Document Detail

Fibrinolysis-inhibitory capacity of clot-embedded surfactant is enhanced by SP-B and SP-C.
MedLine Citation:
PMID:  12388357     Owner:  NLM     Status:  MEDLINE    
Incorporation of pulmonary surfactant into fibrin inhibits its plasmic degradation. In the present study we investigated the influence of surfactant proteins (SP)-A, SP-B, and SP-C on the fibrinolysis-inhibitory capacity of surfactant phospholipids. Plasmin-induced fibrinolysis was quantified by means of a (125)I-fibrin plate assay, and surfactant incorporation into polymerizing fibrin was analyzed by measuring the incorporation of (3)H-labeled L-alpha-dipalmitoylphosphatidylcholine into the insoluble clot material. Incorporation of a calf lung surfactant extract (Alveofact) and an organic extract of natural rabbit large surfactant aggregates (LSA) into a fibrin clot revealed a stronger inhibitory effect on plasmic cleavage of this clot than a synthetic phospholipid mixture (PLX) and unprocessed LSA. Reconstitution of PLX with SP-B and SP-C increased, whereas reconstitution with SP-A decreased, the fibrinolysis-inhibitory capacity of the phospholipids. The SP-B effect was paralleled by an increased incorporation of phospholipids into fibrin. We conclude that the inhibitory effect of surfactant incorporation into polymerizing fibrin on its susceptibility to plasmic cleavage is enhanced by SP-B and SP-C but reduced by SP-A. In the case of SP-B, increased phospholipid incorporation may underlie this finding.
Philipp Markart; Clemens Ruppert; Friedrich Grimminger; Werner Seeger; Andreas Günther
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2002-09-06
Journal Detail:
Title:  American journal of physiology. Lung cellular and molecular physiology     Volume:  284     ISSN:  1040-0605     ISO Abbreviation:  Am. J. Physiol. Lung Cell Mol. Physiol.     Publication Date:  2003 Jan 
Date Detail:
Created Date:  2002-12-09     Completed Date:  2003-01-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  100901229     Medline TA:  Am J Physiol Lung Cell Mol Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  L69-76     Citation Subset:  IM    
Department of Internal Medicine, Justus-Liebig-University-Giessen, Klinikstrasse 36, D-35385 Giessen, Germany.
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MeSH Terms
Blood Coagulation / physiology*
Drug Combinations
Fibrin / metabolism
Fibrinolysis / drug effects,  physiology*
Lipids / pharmacology
Phospholipids / metabolism,  pharmacology
Pulmonary Surfactant-Associated Protein B / pharmacology,  physiology*
Pulmonary Surfactant-Associated Protein C / pharmacology,  physiology*
Pulmonary Surfactants / metabolism*,  pharmacology
Reg. No./Substance:
0/Drug Combinations; 0/Lipids; 0/Phospholipids; 0/Pulmonary Surfactant-Associated Protein B; 0/Pulmonary Surfactant-Associated Protein C; 0/Pulmonary Surfactants; 0/SF-RI 1, bovine surfactant preparation; 9001-31-4/Fibrin

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