Ultrastructural localization of proteins involved in sea urchin biomineralization
Ultrastructural localization of proteins involved in sea urchin biomineralization
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DOI：
10.1177/002215549904700911
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发表时间：
1999-09-01
影响因子：
3.2
通讯作者：
Dubois, P
中科院分区：
文献类型：
--
作者：
Ameye, L;Hermann, R;Dubois, P
用三种血清对紫癜圆心棘足蚴胚胎的总矿化有机基质和两种特异性基质蛋白（SM30和SM50）进行免疫标记，对成年棘足蚴的三个骨骼组织（原蒂、试验和牙齿）进行免疫标记。测试了两种常规化学固定方案和两种高压冷冻/冷冻替代方案。常规方案因其能很好地保存超微结构而被推荐，高压冷冻/冷冻替代方案因其能很好地保留抗原性而被推荐。在三个成人组织中获得免疫标记。它局限于活跃的骨骼形成细胞和结构化的有机基质。结果表明，基质蛋白遵循分泌蛋白组装和输出的经典途径，表明SM30和SM50是有机基质在矿化开始前形成的三维网络的一部分。这些结果表明，部分骨形成的遗传程序在不同的钙化模式和发育阶段是保守的。
Three skeletal tissues of the adult echinoid Paracentrotus lividus (the pedicellaria primordium, the test, and the tooth) were immunolabeled with three sera raised against the total mineralization organic matrix and two specific matrix proteins (SM30 and SM50) from the embryo of the echinoid Strongylocentrotus purpuratus. Two conventional chemical fixation protocols and two high-pressure freezing/freeze-substitution protocols were tested. One conventional protocol is recommended for its good preservation of the ultrastructure, and one high-pressure freezing/freeze-substitution protocol is recommended for its good retention of antigenicity. Immunolabeling was obtained in the three adult tissues. It was confined to the active skeleton-forming cells and to the structured organic matrix. The results indicate that the matrix proteins follow the classical routes of secretory protein assembly and export and suggest that SM30 and SM50 are a part of the tridimensional network formed by the organic matrix before the onset of mineralization. They show that the genetic program of part of skeletogenesis is conserved among different calcification models and developmental stages.