - metabolism Subcellular Fractions - enzymology |
| title | Identification and Possible Localization of cGMP-Dependent Protein Kinase in Bovine Aortic Endothelial Cells |
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