BIOLOGICAL ROLE OF INTRACELLULAR CA2+-BINDING PROTEINS

细胞内 CA2 结合蛋白的生物学作用

• 批准号: 3276872
• 负责人: JOHN R DEDMAN
• 金额: $ 12.4万
• 依托单位: UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON
• 依托单位国家: 美国
• 财政年份: 1980
• 资助国家: 美国
• 起止时间: 1980-12-01 至 1988-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3276872
• 关键词: adenosinetriphosphatase; affinity chromatography; antibody formation; cell cycle; cell growth regulation; cell motility; complementary DNA; electron microscopy; fluorescence spectrometry; gel electrophoresis; immunoelectron microscopy; immunofluorescence technique; immunoprecipitation; methylation; microinjections; mitochondria; monoclonal antibody; muscle proteins; radioimmunoassay; radiotracer; saltwater environment; scintillation spectrometry; tissue /cell culture

It is well established that Ca2+ is a pleiotrophic factor affecting a wide variety of essential cellular processes. It is postulated that many of these actions are mediated via calmodulin. In fact, it is felt that the Ca2+ calmodulin complex may represent the active cellular state of Ca2+. Since all cells contain calmodulin and Ca2+, the specificity of Ca2+ calmoduling action in cells is somewhat of an enigma. Our results, as well as published results of others suggests that specificity of Ca2+ action resides in the calmodulin acceptor proteins (CAPs). That is, the response of any particular cell type to elevated Ca2+ levels is dependent upon the class and population of CAPs. These proteins represent a variety of enzymes which are regulated by Ca2+ calmodulin. It is very possible that the CAPs themselves possess enzyme modifying properties (i.e. protein kinase and methylases). The tissue specificity of such a situation would be extended to not only the CAPs, but the presence of CAP protein substrate as well. We propose to continue our purification of CAPs from electroplax and chicken gizzard. These studies include the subunit structure, immunolocalization, and expression during different physiological states in hopes of better understanding their individual functional roles. We have recently discovered several other high-affinity calcium receptor proteins which form calcium induced hydrophobicity. Due to their functional similarity with troponin C and calmodulin we have referred to them as "calcimedins". We now have the ability to purify these proteins in high quantity in order to pursue a complete physicochemical characterization, produce antibodies, develop immunoassays, and study their functional role in cell regulation. Collectively, our studies will provide a better understanding regarding the mediation and selective discrimination of the regulatory intracellular calcium signal.

众所周知，Ca2+ 是一种影响广泛的多效因子。 各种重要的细胞过程。 据推测，许多 这些作用是通过钙调蛋白介导的。 事实上，大家觉得 Ca2+钙调蛋白复合物可能代表Ca2+的活跃细胞状态。 由于所有细胞都含有钙调蛋白和 Ca2+，Ca2+ 的特异性 细胞中的钙调节作用在某种程度上是一个谜。 我们的成果也 其他人发表的结果表明 Ca2+ 作用的特异性 存在于钙调蛋白受体蛋白 (CAP) 中。 也就是说，响应 任何特定细胞类型的 Ca2+ 水平升高取决于 CAP 的类别和群体。 这些蛋白质代表了多种 受Ca2+钙调蛋白调节的酶。 很有可能 CAP 本身具有酶修饰特性（即蛋白质 激酶和甲基化酶）。 这种情况的组织特异性将 不仅可以扩展到 CAP，还可以扩展到 CAP 蛋白底物的存在 以及。 我们建议继续从 electroplax 中纯化 CAP 和鸡胗。 这些研究包括亚基结构、 免疫定位和不同生理状态下的表达 希望更好地了解他们各自的职能角色。 我们最近发现了其他几种高亲和力钙受体 形成钙诱导疏水性的蛋白质。 由于他们的 与我们提到的肌钙蛋白 C 和钙调蛋白的功能相似 它们被称为“钙调素”。 我们现在有能力纯化这些蛋白质 高数量以追求完整的理化 表征、生产抗体、开发免疫测定并研究它们 细胞调节中的功能作用。 总的来说，我们的研究将提供 对调解和选择性歧视有更好的理解 调节细胞内钙信号。