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J Struct Biol 2013 Aug 01;1832:199-204. doi: 10.1016/j.jsb.2013.04.001.
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SM30 protein function during sea urchin larval spicule formation.

Wilt F , Killian CE , Croker L , Hamilton P .

A central issue in better understanding the process of biomineralization is to elucidate the function of occluded matrix proteins present in mineralized tissues. A potent approach to addressing this issue utilizes specific inhibitors of expression of known genes. Application of antisense oligonucleotides that specifically suppress translation of a given mRNA are capable of causing aberrant biomineralization, thereby revealing, at least in part, a likely function of the protein and gene under investigation. We have applied this approach to study the possible function(s) of the SM30 family of proteins, which are found in spicules, teeth, spines, and tests of Strongylocentrotus purpuratus as well as other euechinoid sea urchins. It is possible using the anti-SM30 morpholino-oligonucleotides (MO''s) to reduce the level of these proteins to very low levels, yet the development of skeletal spicules in the embryo shows little or no aberration. This surprising result requires re-thinking about the role of these, and possibly other occluded matrix proteins.

PubMed ID: 23583702
Article link: J Struct Biol
Grant support: [+]

Genes referenced: LOC100887844
Antibodies: sm30c Ab1
Morpholinos: LOC592088 MO1 sm30a MO1 sm30a MO2 sm30b MO1