SpADAM, a sea urchin ADAM, has conserved structure and expression.
ADAMs are multidomain cell surface proteins that function in receptor-ligand processing, cell adhesion and fusion, and signaling. SpADAM, a single copy sea urchin ADAM gene with a 3072 bp open reading frame, is expressed during embryonic and larval development. The deduced SpADAM protein is 1023 amino acids long and includes all domains characteristic of ADAMs. Northern blots reveal the presence of 4.4 and 2.3 kb SpADAM transcripts throughout development. Predominant SpADAM proteins are 131 and 95 kDa. The deduced primary structure of SpADAM is closely related to vertebrate ADAMs 12, 13, and 19. SpADAM is expressed during cleavage on blastomere surfaces, and later by vegetal plate cells, migrating secondary mesenchyme, skeletogenic mesenchyme, muscles, and neurons within the ciliated band. Apparently, the structure and types of cells in which ADAM 12/13/19 orthologues are expressed are conserved in deuterostomes.
Rise
Matthew
M
Department of Biology, University of Victoria, Victoria, BC, Canada.
Burke
Robert D
RD
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D018507:Gene Expression Regulation, Developmental; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D007814:Larva / Q000254:growth & development / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010802:Phylogeny; D012617:Sea Urchins / Q000235:genetics* / Q000254:growth & development* / Q000378:metabolism
D008565:Membrane Proteins