title: RFLP Molecular Analysis of the Urokinase-Type Plasminogen Activator Gene.
abstract: Several cell biological studies have shown that the invasiveness of a variety of tumors depend on the regulated expression of proteolytic enzymes that degrade the surrounding extracellular matrix and dissociate cell-cell and/or cell-matrix attachments. One such enzyme, the serine protease urokinase-type plasminogen activator (uPA), converts enzymatically inactive plasminogen into the widely acting protease plasmin, which degrades several extracellular matrix components and also activates proenzyme forms of matrix metalloproteases. Thus, uPA is a central molecule in pericellular proteolysis (1-1). uPA (as well as other factors of the plasminogen activator system, the cell surface-associated uPA receptor [uPAR], and the plasminogen activator inhibitor type-1 [PAI-1]) is an important prognostic factor predicting relapse-free and/or survival in patients with a variety of solid malignant tumors including ovarian cancer; in all cases, high levels of uPA are associated with a poor prognosis (4-6).
authors.affiliation: Klinischer Forschergruppe der Frauenklinik der Technischen Universität München, Muenchen, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Muehlenweg
authors.forename: A
authors.initials: A
authors.lastname: Schnelzer
authors.forename: B
authors.initials: B
authors.lastname: Türkmen
authors.forename: E
authors.initials: E
authors.lastname: Lengyel
authors.forename: U
authors.initials: U
authors.lastname: Reuning
authors.forename: H
authors.initials: H
authors.lastname: Graeff
authors.forename: M
authors.initials: M
authors.lastname: Schmitt
authors.forename: V
authors.initials: V
authors.lastname: Magdolen