Angiotensin-Converting Enzyme Substrates Hydrolyzed by Fibroblasts and Vascular Endothelial Cells
Angiotensin-converting enzyme (ACE, E.C. 3.4.15.1) activity has been documented in eight cultures of fibroblasts with the ACE substrates benzoyl-phe-ala-pro and hippuryl-his-leu. Hydrolysis of these ACE substrates by fibroblasts is inhibited by SQ-14225 and SQ-20881, specific inhibitors of ACE activ...
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| Veröffentlicht in: | Experimental lung research 1982-01, Vol.3 (2), p.137-145 |
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| creator | Rubin, D. B. Mason, R. J. Dobbs, L. J. |
| description | Angiotensin-converting enzyme (ACE, E.C. 3.4.15.1) activity has been documented in eight cultures of fibroblasts with the ACE substrates benzoyl-phe-ala-pro and hippuryl-his-leu. Hydrolysis of these ACE substrates by fibroblasts is inhibited by SQ-14225 and SQ-20881, specific inhibitors of ACE activity, and by EDTA. However, ACE activity in seven of eight cultures of fibroblasts tested is less than ACE activity in two cultures of vascular endothelial cells. The rates of hydrolysis of benzoyl-phe-ala-pro by fibroblasts and by endothelial cells differ at high substrate concentrations; therefore, the ACE activity in fibroblasts may be due to either a different isoenzyme of ACE or a different accessibility to substrate. Production of angiotensin II from angio-tensin I is documented in cultures of vascular endothelial cells but not in cultures of fibroblasts, however, angiotensin II is further degraded by fibroblasts and not by endothelial cells. |
| doi_str_mv | 10.3109/01902148209063288 |
| format | Article |
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Production of angiotensin II from angio-tensin I is documented in cultures of vascular endothelial cells but not in cultures of fibroblasts, however, angiotensin II is further degraded by fibroblasts and not by endothelial cells.</description><identifier>ISSN: 0190-2148</identifier><identifier>EISSN: 1521-0499</identifier><identifier>DOI: 10.3109/01902148209063288</identifier><identifier>PMID: 6179773</identifier><language>eng</language><publisher>England: Informa UK Ltd</publisher><subject>Angiotensin-Converting Enzyme Inhibitors ; Animals ; Blood Vessels - cytology ; Blood Vessels - enzymology ; Captopril - pharmacology ; Cattle ; Cells, Cultured ; Edetic Acid - pharmacology ; Endothelium - cytology ; Endothelium - enzymology ; Fibroblasts - enzymology ; Humans ; Hydrolysis ; In Vitro Techniques ; Oligopeptides ; Peptidyl-Dipeptidase A - analysis ; Teprotide - pharmacology</subject><ispartof>Experimental lung research, 1982-01, Vol.3 (2), p.137-145</ispartof><rights>1982 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 1982</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-7bacab02cd617af883f86426e6ac7a587d22c5d38bda822cc1ee6c05470c5c563</citedby><cites>FETCH-LOGICAL-c401t-7bacab02cd617af883f86426e6ac7a587d22c5d38bda822cc1ee6c05470c5c563</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.3109/01902148209063288$$EPDF$$P50$$Ginformahealthcare$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.3109/01902148209063288$$EHTML$$P50$$Ginformahealthcare$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,59626,60415,61200,61381</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6179773$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rubin, D. B.</creatorcontrib><creatorcontrib>Mason, R. J.</creatorcontrib><creatorcontrib>Dobbs, L. J.</creatorcontrib><title>Angiotensin-Converting Enzyme Substrates Hydrolyzed by Fibroblasts and Vascular Endothelial Cells</title><title>Experimental lung research</title><addtitle>Exp Lung Res</addtitle><description>Angiotensin-converting enzyme (ACE, E.C. 3.4.15.1) activity has been documented in eight cultures of fibroblasts with the ACE substrates benzoyl-phe-ala-pro and hippuryl-his-leu. Hydrolysis of these ACE substrates by fibroblasts is inhibited by SQ-14225 and SQ-20881, specific inhibitors of ACE activity, and by EDTA. However, ACE activity in seven of eight cultures of fibroblasts tested is less than ACE activity in two cultures of vascular endothelial cells. The rates of hydrolysis of benzoyl-phe-ala-pro by fibroblasts and by endothelial cells differ at high substrate concentrations; therefore, the ACE activity in fibroblasts may be due to either a different isoenzyme of ACE or a different accessibility to substrate. Production of angiotensin II from angio-tensin I is documented in cultures of vascular endothelial cells but not in cultures of fibroblasts, however, angiotensin II is further degraded by fibroblasts and not by endothelial cells.