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首页> 外文期刊>Cell and Tissue Research >Expression of synaptogyrin-1 in T1R2-expressing type II taste cells and type III taste cells of rat circumvallate taste buds
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Expression of synaptogyrin-1 in T1R2-expressing type II taste cells and type III taste cells of rat circumvallate taste buds

机译:突触结合蛋白-1在T1R2表达的大鼠环味味蕾的II型和III型味觉细胞中的表达

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Synaptogyrins are conserved components of the exocytic apparatus and function as regulators of Ca2+-dependent exocytosis. The synaptogyrin family comprises three isoforms: two neuronal (synaptogyrin-1 and -3) and one ubiquitous (synaptogyrin-2) form. Although the expression patterns of the exocytic proteins synaptotagmin-1, SNAP-25, synaptobrevin-2 and synaptophysin have been elucidated in taste buds, the function and expression pattern of synaptogyrin-1 in rat gustatory tissues have not been determined. Therefore, we examined the expression patterns of synaptogyrin-1 and several cell-specific markers of type II and III cells in rat gustatory tissues. Reverse transcription/polymerase chain reaction assays and immunoblot analysis revealed the expression of synaptogyrin-1 mRNA and its protein in circumvallate papillae. In fungiform, foliate and circumvallate papillae, the antibody against synaptogyrin-1 immunolabeled a subset of taste bud cells and intra- and subgemmal nerve processes. Double-labeling experiments revealed the expression of synaptogyrin-1 in most taste cells immunoreactive for aromatic L-amino acid decarboxylase and the neural cell adhesion molecule. A subset of synaptogyrin-1-immunoreactive taste cells also expressed phospholipase Cβ2, gustducin, or sweet taste receptor (T1R2). In addition, most synaptogyrin-1-immunoreactive taste cells expressed synaptobrevin-2. These results suggest that synaptogyrin-1 plays a regulatory role in transmission at the synapses of type III cells and is involved in exocytic function with synaptobrevin-2 in a subset of type II cells in rat taste buds.
机译:突触融合蛋白是胞外装置的保守成分,并起Ca2 +依赖性胞吐作用的调节剂的作用。突触结合蛋白家族包含三种同工型:两种神经元(突触结合蛋白-1和-3)和一种普遍存在的突触结合蛋白(突触融合蛋白-2)。尽管已经在味蕾中阐明了胞外蛋白突触蛋白-1,SNAP-25,突触素-2和突触素的表达模式,但尚未确定突触蛋白-1在大鼠味觉组织中的功能和表达模式。因此,我们检查了大鼠味觉组织中突触结合蛋白1的表达模式以及II型和III型细胞的几种细胞特异性标志物。逆转录/聚合酶链反应分析和免疫印迹分析显示突触蛋白1 mRNA及其蛋白在环乳突乳头中的表达。在真菌状,叶状和环周乳头状结构中,针对突触结合蛋白1的抗体免疫标记了味蕾细胞的一部分,以及胚内和胚下神经突触。双重标记实验揭示了突触融合蛋白-1在大多数对芳香族L-氨基酸脱羧酶和神经细胞粘附分子具有免疫反应性的味觉细胞中的表达。突触结合蛋白-1-免疫反应性味觉细胞的子集也表达磷脂酶Cβ2,gustducin或甜味受体(T1R2)。另外,大多数突触结合蛋白-1-免疫反应性味觉细胞表达突触结合蛋白-2。这些结果表明突触素-1在III型细胞突触的传递中起调节作用,并且在大鼠味蕾的一部分II型细胞中与突触素2的胞外功能有关。

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