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
Hauptverfasser: Joffs, Cassandra, Gunasinghe, Himali R., Multani, Marlina M., Dorman, B. Hugh, Kratz, John M., Crumbley, A. Jackson, Crawford, Fred A., Spinale, Francis G.
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container_end_page 1523
container_issue 5
container_start_page 1518
container_title The Annals of thoracic surgery
container_volume 71
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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Hugh ; Kratz, John M. ; Crumbley, A. Jackson ; Crawford, Fred A. ; Spinale, Francis G.</creator><creatorcontrib>Joffs, Cassandra ; Gunasinghe, Himali R. ; Multani, Marlina M. ; Dorman, B. Hugh ; Kratz, John M. ; Crumbley, A. Jackson ; Crawford, Fred A. ; Spinale, Francis G.</creatorcontrib><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><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. 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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</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. 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source MEDLINE; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
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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