Collagen metabolism and spicule formation in sea urchin micromeres.
Collagen metabolism and spicule formation in sea urchin micromeres.
复制标题
海胆微粒中的胶原代谢和针状体形成。
DOI：
10.1016/0014-4827(84)90233-7
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发表时间：
1984
影响因子：
3.7
通讯作者：
S. Benson
中科院分区：
文献类型：
--
作者：
J. Blankenship;S. Benson
利用分离的紫球海胆微粒体研究了胶原或胶原样蛋白在海胆胚胎骨骼体外形成中的作用。在含有4%马血清的海水中，在组织培养塑料或I型胶原的细胞外基质上培养微粒。监测了脯氨酸类似物和胶原羟化抑制剂对两种培养系统中体外骨针形成的影响。当微粒在破坏胶原代谢的脯氨酸类似物1-氮杂环丁烷-2-羧酸和1 - 3，4-脱氢脯氨酸的存在下培养时，骨针形成在胶原基质上比在塑料上受到的抑制明显更少。在α，α′-联吡啶（一种胶原羟化抑制剂）存在下，在塑料上培养微粒，几乎完全抑制骨针的形成。α，α′-联吡啶的抑制作用可通过在胶原基质上培养微粒来克服。这些结果不支持胶原是骨针钙化有机基质的观点。相反，他们认为，微粒合成胶原样细胞外基质，这是必要的骨针形成。脯氨酸类似物或胶原加工抑制剂对这种活性的抑制可以通过向细胞提供先前沉积的细胞外基质来克服。
The role of collagen or collagen-like protein(s) in the in vitro formation of the sea urchin embryonic skeleton was investigated using isolated micromeres ofStrongylocentrotus purpuratus. Micromeres were cultured in sea water containing 4% horse serum on tissue culture plastic or an extracellular matrix of type I collagen. The effect of proline analogs and an inhibitor of collagen hydroxylation on in vitro spicule formation in both culture systems was monitored. When micromeres are cultured in the presence of proline analogsl-azetidine-2-carboxylic acid andl-3,4-dehydroproline which disrupt collagen metabolism, spicule formation is significantly less inhibited on a collagen substratum than on plastic. Culturing micromeres on plastic in the presence of α,α′-dipyridyl, an inhibitor of collagen hydroxylation, resulted in almost complete inhibition of spicule formation. The inhibition by α,α′-dipyridyl can be overcome by culturing micromeres on collagen substratum. These results do not support the idea of collagen being the calcified organic matrix of the spicule. Rather, they suggest that micromeres synthesize a collagen-like extracellular matrix which is necessary for spicule formation. Inhibition of this activity by proline analogs or a collagen processing inhibitor can be overcome by providing the cells with a previously deposited extracellular matrix.