Expression of spicule matrix protein gene SM30 in embryonic and adult mineralized tissues of sea urchin <i>Hemicentrotus pulcherrimus</i><sup>†</sup>

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公開日
1996-12
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  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1046/j.1440-169x.1996.t01-5-00012.x
公開者
Wiley

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<jats:p>We have isolated a cDNA clone for spicule matrix protein, SM30, from sea urchin <jats:italic>Hemicentrotus pulcherrimus</jats:italic> and have studied the expression of this gene in comparison with that of another spicule matrix protein gene, <jats:italic>SM50</jats:italic>. In cultured micromeres as well as in intact embryos transcripts of <jats:italic>SM30</jats:italic> were first detectable around the onset of spicule formation and rapidly increased with the growth of spicules, which accompanied accumulation of glycosylated SM30 protein(s). When micromeres were cultured in the presence of Zn<jats:sup>2+</jats:sup>, spicule formation and SM30 expression were suppressed, while both events resumed concurrently after the removal of Zn<jats:sup>2+</jats:sup> from the culture medium. Expression of SM50, in contrast, started before the appearance of spicules and was not sensitive to Zn<jats:sup>2+</jats:sup>. Differences were also observed in adult tissues; <jats:italic>SM30</jats:italic> mRNA was detected in spines and tube feet but not in the test, while <jats:italic>SM50</jats:italic> mRNA was apparent in all of these mineralized tissues at similar levels. These results strongly suggest that the <jats:italic>SM30</jats:italic> gene is regulated by a different mechanism to that of the <jats:italic>SM50</jats:italic> gene and that the products of these two genes are differently involved in sea urchin biomineralization. A possible role of SM30 protein in skeleton formation is discussed.</jats:p>

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