Structure and developmental expression of a sea urchin fibrillar collagen gene

M. D'Alessio, F. Ramirez, H. R. Suzuki, M. Solursh, R. Gambino

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


We have isolated and characterized cDNA and genomic clones that specify a Paracentrotus lividus procollagen chain. The cDNAs code for 160 uninterrupted Gly-Xaa-Yaa triplets and a 252-amino acid carboxyl propeptide. Analysis of the deduced amino acid sequences indicated that the sea urchin polypeptide exhibits structural features that are characteristic of the fibril-forming class of collagen molecules. Partial characterization of two genomic recombinants revealed that the 30 end of the echinoid gene displays a complex organization that closely resembles that of a prototypical vertebrate fibrillar collagen gene. In situ and Northern (RNA) blot hybridizations established the size, time of appearance, and tissue distribution of the collagen transcripts in the developing sea urching embryo. Collagen mRNA, ~ 6 kilobases in size, is first detected in the forming primary mesenchyme cells of late blastulae where it progressively accumulates until the free swimming/feeding pluteus larval stage. Interestingly, collagen transcripts are also detected in the forming secondary mesenchyme cells of late gastrulae, and by the prism stage, their derivatives appear to be the most intensively labeled cells.

Original languageEnglish
Pages (from-to)9303-9307
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number23
StatePublished - 1989
Externally publishedYes


  • gene evolution
  • invertebrate collagens
  • mesenchyme lineage
  • skeletogenesis


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