Fibronectin-derived fragments as inducers of adhesion and chemotaxis of Entamoeba histolytica trophozoites.
Active migration of Entamoeba histolytica trophozoites through extracellular matrixes might play a role in host tissue destruction. Trophozoites degrade soluble fibronectin (FN) bound to their surface and adhere to substrate-bound FN, producing local degradation. FN proteolytic fragments were used to determine the nature of adhesion and motility-promoting domains within the protein. The 70-kDa fragment (amino-terminal end) promoted the highest adhesion, followed by the 120-kDa fragment, which contains the cell-binding domain. The 25-kDa fragment (carboxy-terminal end of the A chain) promoted half the adhesion, while two Hep II-binding fragments had no effect. The 70- and 120-kDa fragments also stimulated directed migration and chemokinesis. Intact FN and the 25-kDa fragment showed lower stimulation. The Hep II-binding fragments had no activity. Results support previous evidence for distinct cell-surface components as mediators of adhesion to FN and trophozoite motility and the potential importance of cell matrix recognition and degradation in their invasive behavior.
Franco
E
E
Departamento de Biología Celular, Centro de Investigación y de Estudios Avanzados del I.P.N., Mexico City, Mexico.
Vázquez-Prado
J
J
Meza
I
I
D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D002448:Cell Adhesion; D002633:Chemotaxis; D004748:Entamoeba histolytica / Q000378:metabolism / Q000472:pathogenicity / Q000502:physiology*; D005109:Extracellular Matrix / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011485:Protein Binding
D005353:Fibronectins; D010446:Peptide Fragments; D002403:Cathepsins