APPEARANCE OF THE MYOFIBROBLASTIC PHENOTYPE IN DUPUYTRENS DISEASE IS ASSOCIATED WITH A FIBRONECTIN, LAMININ, COLLAGEN TYPE-IV AND TENASCIN EXTRACELLULAR-MATRIX
APPEARANCE OF THE MYOFIBROBLASTIC PHENOTYPE IN DUPUYTRENS DISEASE IS ASSOCIATED WITH A FIBRONECTIN, LAMININ, COLLAGEN TYPE-IV AND TENASCIN EXTRACELLULAR-MATRIX
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DOI：
10.1159/000163879
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发表时间：
1994-03-01
期刊：
影响因子：
5
通讯作者：
TAUCHMANN, V
中科院分区：
文献类型：
--
作者：
BERNDT, A;KOSMEHL, H;TAUCHMANN, V
掌腱膜挛缩症的增殖性结节在电子显微镜下的特征是存在具有基底层样物质的肌成纤维细胞。正如文献报道的，免疫组织化学研究显示了纤连蛋白基质，但未能证明层粘连蛋白。电子显微镜特征和免疫组织化学结果之间的这种差异促使我们检查细胞外基质（纤连蛋白、层粘连蛋白、IV 型胶原蛋白和生腱蛋白）的组成与来自 13 个结节性手掌纤维瘤病（掌腱膜挛缩症）天然手术标本的增殖结节中肌成纤维细胞表型的关系。纤连蛋白的免疫组织化学染色在整个手掌腱膜内呈阳性，并且在增殖区域尤其强烈，而层粘连蛋白、IV型胶原和腱蛋白标记仅限于α-平滑肌肌动蛋白阳性增殖结节。为了明确排除非特异性层粘连蛋白标记，进行了 SDS-PAGE 和免疫印迹。掌腱膜挛缩症组织的电泳图显示层粘连蛋白，并且与用作阳性对照的人胎盘组织一致。结果证实了肌成纤维细胞形成了以纤连蛋白、层粘连蛋白、IV 型胶原蛋白和腱蛋白为成分的细胞外基质。因此，层粘连蛋白表达不再被认为是肌成纤维细胞和平滑肌细胞之间的区别特征。
The proliferative nodules of Dupuytren's disease are electron microscopically characterized by the occurrence of myofibroblasts with a basal lamina-like material. As reported in the literature, immunohistochemical investigations showed a fibronectin matrix but failed to demonstrate laminin. This discrepancy between electron microscopic features and immunohistochemical findings prompted us to examine the composition of extracellular matrix (fibronectin, laminin, collagen type IV and tenascin) in relation to the myofibroblast phenotype in proliferative nodules from 13 native surgical specimens of nodular palmar fibromatosis (Dupuytren's disease). The immunohistochemical staining for fibronectin was positive within the whole palmar aponeurosis and was particularly intense in the proliferative areas, whereas laminin, collagen type IV and tenascin labelling was restricted to the alpha-smooth muscle actin-positive proliferative nodules. To exclude definitively an unspecific laminin labelling, SDS-PAGE and immunoblot were performed. The electrophoretic pattern of Dupuytren's disease tissue revealed laminin and was in congruence with human placental tissue used as positive control. The results substantiate an extracellular matrix formation by myofibroblasts with fibronectin, laminin, collagen type IV and tenascin as constituents. Therefore, laminin expression can no longer be considered to be a distinguishing feature between myofibroblasts and smooth muscle cells.