Abstract
The matricellular glycoprotein SPARC is composed of three functional domains that are evolutionarily conserved in organisms ranging from nematodes to mammals: a Ca2+-binding glutamic acid-rich acidic domain at the N-terminus (domain I), a follistatin-like module (domain II), and an extracellular Ca2+-binding (EC) module that contains two EF-hands and two collagen-binding epitopes (domain III). We report that four SPARC orthologs (designated nvSPARC1-4) are expressed by the genome of the starlet anemone Nematostella vectensis, a diploblastic basal cnidarian composed of an ectoderm and endoderm separated by collagen-based mesoglea. We also report that domain I is absent from all N. vectensis SPARC orthologs. In situ hybridization data indicate that N. vectensis SPARC mRNAs are restricted to the endoderm during post-gastrula development. The absence of the Ca2+-binding N-terminal domain in cnidarians and conservation of collagen-binding epitopes suggests that SPARC first evolved as a collagen-binding matricellular glycoprotein, an interaction likely to be dependent on the binding of Ca2+-ions to the two EF-hands in the EC domain. We propose that further Ca2+-dependent activities emerged with the acquisition of an acidic N-terminal module in triplobastic organisms.
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Acknowledgments
This work was supported by Discovery grants to B.C., M.R., S.D., and U.T. from National Sciences and Research Council of Canada and an Early Researcher Award to B.C.
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Communicated by M.Q. Martindale
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Koehler, A., Desser, S., Chang, B. et al. Molecular evolution of SPARC: absence of the acidic module and expression in the endoderm of the starlet sea anemone, Nematostella vectensis . Dev Genes Evol 219, 509–521 (2009). https://doi.org/10.1007/s00427-009-0313-9
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DOI: https://doi.org/10.1007/s00427-009-0313-9