Calcitonin, prostaglandin E2, and dibutyryl cyclic adenosine 3',5'-monophosphate disperse the specific microfilament structure in resorbing osteoclasts.
Calcitonin, prostaglandin E2, and dibutyryl cyclic adenosine 3',5'-monophosphate disperse the specific microfilament structure in resorbing osteoclasts.
复制标题
降钙素、前列腺素 E2 和二丁酰环腺苷 3,5-一磷酸分散吸收破骨细胞中的特定微丝结构。
DOI：
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发表时间：
1990
影响因子：
3.2
通讯作者：
Vaananen
中科院分区：
文献类型：
--
作者：
Paivi;Lakkakorpi;H.;Kalervo;Vaananen
Bone resorbing osteoclasts form a specific microfilament structure at the attachment area, in which vinculin and talin appear as a double-circle structure and F-actin fills the space between these circles. This distribution of microfilaments is associated with the resorption lacunae, and F-actin, vinculin, and talin zones correspond roughly to the edges of the lacunae. In the present work, we examined by immunofluorescence the effects of calcitonin (CT) and prostaglandin E2 (PGE2), inhibitors of osteoclastic activity, as well as dibutyryl cyclic AMP (Bt2cAMP) and cytochalasin B, on the microfilament organization in resorbing osteoclasts. CT, PGE2, and Bt2cAMP rapidly dispersed the specific microfilament structure in resorbing osteoclasts. All microfilament proteins studied (vinculin, talin, and F-actin) spread to the central areas of the original circles. The effect of CT was dose dependent. The effects of CT and PGE2 could be reversed, but recovery was slower after CT treatment than after PGE2 treatment. Cytochalasin B entirely destroyed the F-actin organization but only partially the vinculin organization. The results suggest that one structural change leading to the inactivation of the osteoclasts caused by CT and PGE2 is the disintegration of the microfilament structure at the attachment area of resorbing osteoclasts.
