Gastrulation in the sea urchin, Strongylocentrotus purpuratus, is disrupted by the small laminin peptides YIGSR and IKVAV.
Laminin is present on the apical and basolateral sides of epithelial cells of very early sea urchin blastulae. We investigated whether small laminin-peptides, known to have cell binding activities, alter the development of sea urchin embryos. The peptide YIGSR-NH2 (850 microM) and the peptide PA22-2 (5 microM), which contains the peptide sequence IKVAV (Tashiro et al., J. Biol. Chem. 264, 16174, 1989), typically blocked archenteron formation when added to the sea water soon after fertilization. At lower doses, the YIGSR peptide allowed invagination of the archenteron but blocked archenteron extension and differentiation and evagination of the feeding arms. The effect of YIGSR and PA22-2 peptides declined when added to progressively older stages until no effect was seen when added at the mesenchyme blastula stage (24 hours after fertilization). Control peptides GRGDS, YIGSE, and SHA22, a dodeca-peptide with a scrambled IKVAV sequence, had no effect on development. The YIGSK peptide containing a conserved amino acid modification had only a small effect on gastrulation. The results suggest that YIGSR and IKVAV peptides specifically disrupt cell/extracellular matrix interactions required for normal development of the archenteron and feeding arms. Our recent finding that YTGIR is at the cell binding site of the B1 chain of S. purpuratus laminin supports this conclusion. Evidently, laminin or other laminin-like molecules are among the many extracellular matrix components needed for the invagination and extension of the archenteron during the gastrulation movements of these embryos.
Hawkins
R L
RL
Department of Zoology, University of Washington, Seattle 98195-1800, USA.
Fan
J
J
Hille
M B
MB
D000595:Amino Acid Sequence; D000818:Animals; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000187:drug effects / Q000502:physiology*; D005260:Female; D005306:Fertilization; D005775:Gastrula / Q000166:cytology / Q000187:drug effects / Q000502:physiology*; D007700:Kinetics; D007797:Laminin / Q000494:pharmacology*; D008648:Mesoderm / Q000166:cytology / Q000187:drug effects / Q000502:physiology; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology*; D012617:Sea Urchins / Q000196:embryology*; D013329:Structure-Activity Relationship; D013997:Time Factors
D007797:Laminin; D009842:Oligopeptides; D010446:Peptide Fragments; D010455:Peptides; C081571:tyrosyl-isoleucyl-glycyl-seryl-arginine; C083321:isoleucyl-lysyl-valyl-alanyl-valine