<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>Menoud PA</dc:creator>
  <dc:creator>Sappino N</dc:creator>
  <dc:creator>Boudal-Khoshbeen M</dc:creator>
  <dc:creator>Vassalli JD</dc:creator>
  <dc:creator>Sappino AP</dc:creator>
  <dc:date>1996</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">The serpin alpha2-antiplasmin (alpha2-AP) is the major circulating inhibitor of plasmin; it plays a determining role in the regulation of intravascular fibrinolysis, In addition to blood plasma, plasmin formation occurs in various organs where it is thought to fulfill a spectrum of functions not restricted to clot lysis. Alpha2-AP is synthesized by hepatocytes, but other possible sites of production have not been investigated. To explore the potential extravascular contribution of alpha2-AP in the regulation of proteolysis, we have isolated the murine alpha2-AP cDNA and determined its mRNA distribution in adult tissues. In addition to liver, kidneys are major sites of alpha2-AP mRNA accumulation in the mouse. The transcript is present in epithelial cells lining the convoluted portion of proximal tubules, and its accumulation is under androgen control. Human kidneys also contain high levels of alpha2-AP mRNA. Moderate amounts Of alpha2-AP mRNA are detected in other murine tissues such as muscle, intestine, central nervous system, and placenta. Our observations indicate that alpha2-AP can be synthesized in a number of tissues, where it could function as a distal regulator of plasmin-mediated extracellular proteolysis.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/175036</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1172/JCI118694</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/8647939</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>The Journal of clinical investigation. - 1996</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Amino Acid Sequence</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Cattle</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Cloning, Molecular</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Female</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Humans</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Kidney</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Liver</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Male</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Mice</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Mice, Inbred Strains</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Molecular Sequence Data</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Orchiectomy</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Organ Specificity</dc:subject>
  <dc:subject xmlns:ns15="xml" ns15:lang="en">Pregnancy</dc:subject>
  <dc:subject xmlns:ns16="xml" ns16:lang="en">RNA, Messenger</dc:subject>
  <dc:subject xmlns:ns17="xml" ns17:lang="en">Sequence Homology, Amino Acid</dc:subject>
  <dc:subject xmlns:ns18="xml" ns18:lang="en">Tissue Plasminogen Activator</dc:subject>
  <dc:subject xmlns:ns19="xml" ns19:lang="en">Transcription, Genetic</dc:subject>
  <dc:subject xmlns:ns20="xml" ns20:lang="en">Urokinase-Type Plasminogen Activator</dc:subject>
  <dc:subject xmlns:ns21="xml" ns21:lang="en">alpha-2-Antiplasmin</dc:subject>
  <dc:title xmlns:ns22="xml" ns22:lang="en">The kidney is a major site of alpha(2)-antiplasmin production.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
