title: Extracellular matrix degradation via enolase/plasminogen interaction: Evidence for a mechanism conserved in Metazoa.
abstract: BACKGROUND
  While enolase is a ubiquitous metalloenzyme involved in the glycolytic pathway, it is also known as a multifunctional protein, since enolases anchored on the outer surface of the plasma membrane are involved in tissue invasion.
  
  
  RESULTS
  We have identified an extracellular enolase (Ae-ENO) produced by the teratocytes, embryonic cells of the insect parasitoid Aphidius ervi. We demonstrate that Ae-ENO, although lacking a signal peptide, accumulates in cytoplasmic vesicles oriented towards the cell membrane. Ae-ENO binds to and activates a plasminogen-like molecule inducing digestion of the host tissue and thereby ensuring successful parasitism.
  
  
  CONCLUSIONS
  These results support the hypothesis that plasminogen-like proteins exist in invertebrates. Interestingly the activation of a plasminogen-like protein is mediated by a mechanisms involving the surface enolase/fibrinolytic system considered, until now, exclusive of vertebrates, and that instead is conserved across species.
  
  
  CONCLUSIONS
  To our knowledge, this is the first example of enolase mediated Plg-like binding and activation in insect cells, demonstrating the existence of an ECM degradation process via a Plg-like protein in invertebrates.
authors: Department of Sciences, University of Basilicata, Potenza, 85100, Italy.
authors: Gerarda
authors: G
authors: Grossi
authors: Department of Biotechnology and Life Sciences, University of Insubria, Varese, 21100, Italy.
authors: Annalisa
authors: A
authors: Grimaldi
authors: Department of Bioscience, Biotechnologies and Biopharmaceutics, University of Bari, Bari, 70126, Italy.
authors: Rosa A
authors: RA
authors: Cardone
authors: Department of Sciences, University of Basilicata, Potenza, 85100, Italy.
authors: Magnus
authors: M
authors: Monné
authors: Department of Bioscience, Biotechnologies and Biopharmaceutics, University of Bari, Bari, 70126, Italy.
authors: Stephan J
authors: SJ
authors: Reshkin
authors: Department of Biotechnology and Life Sciences, University of Insubria, Varese, 21100, Italy.
authors: Rossana
authors: R
authors: Girardello
authors: Department of Bioscience, Biotechnologies and Biopharmaceutics, University of Bari, Bari, 70126, Italy.
authors: Maria R
authors: MR
authors: Greco
authors: Department of Sciences, University of Basilicata, Potenza, 85100, Italy.
authors: Elena
authors: E
authors: Coviello
authors: Department of Sciences, University of Basilicata, Potenza, 85100, Italy.
authors: Simona
authors: S
authors: Laurino
authors: Department of Sciences, University of Basilicata, Potenza, 85100, Italy.
authors: Patrizia
authors: P
authors: Falabella
mesh_terms: D000818:Animals; D019143:Evolution, Molecular; D005109:Extracellular Matrix / Q000235:genetics / Q000378:metabolism*; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism*; D010751:Phosphopyruvate Hydratase / Q000235:genetics / Q000378:metabolism*; D010958:Plasminogen / Q000235:genetics / Q000378:metabolism*; D014863:Wasps / Q000235:genetics / Q000378:metabolism*
chemical_list: D019476:Insect Proteins; D010958:Plasminogen; D010751:Phosphopyruvate Hydratase
keywords: Enolase; Extracellular matrix digestion; Hymenoptera; Plasminogen; Teratocytes