
doi: 10.1007/bf01946925
pmid: 7498451
Gastrulation is characterized by dramatic cell migration which is thought to require the interaction of cell adhesion molecules with extracellular molecules. We have tested two novel peptides, a fibronectin peptide and a fibronectin receptor peptide, for their effects on gastrulation of the leopard frog Rana pipiens. The fibronectin peptide DRVPHSRNSIT corresponds to residues 1373-1383 of the cell-binding domain of fibronectin; 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 after being microinjected into mid-blastulae. These results indicate that these sequences may correspond to the ligand/receptor interaction sites of fibronectin and its receptor(s).
Male, Embryo, Nonmammalian, Dose-Response Relationship, Drug, Microinjections, Molecular Sequence Data, Rana pipiens, Gastrula, Peptide Fragments, Fibronectins, Structure-Activity Relationship, Receptors, Fibronectin, Animals, Female, Amino Acid Sequence
Male, Embryo, Nonmammalian, Dose-Response Relationship, Drug, Microinjections, Molecular Sequence Data, Rana pipiens, Gastrula, Peptide Fragments, Fibronectins, Structure-Activity Relationship, Receptors, Fibronectin, Animals, Female, Amino Acid Sequence
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