Extracellular matrix degradation via enolase/plasminogen interaction: Evidence for a mechanism conserved in Metazoa.
Biol Cell
; 108(6): 161-78, 2016 Jun.
Article
em En
| MEDLINE
| ID: mdl-26847147
ABSTRACT
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.Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfopiruvato Hidratase
/
Plasminogênio
/
Vespas
/
Evolução Molecular
/
Proteínas de Insetos
/
Matriz Extracelular
Limite:
Animals
Idioma:
En
Revista:
Biol Cell
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Itália