Desmin: molecular interactions and putative functions of the muscle intermediate filament protein
Desmin: molecular interactions and putative functions of the muscle intermediate filament protein
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DOI：
10.1590/s0100-879x2004001200007
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发表时间：
2004-12-01
影响因子：
2.3
通讯作者：
Mermelstein, C.S.
中科院分区：
文献类型：
--
作者：
Costa, M.L.;Escaleira, R.;Mermelstein, C.S.
结蛋白是仅在肌肉和内皮细胞中存在的中间丝（IF）蛋白。除了普遍存在的核纤层蛋白外，肌肉中还有其他IF蛋白，如巢蛋白、外周蛋白和波形蛋白，但它们不是肌肉所特有的。结蛋白在1977年被纯化，结蛋白基因在1989年被表征，并且在1996年产生敲除动物。已经描述了几种同种型。结蛋白IF存在于整个平滑肌、心肌和骨骼肌细胞中，但可以更集中于一些特定的结构中，例如致密体、核周围、Z线周围或肋肌中。结蛋白在肌肉来源的细胞适应中上调，包括心脏中的传导纤维、电器官、一些肌病以及用诱导肌肉变性的药物（如佛波醇酯）进行的实验性治疗。已经报道了许多分子与结蛋白相关，例如其他IF蛋白（包括膜肌营养不良蛋白聚糖复合物的成员）、星云蛋白、肌动蛋白和微管蛋白结合蛋白质类凝集素、分子运动动力蛋白、基因调节蛋白MyoD、DNA、伴侣蛋白α B-晶状体蛋白和蛋白酶如钙蛋白酶和半胱天冬酶。结蛋白具有重要的医学作用，因为它被用作肿瘤起源的标志物。最近，已经描述了几种肌病，具有结蛋白沉积物的积累。然而，在其被发现近30年后，结蛋白的功能仍然不清楚。建议的功能包括肌原纤维形成，肌肉的机械支持，线粒体定位，基因表达调控和细胞内信号。本文综述了结蛋白的生物化学相互作用，并讨论了其可能的功能。
Desmin is the intermediate filament (IF) protein occurring exclusively in muscle and endothelial cells. There are other IF proteins in muscle such as nestin, peripherin, and vimentin, besides the ubiquitous lamins, but they are not unique to muscle. Desmin was purified in 1977, the desmin gene was characterized in 1989, and knock-out animals were generated in 1996. Several isoforms have been described. Desmin IFs are present throughout smooth, cardiac and skeletal muscle cells, but can be more concentrated in some particular structures, such as dense bodies, around the nuclei, around the Z-line or in costameres. Desmin is up-regulated in muscle-derived cellular adaptations, including conductive fibers in the heart, electric organs, some myopathies, and experimental treatments with drugs that induce muscle degeneration, like phorbol esters. Many molecules have been reported to associate with desmin, such as other IF proteins (including members of the membrane dystroglycan complex), nebulin, the actin and tubulin binding protein plectin, the molecular motor dynein, the gene regulatory protein MyoD, DNA, the chaperone alphaB-crystallin, and proteases such as calpain and caspase. Desmin has an important medical role, since it is used as a marker of tumors' origin. More recently, several myopathies have been described, with accumulation of desmin deposits. Yet, after almost 30 years since its identification, the function of desmin is still unclear. Suggested functions include myofibrillogenesis, mechanical support for the muscle, mitochondrial localization, gene expression regulation, and intracellular signaling. This review focuses on the biochemical interactions of desmin, with a discussion of its putative functions.