title: The betaL integrin subunit is necessary for gastrulation in sea urchin embryos.
abstract: Integrins are a family of cell adhesion molecules reported to mediate cellular interactions essential for normal embryonic morphogenesis. Here we describe a beta integrin subunit that is expressed during early embryogenesis in the sea urchin embryo and appears to be necessary for normal development. The deduced amino acid sequence of betaL is similar to vertebrate beta integrin subunits, but is most closely related to the sea urchin betaG subunit. Northern blots show that betaL is expressed at all stages with maximum expression beginning during gastrulation. Immunolocalization and in situ RNA hybridization show that in blastulae betaL is expressed in the blastoderm and by the ring of bottle cells in the vegetal plate during the initial phase of gastrulation. Presumptive secondary mesenchyme cells express high levels of betaL throughout elongation of the archenteron and in the pluteus betaL is expressed by blastocoelar cells, skeletal mesenchyme, and pigment cells. Antibodies and Fab fragments against betaL block spreading of dissociated embryonic cells on RGD (arginine-glycine-aspartate)-containing substrates. Treating embryos with anti-betaL antibodies blocks the initial phase of gastrulation and interferes with the organization of actin filaments. Prior to gastrulation, the antibodies cause thickening of the blastoderm and later in development defects in skeletal patterning result. Probing for antibody in treated embryos indicates that it penetrates the ectoderm to cells within the blastocoel and is actively endocytosed. We propose that betaL forms receptors that bind to RGD-containing ligands and anchors actin filaments. These receptors appear to be essential in several aspects of morphogenesis.
authors.affiliation: Department of Biology, University of Victoria, Victoria, British Columbia, V8W 2Y2, Canada.
authors.forename: M
authors.initials: M
authors.lastname: Marsden
authors.forename: R D
authors.initials: RD
authors.lastname: Burke
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000494:pharmacology; D002448:Cell Adhesion / Q000187:drug effects / Q000502:physiology; D003001:Cloning, Molecular; D047108:Embryonic Development; D005455:Fluorescent Antibody Technique; D005456:Fluorescent Dyes / Q000378:metabolism; D005775:Gastrula / Q000166:cytology*; D018507:Gene Expression Regulation, Developmental / Q000235:genetics; D017403:In Situ Hybridization; D039641:Integrin beta Chains; D016023:Integrins / Q000737:chemistry* / Q000276:immunology; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000502:physiology; D012333:RNA, Messenger / Q000235:genetics; D012617:Sea Urchins / Q000196:embryology*; D017422:Sequence Analysis, DNA
chemical_list: D000906:Antibodies; D005456:Fluorescent Dyes; D039641:Integrin beta Chains; D016023:Integrins; D009842:Oligopeptides; D012333:RNA, Messenger; C115862:integrin betaL, Strongylocentrotus purpuratus; C049554:glycyl-arginyl-glycyl-aspartyl-serine