</description><subject>Angiotensin-Converting Enzyme Inhibitors</subject><subject>Animals</subject><subject>Blood Vessels - cytology</subject><subject>Blood Vessels - enzymology</subject><subject>Captopril - pharmacology</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Edetic Acid - pharmacology</subject><subject>Endothelium - cytology</subject><subject>Endothelium - enzymology</subject><subject>Fibroblasts - enzymology</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>In Vitro Techniques</subject><subject>Oligopeptides</subject><subject>Peptidyl-Dipeptidase A - analysis</subject><subject>Teprotide - pharmacology</subject><issn>0190-2148</issn><issn>1521-0499</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF1LHDEUhkNp0XXbH9ALYa56NzbJfGWoN7KsWhB6oe3tcCY540YyiSaZltlfb5ZdBCl6dQ68H7w8hHxl9KxgtP1OWUs5KwWnLa0LLsQHsmAVZzkt2_YjWez0fGc4JichPFBKeSXqI3JUs6ZtmmJB4MLeaxfRBm3zlbN_0Udt77O13c4jZrdTH6KHiCG7npV3Zt6iyvo5u9S9d72BEEMGVmV_IMjJgE9B5eIGjQaTrdCY8Jl8GsAE_HK4S_L7cn23us5vfl39XF3c5LKkLOZNDxJ6yqVK22AQohhEXfIaa5ANVKJRnMtKFaJXINIrGWItaVU2VFayqosl-bbvffTuacIQu1EHmRaARTeFrilZWSRqycj2RuldCB6H7tHrEfzcMdrtsHb_YU2Z00P51I-oXhIHjkk_3-vaDs6P8M95o7oIs3F-8GClDrvqt-t_vIpvEEzcSPDYPbjJ28TtnXHPjciZjg</recordid><startdate>19820101</startdate><enddate>19820101</enddate><creator>Rubin, D. B.</creator><creator>Mason, R. J.</creator><creator>Dobbs, L. J.</creator><general>Informa UK Ltd</general><general>Taylor & Francis</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>19820101</creationdate><title>Angiotensin-Converting Enzyme Substrates Hydrolyzed by Fibroblasts and Vascular Endothelial Cells</title><author>Rubin, D. B. ; Mason, R. J. ; Dobbs, L. J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-7bacab02cd617af883f86426e6ac7a587d22c5d38bda822cc1ee6c05470c5c563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Angiotensin-Converting Enzyme Inhibitors</topic><topic>Animals</topic><topic>Blood Vessels - cytology</topic><topic>Blood Vessels - enzymology</topic><topic>Captopril - pharmacology</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Edetic Acid - pharmacology</topic><topic>Endothelium - cytology</topic><topic>Endothelium - enzymology</topic><topic>Fibroblasts - enzymology</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>In Vitro Techniques</topic><topic>Oligopeptides</topic><topic>Peptidyl-Dipeptidase A - analysis</topic><topic>Teprotide - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rubin, D. B.</creatorcontrib><creatorcontrib>Mason, R. J.</creatorcontrib><creatorcontrib>Dobbs, L. J.</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>Experimental lung research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rubin, D. B.</au><au>Mason, R. J.</au><au>Dobbs, L. J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Angiotensin-Converting Enzyme Substrates Hydrolyzed by Fibroblasts and Vascular Endothelial Cells</atitle><jtitle>Experimental lung research</jtitle><addtitle>Exp Lung Res</addtitle><date>1982-01-01</date><risdate>1982</risdate><volume>3</volume><issue>2</issue><spage>137</spage><epage>145</epage><pages>137-145</pages><issn>0190-2148</issn><eissn>1521-0499</eissn><abstract>Angiotensin-converting enzyme (ACE, E.C. 3.4.15.1) activity has been documented in eight cultures of fibroblasts with the ACE substrates benzoyl-phe-ala-pro and hippuryl-his-leu. Hydrolysis of these ACE substrates by fibroblasts is inhibited by SQ-14225 and SQ-20881, specific inhibitors of ACE activity, and by EDTA. However, ACE activity in seven of eight cultures of fibroblasts tested is less than ACE activity in two cultures of vascular endothelial cells. The rates of hydrolysis of benzoyl-phe-ala-pro by fibroblasts and by endothelial cells differ at high substrate concentrations; therefore, the ACE activity in fibroblasts may be due to either a different isoenzyme of ACE or a different accessibility to substrate. Production of angiotensin II from angio-tensin I is documented in cultures of vascular endothelial cells but not in cultures of fibroblasts, however, angiotensin II is further degraded by fibroblasts and not by endothelial cells.</abstract><cop>England</cop><pub>Informa UK Ltd</pub><pmid>6179773</pmid><doi>10.3109/01902148209063288</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0190-2148 |
| ispartof | Experimental lung research, 1982-01, Vol.3 (2), p.137-145 |
| issn | 0190-2148 1521-0499 |
| language | eng |
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| source | MEDLINE; Taylor & Francis |
| subjects | Angiotensin-Converting Enzyme Inhibitors Animals Blood Vessels - cytology Blood Vessels - enzymology Captopril - pharmacology Cattle Cells, Cultured Edetic Acid - pharmacology Endothelium - cytology Endothelium - enzymology Fibroblasts - enzymology Humans Hydrolysis In Vitro Techniques Oligopeptides Peptidyl-Dipeptidase A - analysis Teprotide - pharmacology |
| title | Angiotensin-Converting Enzyme Substrates Hydrolyzed by Fibroblasts and Vascular Endothelial Cells |
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