Cardiopulmonary bypass induces the synthesis and release of matrix metalloproteinases
Background. A number of cellular and molecular events can be induced after cardiac procedures requiring cardiopulmonary bypass (CPB). The matrix metalloproteinases (MMPs) are a recently discovered family of enzymes that degrade the extracellular matrix, but expression during and after CPB is unknown...
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Veröffentlicht in: | The Annals of thoracic surgery 2001-05, Vol.71 (5), p.1518-1523 |
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container_title | The Annals of thoracic surgery |
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creator | Joffs, Cassandra Gunasinghe, Himali R. Multani, Marlina M. Dorman, B. Hugh Kratz, John M. Crumbley, A. Jackson Crawford, Fred A. Spinale, Francis G. |
description | Background. A number of cellular and molecular events can be induced after cardiac procedures requiring cardiopulmonary bypass (CPB). The matrix metalloproteinases (MMPs) are a recently discovered family of enzymes that degrade the extracellular matrix, but expression during and after CPB is unknown.
Methods. Systemic plasma MMP levels were measured in patients (n = 28, 63 ± 1 years) undergoing elective coronary revascularization requiring CPB at baseline, termination of CPB, and 30 minutes, 6 and 24 hours after CPB. Representative classes of MMP species known to degrade matrix and basement membrane components were selected for study. Specifically, the interstitial collagenases MMP-8 and MMP-13, and the gelatinases MMP-2 and MMP-9 were determined by internally validated enzyme-linked immunosorbent assay.
Results. The MMP-8 levels increased by fourfold at separation from CPB, and returned to within normal values within 30 minutes after CPB. The proenzyme forms of MMP-13 and MMP-9 increased by more than twofold at cross-clamp release and returned within normal limits within 6 hours after CPB. The proform of MMP-2 increased from baseline values at 6 and 24 hours postoperatively; likely indicative of de novo synthesis.
Conclusions. A specific portfolio of MMPs are released and synthesized during and after CPB. Because MMPs can degrade extracellular proteins essential for maintaining normal cellular architecture and function, enhanced MMP release and activation may contribute to alterations in tissue homeostasis in the early postoperative period. |
doi_str_mv | 10.1016/S0003-4975(01)02442-0 |
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Methods. Systemic plasma MMP levels were measured in patients (n = 28, 63 ± 1 years) undergoing elective coronary revascularization requiring CPB at baseline, termination of CPB, and 30 minutes, 6 and 24 hours after CPB. Representative classes of MMP species known to degrade matrix and basement membrane components were selected for study. Specifically, the interstitial collagenases MMP-8 and MMP-13, and the gelatinases MMP-2 and MMP-9 were determined by internally validated enzyme-linked immunosorbent assay.
Results. The MMP-8 levels increased by fourfold at separation from CPB, and returned to within normal values within 30 minutes after CPB. The proenzyme forms of MMP-13 and MMP-9 increased by more than twofold at cross-clamp release and returned within normal limits within 6 hours after CPB. The proform of MMP-2 increased from baseline values at 6 and 24 hours postoperatively; likely indicative of de novo synthesis.
Conclusions. A specific portfolio of MMPs are released and synthesized during and after CPB. Because MMPs can degrade extracellular proteins essential for maintaining normal cellular architecture and function, enhanced MMP release and activation may contribute to alterations in tissue homeostasis in the early postoperative period.</description><identifier>ISSN: 0003-4975</identifier><identifier>EISSN: 1552-6259</identifier><identifier>DOI: 10.1016/S0003-4975(01)02442-0</identifier><identifier>PMID: 11383793</identifier><identifier>CODEN: ATHSAK</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Aged ; Anesthesia ; Anesthesia depending on type of surgery ; Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy ; Biological and medical sciences ; Cardiopulmonary Bypass ; Coronary Artery Bypass ; Enzyme Induction - physiology ; Enzyme-Linked Immunosorbent Assay ; Female ; Humans ; Male ; Matrix Metalloproteinases - blood ; Medical sciences ; Middle Aged ; Thoracic and cardiovascular surgery. Cardiopulmonary bypass</subject><ispartof>The Annals of thoracic surgery, 2001-05, Vol.71 (5), p.1518-1523</ispartof><rights>2001 The Society of Thoracic Surgeons</rights><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c543t-1593a572bdad8a5b76ae9bb110a650f8415465cd4c871afa8993c41d2be5a833</citedby><cites>FETCH-LOGICAL-c543t-1593a572bdad8a5b76ae9bb110a650f8415465cd4c871afa8993c41d2be5a833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0003-4975(01)02442-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27928,27929,45999</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=983923$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11383793$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Joffs, Cassandra</creatorcontrib><creatorcontrib>Gunasinghe, Himali R.</creatorcontrib><creatorcontrib>Multani, Marlina M.</creatorcontrib><creatorcontrib>Dorman, B. Hugh</creatorcontrib><creatorcontrib>Kratz, John M.</creatorcontrib><creatorcontrib>Crumbley, A. Jackson</creatorcontrib><creatorcontrib>Crawford, Fred A.</creatorcontrib><creatorcontrib>Spinale, Francis G.</creatorcontrib><title>Cardiopulmonary bypass induces the synthesis and release of matrix metalloproteinases</title><title>The Annals of thoracic surgery</title><addtitle>Ann Thorac Surg</addtitle><description>Background. A number of cellular and molecular events can be induced after cardiac procedures requiring cardiopulmonary bypass (CPB). The matrix metalloproteinases (MMPs) are a recently discovered family of enzymes that degrade the extracellular matrix, but expression during and after CPB is unknown.
