<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Belin, D</dc:creator>
  <dc:creator>Baccino, D</dc:creator>
  <dc:creator>Wohlwend, A</dc:creator>
  <dc:creator>Estreicher, A</dc:creator>
  <dc:creator>Hurate, J</dc:creator>
  <dc:creator>Vassalli, J-D</dc:creator>
  <dc:date>2018</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">&lt;jats:p&gt;Recent cell biological and biochemical studies on the urokinase-type plasminogen activator (u-PA) have revealed an unsuspected property of this protein: it binds with high affinity and specificity to the plasma membrane of a number of cell types. Hence, while the interaction of tissue-type plasminogen activator (t-PA) with fibrin suggests a preferred role for this enzyme in the maintenance of fluidity of the extracellular milieu, the cellular binding of u-PA results in the focalisation of plasmin generation to the close environment of the cell surface; this appears as an optimal configuration if u-PA is to participate in the enzymatic events required for cell migration.&lt;/jats:p&gt;&lt;jats:p&gt;The available information on the cellular binding of u-PA can be summarized as follows:&lt;/jats:p&gt;&lt;jats:p&gt;1. Human monocytes-macrophages, monocyte-like cell lines, fibroblasts, and a variety of other cell lines all express u-PA binding sites. The number of u-PA binding sites on a given cell type may vary as a function of the functional state of the cells. In some cases all sites are occupied by “endogenous” u-PA.&lt;/jats:p&gt;&lt;jats:p&gt;2. Binding does not require u-PA activity, and prou-PA binds with the same affinity as does the active enzyme.&lt;/jats:p&gt;&lt;jats:p&gt;3. The Kd for u-PA binding is between 1 and 10×10-10 M. The binding site appears to be specific for u-PA.&lt;/jats:p&gt;&lt;jats:p&gt;4. Binding requires the presence of the A chain of u-PA; the growth factor module of the A chain is involved in this interaction.&lt;/jats:p&gt;&lt;jats:p&gt;5. Bound enzyme does not dissociate readily, nor is it rapidly endocytosed; most importantly, it retains catalytic activity.&lt;/jats:p&gt;&lt;jats:p&gt;Studies in progress are aimed at further defining the u-PA determinants responsible for binding. In this context it is noteworthy that there is a tight species specificity of binding: human and murine u-PA, for instance, bind only to cells of the homologous species. Characterization of the u-PA binding site suggests that it is an integral membrane protein that includes at least one Mf 50.000 polypeptide chain.&lt;/jats:p&gt;&lt;jats:p&gt;In addition to allowing for the peri-cellular focalisation of u-PA catalysed proteolysis, expression of the u-PA binding site provides a mecanism whereby one cell type can acquire membrane-bound u-PA activity following secretion of the (pro)enzyme by another cell population. A striking example of this is the binding of u-PA, synthesized by the epithelial layer of the male genital tract, to the head region of murine spermatozoa.&lt;/jats:p&gt;</dc:description>
  <dc:identifier>https://sonar.ch/global/documents/54589</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1055/s-0038-1642957</dc:relation>
  <dc:source>XIth International Congress on Thrombosis and Haemostasis. - Schattauer GmbH. - 1987</dc:source>
  <dc:title xmlns:ns1="xml" ns1:lang="en">A CELLULAR RECEPTOR FOR UROKINASE-TYPE PLASMINOGEN ACTIVATOR</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
