Are beta 1 integrins involved in Xenopus gastrulation?
The molecular basis of vertebrate gastrulation is poorly understood. Work on urodele amphibians has implicated beta 1-containing integrins, but the limited information available for Xenopus indicates otherwise: peptides containing the RGD sequence do not inhibit gastrulation and induction of cell spreading in presumptive ectodermal cells by activin is not accompanied by an increase in synthesis of integrin beta 1. Here we report that beta 1-containing integrins are, nevertheless, the principal fibronectin receptors in the Xenopus gastrula, although their cell surface levels are low. Antibodies recognizing the external domain of the molecule can, unlike peptides containing the RGD site, block gastrulation when introduced into the blastocoel. These results allow us to propose a model to explain the role of integrin beta 1 in Xenopus gastrulation.
Howard
J E
JE
Laboratory of Developmental Biology, National Institute for Medical Research, London, UK.
Hirst
E M
EM
Smith
J C
JC
D028341:Activins; D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000276:immunology; D001755:Blastocyst / Q000187:drug effects; D005314:Embryonic and Fetal Development / Q000502:physiology*; D005775:Gastrula / Q000502:physiology*; D007265:Inhibins / Q000494:pharmacology; D019012:Integrin beta1; D016023:Integrins / Q000096:biosynthesis / Q000276:immunology / Q000502:physiology*; D008969:Molecular Sequence Data; D009842:Oligopeptides; D017469:Receptors, Fibronectin / Q000096:biosynthesis / Q000276:immunology / Q000502:physiology*; D014982:Xenopus laevis / Q000196:embryology*
D000906:Antibodies; D019012:Integrin beta1; D016023:Integrins; D009842:Oligopeptides; D017469:Receptors, Fibronectin; D028341:Activins; D007265:Inhibins; C047981:arginyl-glycyl-aspartic acid