SYNEMIN - A NEW HIGH MOLECULAR-WEIGHT PROTEIN ASSOCIATED WITH DESMIN AND VIMENTIN FILAMENTS IN MUSCLE
SYNEMIN - A NEW HIGH MOLECULAR-WEIGHT PROTEIN ASSOCIATED WITH DESMIN AND VIMENTIN FILAMENTS IN MUSCLE
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DOI:
10.1016/0092-8674(80)90549-8
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发表时间:
1980-01-01
期刊:
影响因子:
64.5
通讯作者:
LAZARIDES, E
中科院分区:
文献类型:
--
作者:
GRANGER, BL;LAZARIDES, E
A 230,000 dalton polypeptide co-purifies through cycles of depolymerization and polymerization with intermediate filament subunits, desmin and vimentin, from avian smooth muscle. This protein is present in skeletal muscle and is distinct from myosin and filamin. Double immunofluorescence microscopy of cultured cells, using antisera shown to be specific by immunoautoradiography, revealed that this protein has the same spatial distribution as desmin and vimentin. During skeletal myogenesis, all 3 antigens exist initially in multinucleate myotubes as wavy filaments throughout the cytoplasm. Within a week after myoblast fusion, they begin to coalesce at the peripheries of the myofibril Z discs, attaining the distribution observed in mature muscle, a network of interlinked rings within the Z plane. Treatment of cultured myotubes with colcemide causes the filamentous forms of these 3 proteins to co-aggregate into cytoplasmic bundles, but has little effect on them when they are associated with the Z discs. Extraction of cells with nonionic detergent and high salt leaves cytoskeletons containing desmin, vimentin and the 230,000 dalton polypeptide with immunofluorescent patterns that are indistinguishable from one another. This high MW protein apparently is closely associated with desmin and vimentin filaments in muscle cells. The protein was named synemin, from the Greek meaning with filament.