Intracoronary thrombolysis in evolving myocardial infarction. 1981

W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan

After experimental studies in dogs confirmed the feasibility and safety of rapid intracoronary thrombolysis by local infusion of Thrombolysin (streptokinase and plasmin), intracoronary thrombolysis was attempted in 20 patients with evolving myocardial infarction who were hospitalized within 3 hours from the onset of symptoms during the day and within 2 hours at night. Thrombolysin was infused in the immediate vicinity of the site of coronary occlusion using a 0.85 mm outer diameter catheter advanced through the lumen of the Judkins catheter. Reperfusion was achieved in four patients after an average of 43 minutes of Thrombolysin infusion at a rate of 2000 IU/min and in 15 patients after an average of 21 minutes of Thrombolysin infusion at a rate of 4000 IU/min. The failure to open the artery in one patient may have been caused by our inability to advance the infusion catheter close to the site of occlusion. Rethrombosis occurred in one patient 8 days after reperfusion and 2 days after discontinuation of anticoagulants because of a history of chronic alcoholism. Wall motion and perfusion studies showed improvement following reperfusion. Patency of the artery was achieved an average of 4 hours after the onset of symptoms. The need for earlier reperfusion is emphasized.

UI MeSH Term Description Entries
D008297 Male Males
D009203 Myocardial Infarction NECROSIS of the MYOCARDIUM caused by an obstruction of the blood supply to the heart (CORONARY CIRCULATION). Cardiovascular Stroke,Heart Attack,Myocardial Infarct,Cardiovascular Strokes,Heart Attacks,Infarct, Myocardial,Infarction, Myocardial,Infarctions, Myocardial,Infarcts, Myocardial,Myocardial Infarctions,Myocardial Infarcts,Stroke, Cardiovascular,Strokes, Cardiovascular
D010958 Plasminogen Precursor of plasmin (FIBRINOLYSIN). It is a single-chain beta-globulin of molecular weight 80-90,000 found mostly in association with fibrinogen in plasma; plasminogen activators change it to fibrinolysin. It is used in wound debriding and has been investigated as a thrombolytic agent. Profibrinolysin,Glu-Plasminogen,Glutamic Acid 1-Plasminogen,Glutamyl Plasminogen,1-Plasminogen, Glutamic Acid,Glu Plasminogen,Glutamic Acid 1 Plasminogen,Plasminogen, Glutamyl
D003331 Coronary Vessels The veins and arteries of the HEART. Coronary Arteries,Sinus Node Artery,Coronary Veins,Arteries, Coronary,Arteries, Sinus Node,Artery, Coronary,Artery, Sinus Node,Coronary Artery,Coronary Vein,Coronary Vessel,Sinus Node Arteries,Vein, Coronary,Veins, Coronary,Vessel, Coronary,Vessels, Coronary
D003402 Creatine Kinase A transferase that catalyzes formation of PHOSPHOCREATINE from ATP + CREATINE. The reaction stores ATP energy as phosphocreatine. Three cytoplasmic ISOENZYMES have been identified in human tissues: the MM type from SKELETAL MUSCLE, the MB type from myocardial tissue and the BB type from nervous tissue as well as a mitochondrial isoenzyme. Macro-creatine kinase refers to creatine kinase complexed with other serum proteins. Creatine Phosphokinase,ADP Phosphocreatine Phosphotransferase,ATP Creatine Phosphotransferase,Macro-Creatine Kinase,Creatine Phosphotransferase, ATP,Kinase, Creatine,Macro Creatine Kinase,Phosphocreatine Phosphotransferase, ADP,Phosphokinase, Creatine,Phosphotransferase, ADP Phosphocreatine,Phosphotransferase, ATP Creatine
D004285 Dogs The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065) Canis familiaris,Dog
D005260 Female Females
D005338 Fibrin Fibrinogen Degradation Products Soluble protein fragments formed by the proteolytic action of plasmin on fibrin or fibrinogen. FDP and their complexes profoundly impair the hemostatic process and are a major cause of hemorrhage in intravascular coagulation and fibrinolysis. Antithrombin VI,Fibrin Degradation Product,Fibrin Degradation Products,Fibrin Fibrinogen Split Products,Degradation Product, Fibrin,Degradation Products, Fibrin,Product, Fibrin Degradation
D005340 Fibrinogen Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products. Coagulation Factor I,Factor I,Blood Coagulation Factor I,gamma-Fibrinogen,Factor I, Coagulation,gamma Fibrinogen
D005341 Fibrinolysin A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins. Plasmin,Fibrogammin,Glu-Plasmin,Protease F,Thrombolysin,Glu Plasmin

Related Publications

W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
October 1981, Annals of internal medicine,
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
August 1984, Arquivos brasileiros de cardiologia,
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
November 1983, Schweizerische medizinische Wochenschrift,
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
December 1988, South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde,
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
September 1989, Journal of cardiology,
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
July 1988, Japanese circulation journal,
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
February 1984, Presse medicale (Paris, France : 1983),
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
January 1987, Catheterization and cardiovascular diagnosis,
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
August 1982, Harefuah,
W Ganz, and N Buchbinder, and H Marcus, and A Mondkar, and J Maddahi, and Y Charuzi, and L O'Connor, and W Shell, and M C Fishbein, and R Kass, and A Miyamoto, and H J Swan
December 1982, Nihon Naika Gakkai zasshi. The Journal of the Japanese Society of Internal Medicine,
Copied contents to your clipboard!