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首页> 外文期刊>American Journal of Physiology >Muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs. muscle cells.
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Muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs. muscle cells.

机译：小窝同工型的肌肉特异性相互作用：成纤维细胞与肌肉细胞中小窝之间的差异复合物形成。

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It is generally well accepted that caveolin-3 expression is muscle specific, whereas caveolin-1 and -2 are coexpressed in a variety of cell types, including adipocytes, endothelial cells, epithelial cells, and fibroblasts. Caveolin-1 and -2 are known to form functional hetero-oligomeric complexes in cells where they are coexpressed, whereas caveolin-3 forms homo-oligomeric high molecular mass complexes. Although caveolin-2 might be expected to interact in a similar manner with caveolin-3, most studies indicate that this is not the case. However, this view has recently been challenged as it has been demonstrated that caveolin-2 and -3 are coexpressed in primary cultures of cardiac myocytes, where these two proteins can be coimmunoprecipitated. Thus it remains controversial whether caveolin-2 interacts with caveolin-3. Here, we directly address the issue of caveolin isoform protein-protein interactions by means of three distinct molecular genetic approaches. First, using caveolin-1-deficient mouse embryonic fibroblasts, in which we have stably expressed caveolin-1, -2, or -3, we find that caveolin-1 interacts with caveolin-2 in this setting, whereas caveolin-3 does not, in agreement with most published observations. Next, we used a transfected L6 myoblast cell system expressing all three caveolin proteins. Surprisingly, we found that caveolin-1, -2, and -3 all coimmunoprecipitate in this cell type, suggesting that this interaction is muscle cell specific. Similar results were obtained when the skeletal muscle of caveolin-1 transgenic animals was analyzed for caveolin-1 and caveolin-3 coimmunoprecipitation. Thus we conclude that all three caveolins can interact to form a discrete hetero-oligomeric complex, but that such complex formation is clearly muscle specific.
机译：众所周知，caveolin-3表达是肌肉特异性的，而caveolin-1和-2在多种细胞类型中共表达，包括脂肪细胞，内皮细胞，上皮细胞和成纤维细胞。已知caveolin-1和-2在它们共表达的细胞中形成功能性异寡聚复合物，而caveolin-3形成均寡聚高分子复合物。尽管可以预期小窝蛋白2与小窝蛋白3的相互作用方式类似，但大多数研究表明事实并非如此。然而，这种观点最近受到了挑战，因为已经证明caveolin-2和-3在心肌细胞的原代培养物中共表达，在这两种培养物中可以将这两种蛋白共免疫沉淀。因此，caveolin-2是否与caveolin-3相互作用仍存在争议。在这里，我们通过三种不同的分子遗传学方法直接解决小窝蛋白同工型蛋白-蛋白相互作用的问题。首先，使用缺乏caveolin-1的小鼠胚胎成纤维细胞（其中我们稳定表达了caveolin-1，-2或-3），我们发现caveolin-1在这种情况下与caveolin-2相互作用，而caveolin-3却没有。 ，与大多数已发表的观察结果一致。接下来，我们使用了表达所有三种小窝蛋白的转染L6成肌细胞系统。出人意料的是，我们发现小窝蛋白-1，-2和-3在这种细胞类型中都共免疫沉淀，表明这种相互作用是肌肉细胞特异性的。当对caveolin-1转基因动物的骨骼肌进行caveolin-1和caveolin-3共免疫沉淀分析时，获得了相似的结果。因此，我们得出结论，所有三种小孔蛋白都可以相互作用形成离散的异寡聚复合物，但是这种复合物的形成显然是特定于肌肉的。

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