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Biochem J
1994 Dec 15;304 ( Pt 3):911-6. doi: 10.1042/bj3040911.
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Identification and partial sequence analysis of novel annexins in Lytechinus pictus oocytes.
Shen WJ
,
Avery J
,
Totty NF
,
Hsuan JJ
,
Whitaker M
,
Moss SE
.
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The annexins are a major class of calcium-binding proteins with unknown functions. In an attempt to define novel model systems in which to study members of the annexin family, we have investigated the expression of annexins in eggs from the sea urchin Lytechinus pictus. Western blot analysis of L. pictus eggs using antisera raised against human annexins I, V and VI revealed the presence of immunoreactive proteins of approximately 34 kDa, 35 kDa and 68 kDa respectively. The sea urchin annexins behaved similarly to their mammalian counterparts, both during purification and in their ability to bind calcium-dependently to anionic phospholipids. Of the three sea urchin annexins, the 34 kDa form was most abundant, yielding sufficient quantities for peptide microsequencing. The amino acid sequences derived in this way showed the L. pictus annexin to be closely related both to mammalian annexin I and to annexins IX, X and XII from Drosophila and Hydra. However, N-terminal sequence from the L. pictus annexin showed it to be a novel member of the annexin super-gene family. The results are interesting in view of the complex evolution of the annexin gene family, and also point to the potential usefulness of echinoderm eggs as a model system in which to study annexin function.
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