title: From plasminogen to plasmin: role of plasminogen receptors in human cancer.
abstract: Cell surface-associated proteolysis mediated by plasmin (PLA) is an essential feature of wound healing, angiogenesis and cell invasion, processes that are dysregulated in cancer development, progression and systemic spread. The generation of PLA, initiated by the binding of its precursor plasminogen (PLG) to the cell surface, is regulated by an array of activators, inhibitors and receptors. In this review, we will highlight the importance of the best-characterized components of the PLG/PLA cascade in the pathogenesis of cancer focusing on the role of the cell surface-PLG receptors (PLG-R). PLG-R overexpression has been associated with poor prognosis of cancer patients and resistance to chemotherapy. We will also discuss recent findings on the molecular mechanisms regulating cell surface expression and distribution of PLG-R.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany. miroslava.didiasova@biochemie.med.uni-giessen.de.
authors.forename: Miroslava
authors.initials: M
authors.lastname: Didiasova
authors.affiliation: Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany. lukasz.wujak@mpi-bn.mpg.de.
authors.forename: Lukasz
authors.initials: L
authors.lastname: Wujak
authors.affiliation: Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany. malgorzata.wygrecka@innere.med.uni-giessen.de.
authors.forename: Malgorzata
authors.initials: M
authors.lastname: Wygrecka
authors.affiliation: Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany. dariusz.zakrzewicz@innere.med.uni-giessen.de.
authors.forename: Dariusz
authors.initials: D
authors.lastname: Zakrzewicz
mesh_terms: D000199:Actins / Q000235:genetics / Q000378:metabolism; D000818:Animals; D017306:Annexin A2 / Q000235:genetics / Q000378:metabolism; D014408:Biomarkers, Tumor / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D005341:Fibrinolysin / Q000378:metabolism*; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D053533:Keratin-8 / Q000235:genetics / Q000378:metabolism; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D010751:Phosphopyruvate Hydratase / Q000235:genetics / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism*; D021381:Protein Transport; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism; D025521:Tumor Suppressor Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D000199:Actins; D017306:Annexin A2; D014408:Biomarkers, Tumor; D004268:DNA-Binding Proteins; D053533:Keratin-8; D011956:Receptors, Cell Surface; D025521:Tumor Suppressor Proteins; D010958:Plasminogen; D005341:Fibrinolysin; C095157:ENO1 protein, human; D010751:Phosphopyruvate Hydratase