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Extracellular matrix degradation via enolase/plasminogen interaction: Evidence for a mechanism conserved in Metazoa
Author(s) -
Grossi Gerarda,
Grimaldi Annalisa,
Cardone Rosa A.,
Monné Magnus,
Reshkin Stephan J.,
Girardello Rossana,
Greco Maria R.,
Coviello Elena,
Laurino Simona,
Falabella Patrizia
Publication year - 2016
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/boc.201500095
Subject(s) - biology , microbiology and biotechnology , enolase , cytoplasm , biochemistry , extracellular matrix , extracellular , immunology , immunohistochemistry
Background Information 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. Significance 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.