Methods. Systemic plasma MMP levels were measured in patients (n = 28, 63 ± 1 years) undergoing elective coronary revascularization requiring CPB at baseline, termination of CPB, and 30 minutes, 6 and 24 hours after CPB. Representative classes of MMP species known to degrade matrix and basement membrane components were selected for study. Specifically, the interstitial collagenases MMP-8 and MMP-13, and the gelatinases MMP-2 and MMP-9 were determined by internally validated enzyme-linked immunosorbent assay.
Results. The MMP-8 levels increased by fourfold at separation from CPB, and returned to within normal values within 30 minutes after CPB. The proenzyme forms of MMP-13 and MMP-9 increased by more than twofold at cross-clamp release and returned within normal limits within 6 hours after CPB. The proform of MMP-2 increased from baseline values at 6 and 24 hours postoperatively; likely indicative of de novo synthesis.
Conclusions. A specific portfolio of MMPs are released and synthesized during and after CPB. Because MMPs can degrade extracellular proteins essential for maintaining normal cellular architecture and function, enhanced MMP release and activation may contribute to alterations in tissue homeostasis in the early postoperative period.</description><subject>Aged</subject><subject>Anesthesia</subject><subject>Anesthesia depending on type of surgery</subject><subject>Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy</subject><subject>Biological and medical sciences</subject><subject>Cardiopulmonary Bypass</subject><subject>Coronary Artery Bypass</subject><subject>Enzyme Induction - physiology</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Female</subject><subject>Humans</subject><subject>Male</subject><subject>Matrix Metalloproteinases - blood</subject><subject>Medical sciences</subject><subject>Middle Aged</subject><subject>Thoracic and cardiovascular surgery. 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Jackson ; Crawford, Fred A. ; Spinale, Francis G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c543t-1593a572bdad8a5b76ae9bb110a650f8415465cd4c871afa8993c41d2be5a833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Aged</topic><topic>Anesthesia</topic><topic>Anesthesia depending on type of surgery</topic><topic>Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy</topic><topic>Biological and medical sciences</topic><topic>Cardiopulmonary Bypass</topic><topic>Coronary Artery Bypass</topic><topic>Enzyme Induction - physiology</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Female</topic><topic>Humans</topic><topic>Male</topic><topic>Matrix Metalloproteinases - blood</topic><topic>Medical sciences</topic><topic>Middle Aged</topic><topic>Thoracic and cardiovascular surgery. Cardiopulmonary bypass</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Joffs, Cassandra</creatorcontrib><creatorcontrib>Gunasinghe, Himali R.</creatorcontrib><creatorcontrib>Multani, Marlina M.</creatorcontrib><creatorcontrib>Dorman, B. Hugh</creatorcontrib><creatorcontrib>Kratz, John M.</creatorcontrib><creatorcontrib>Crumbley, A. Jackson</creatorcontrib><creatorcontrib>Crawford, Fred A.</creatorcontrib><creatorcontrib>Spinale, Francis G.</creatorcontrib><collection>Pascal-Francis</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>The Annals of thoracic surgery</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joffs, Cassandra</au><au>Gunasinghe, Himali R.</au><au>Multani, Marlina M.</au><au>Dorman, B. Hugh</au><au>Kratz, John M.</au><au>Crumbley, A. Jackson</au><au>Crawford, Fred A.</au><au>Spinale, Francis G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cardiopulmonary bypass induces the synthesis and release of matrix metalloproteinases</atitle><jtitle>The Annals of thoracic surgery</jtitle><addtitle>Ann Thorac Surg</addtitle><date>2001-05-01</date><risdate>2001</risdate><volume>71</volume><issue>5</issue><spage>1518</spage><epage>1523</epage><pages>1518-1523</pages><issn>0003-4975</issn><eissn>1552-6259</eissn><coden>ATHSAK</coden><abstract>Background. A number of cellular and molecular events can be induced after cardiac procedures requiring cardiopulmonary bypass (CPB). The matrix metalloproteinases (MMPs) are a recently discovered family of enzymes that degrade the extracellular matrix, but expression during and after CPB is unknown.
Methods. Systemic plasma MMP levels were measured in patients (n = 28, 63 ± 1 years) undergoing elective coronary revascularization requiring CPB at baseline, termination of CPB, and 30 minutes, 6 and 24 hours after CPB. Representative classes of MMP species known to degrade matrix and basement membrane components were selected for study. Specifically, the interstitial collagenases MMP-8 and MMP-13, and the gelatinases MMP-2 and MMP-9 were determined by internally validated enzyme-linked immunosorbent assay.
Results. The MMP-8 levels increased by fourfold at separation from CPB, and returned to within normal values within 30 minutes after CPB. The proenzyme forms of MMP-13 and MMP-9 increased by more than twofold at cross-clamp release and returned within normal limits within 6 hours after CPB. The proform of MMP-2 increased from baseline values at 6 and 24 hours postoperatively; likely indicative of de novo synthesis.
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subjects | Aged Anesthesia Anesthesia depending on type of surgery Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy Biological and medical sciences Cardiopulmonary Bypass Coronary Artery Bypass Enzyme Induction - physiology Enzyme-Linked Immunosorbent Assay Female Humans Male Matrix Metalloproteinases - blood Medical sciences Middle Aged Thoracic and cardiovascular surgery. Cardiopulmonary bypass |
title | Cardiopulmonary bypass induces the synthesis and release of matrix metalloproteinases |
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