1. Effect on collagen metabolism of thrombolytic therapy with tissue-plasminogen activator. A randomized, placebo-controlled study
- Author
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O. G. Larsen, M. B. Stoltenberg, P. Aurup, L. T. Jensen, and N. B. Høst
- Subjects
Adult ,Male ,medicine.medical_specialty ,Adolescent ,medicine.medical_treatment ,Clinical Biochemistry ,Myocardial Infarction ,Placebo-controlled study ,Placebo ,Biochemistry ,Tissue plasminogen activator ,Internal medicine ,medicine ,Humans ,Thrombolytic Therapy ,Myocardial infarction ,Aged ,Chemotherapy ,Activator (genetics) ,business.industry ,General Medicine ,Middle Aged ,medicine.disease ,Peptide Fragments ,Procollagen peptidase ,Tissue Plasminogen Activator ,Cardiology ,Female ,Collagen ,business ,Biomarkers ,Procollagen ,Type I collagen ,medicine.drug - Abstract
This paper assesses alterations in collagen metabolism following thrombolytic therapy of acute myocardial infarction with tissue-plasminogen activator. Sequential serum measurements of the amino-terminal propeptide of type III procollagen (S-PIIINP) and the carboxyterminal propeptide of type I collagen (S-PICP) in patients suspected of acute myocardial infarction randomized to tissue-plasminogen activator or placebo were used. S-PIIINP increased at 3h in patients with acute myocardial infarction treated with tissue-plasminogen activator (P < 0.05). S-PIIINP was higher in patients treated with tissue-plasminogen activator compared with placebo-treated patients at 3 and 6 h (P < 0.05). S-PICP decreased independently of therapy and diagnosis. Tissue-plasminogen activator, therefore, induces breakdown of collagen, some of which is located in the wall of atheromatous arteries. Vascular patency following thrombolytic therapy may partly be mediated by breakdown of thrombogenic collagen in the vessel wall. The findings may suggest a role for S-PIIINP as a non-invasive indicator of the risk of reocclusion.
- Published
- 1995
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