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IDENTIFICATION OF CLATHRIN IN GASTRIC PARIETAL CELLS

IDENTIFICATION OF CLATHRIN IN GASTRIC PARIETAL CELLS
胃壁细胞中网格蛋白的鉴定
批准号:
6281220
负责人:
JOHN G FORTE
金额:
$0.42万
依托单位国家:
美国
项目类别:
财政年份:
1998
资助国家:
美国
项目状态:
已结题
起止时间:
1998-03-01 至 1999-02-28

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中文摘要
翻译
胃氧合细胞中H,K-ATPase的转运 在根尖下的管状室和根尖之间 膜以促分泌剂特有的方式出现。潜在的 这一过程的机制在很大程度上尚不清楚。对此的洞察 这一过程可能与心尖循环途径有关。 其他上皮细胞。我们已经从免疫学上确定了重病 含氧细胞管泡上的网状蛋白链。氯氰菊酯是一种 泡囊外壳蛋白已被证明在 质膜和质膜蛋白的内化 在形成跨高尔基网络的运输小泡过程中。 对肾小管上网状蛋白的鉴定很有趣,给出了 典型组装型网壳蛋白涂层的观察 电子显微镜下未见小管泡。因此, 含氧细胞微管囊泡蛋白可能代表一种新的异构体 网状蛋白。这种异构体可以以不同的方式组装,从而 在形态不清的泡状被毛中。或者,其他 调节分子筛组装的外壳蛋白,如分子筛光 链和网状蛋白接头复合体可能是独特的异构体。因此, 以帮助分子表征化合物的组成 含络合蛋白的管泡状被膜,我们建议获得多肽 利用质谱学从胰蛋白酶多肽中提取序列。细菌的蛋白质 兴趣包括:分子筛重链、分子筛轻链和 笼状蛋白适配器。多肽序列将立即提供 感兴趣的蛋白质的特征。此外,他们还可以 用于产生抗肽抗体和寡核苷酸探针 用于感兴趣的蛋白质的分子克隆。
英文摘要
In gastric oxyntic cells, the trafficking of the H,K-ATPase between a subapical tubulovesicular compartment and the apical membrane occurs in a secretagogue-specific manner. The underlying mechanism of this process is largely uncharacterized. Insight in this process is likely to be relevant to the apical recycling pathway of other epithelial cells. We have immunologically identified the heavy chain of clathrin on oxyntic cell tubulovesicles. Clathrin is a vesicular coat protein that has been demonstrated to play a role in the internalization of membrane proteins from the plasma membrane and in the formation of transport vesicles from the trans-Golgi network. The identification of clathrin on tubulovesicles is intriguing, given the observation that typical assembled clathrin coats on tubulovesicles have not been observed by electron microscopy. Thus, oxyntic cell tubulovesicular clathrin may represent a novel isoform of clathrin. This isoform may assemble in a different manner resulting in a morphologically indistinct vesicular coat. Alternatively, other coat proteins modulating clathrin assembly, such as clathrin light chains and clathrin adaptor complexes, may be unique isoforms. Thus, to aid in the molecular characterization of the components of the clathrin-containing tubulovesicular coat, we propose to obtain peptide sequences from tryptic peptides by mass spectrometry. The proteins of interest include: clathrin heavy chain, clathrin light chain, and clathrin adaptors. The peptide sequences will provide immediate characterization of the proteins of interest. In addition, they may be used to generate anti-peptide antibodies and oligonucleotide probes for molecular cloning of the proteins of interest.
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TOPOLOGICAL ORGANIZATION OF GASTRIC H,K ATPASE
TOPOLOGICAL ORGANIZATION OF GASTRIC H,K ATPASE
TOPOLOGICAL ORGANIZATION OF GASTRIC H,K ATPASE
TOPOLOGICAL ORGANIZATION OF GASTRIC H,K ATPASE
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