X. Wang et al., FIBRONECTIN PEPTIDE DRVPHSRNSIT AND FIBRONECTIN RECEPTOR PEPTIDE DLYYLMDL ARREST GASTRULATION OF RANA-PIPIENS, Experientia, 51(11), 1995, pp. 1097-1102
Gastrulation is characterized by dramatic cell migration which is thou
ght to require the interaction of cell adhesion molecules with extrace
llular molecules. We have tested two novel peptides, a fibronectin pep
tide and a fibronectin receptor peptide, for their effects on gastrula
tion of the leopard frog Rana pipiens. The fibronectin peptide DRVPHSR
NSIT corresponds to residues 1373-1383 of the cell-binding domain of f
ibronectin; the receptor peptide DLYYLMDL corresponds to residues 124-
131 of beta 1 subunit of a variety of integrins including alpha 5 beta
1. Either of these peptides significantly inhibited gastrulation afte
r being microinjected into mid-blastulae. These results indicate that
these sequences may correspond to the ligand/receptor interaction site
s of fibronectin and its receptor(s).