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Plasminogen activation in healing human wounds.
Am J Pathol. 1994 Jun; 144(6):1269-80.AJ

Abstract

Tissue injury is followed by formation of a provisional, fibrin-containing matrix. It is later on replaced by granulation tissue. Replacement involves extracellular proteolysis by fibrinolytic enzymes. Plasmin is a fibrinolytic proteinase and is generated from ubiquitous plasminogen by cell-derived urokinase-type (uPA) or tissue-type (tPA) plasminogen activator. To explore the cells and components involved in plasminogen activation, we have performed a combined immunohistological and zymographic study on human skin wounds produced iatrogenically by debridement. The fibrin(ogen)-specific staining indicated the progressive removal of a fibrin-containing provisional matrix. Plasmin(ogen) was present over the entire observation period. It was diffusely distributed and also displayed a conspicuous association with cells of the granulation tissue, in particular with monocytes/macrophages and fibroblasts. Also, uPA was associated with monocytes/macrophages and fibroblasts, whereas the uPA-receptor (uPA-R) was stained in monocytes/macrophages only. The uPA was potentially active as indicated by zymography. No tPA-specific staining was found. The findings point at the importance of monocytes/macrophages and fibroblasts in uPA-mediated plasminogen activation in healing human skin wounds.

Authors+Show Affiliations

Institut für Immunologie und Serologie, Universität Heidelberg, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8203466

Citation

Schäfer, B M., et al. "Plasminogen Activation in Healing Human Wounds." The American Journal of Pathology, vol. 144, no. 6, 1994, pp. 1269-80.
Schäfer BM, Maier K, Eickhoff U, et al. Plasminogen activation in healing human wounds. Am J Pathol. 1994;144(6):1269-80.
Schäfer, B. M., Maier, K., Eickhoff, U., Todd, R. F., & Kramer, M. D. (1994). Plasminogen activation in healing human wounds. The American Journal of Pathology, 144(6), 1269-80.
Schäfer BM, et al. Plasminogen Activation in Healing Human Wounds. Am J Pathol. 1994;144(6):1269-80. PubMed PMID: 8203466.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Plasminogen activation in healing human wounds. AU - Schäfer,B M, AU - Maier,K, AU - Eickhoff,U, AU - Todd,R F, AU - Kramer,M D, PY - 1994/6/1/pubmed PY - 1994/6/1/medline PY - 1994/6/1/entrez SP - 1269 EP - 80 JF - The American journal of pathology JO - Am J Pathol VL - 144 IS - 6 N2 - Tissue injury is followed by formation of a provisional, fibrin-containing matrix. It is later on replaced by granulation tissue. Replacement involves extracellular proteolysis by fibrinolytic enzymes. Plasmin is a fibrinolytic proteinase and is generated from ubiquitous plasminogen by cell-derived urokinase-type (uPA) or tissue-type (tPA) plasminogen activator. To explore the cells and components involved in plasminogen activation, we have performed a combined immunohistological and zymographic study on human skin wounds produced iatrogenically by debridement. The fibrin(ogen)-specific staining indicated the progressive removal of a fibrin-containing provisional matrix. Plasmin(ogen) was present over the entire observation period. It was diffusely distributed and also displayed a conspicuous association with cells of the granulation tissue, in particular with monocytes/macrophages and fibroblasts. Also, uPA was associated with monocytes/macrophages and fibroblasts, whereas the uPA-receptor (uPA-R) was stained in monocytes/macrophages only. The uPA was potentially active as indicated by zymography. No tPA-specific staining was found. The findings point at the importance of monocytes/macrophages and fibroblasts in uPA-mediated plasminogen activation in healing human skin wounds. SN - 0002-9440 UR - https://www.unboundmedicine.com/medline/citation/8203466/Plasminogen_activation_in_healing_human_wounds_ L2 - https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/8203466/ DB - PRIME DP - Unbound Medicine ER -