The amino acid sequence of the pancreatic islet mitochondrial glycerol phosphate dehydrogenase is not unique and the enzyme is not thyroid or glucose responsive.
The amino acid sequence of the pancreatic islet mitochondrial glycerol phosphate dehydrogenase is not unique and the enzyme is not thyroid or glucose responsive.
复制标题
胰岛线粒体磷酸甘油脱氢酶的氨基酸序列并不独特，并且该酶不具有甲状腺或葡萄糖反应性。
DOI：
10.1006/abbi.1995.1297
复制
发表时间：
1995
影响因子：
3.9
通讯作者：
Simonson,GD
中科院分区：
文献类型：
--
作者：
MacDonald,MJ;Moran,SM;Simonson,GD
线粒体甘油磷酸脱氢酶（mGPD）是胰岛中丰富的几种蛋白质之一。激素和营养的影响赋予这些蛋白质中的许多蛋白质的表达的组织特异性模式，并且这些蛋白质在胰岛中的一级氨基酸序列通常不同于其他组织中的那些。而大鼠胰岛mGPD的氨基酸序列与睾丸和肝脏的相同。(The胰岛mGPD也具有钙调素样钙结合序列。）通过在不同浓度的胰岛素促分泌素、葡萄糖、亮氨酸、谷氨酰胺或琥珀酸甲酯下培养胰岛，没有改变胰岛mGPD活性和蛋白质的量，这些是改变胰岛中其他酶的量的条件。与mGPD活性较低的组织（如肝脏）不同，在甲亢大鼠中或通过向培养的胰岛或大鼠胰岛素瘤细胞中加入T3，未进一步诱导大量的胰岛mGPD。这表明胰岛mGPD与其活性低的组织中的酶处于不同的调节下。
The mitochondrial glycerol phosphate dehydrogenase (mGPD) is one of several proteins that are abundant in the pancreatic islet. Hormonal and nutritional influences confer tissue-specific patterns of expression on many of these proteins and the primary amino acid sequence of these proteins in the islet often differs from those in other tissues. However, the deduced amino acid sequence of the rat islet mGPD was identical to that of testis and liver. (The islet mGPD also possesses calmodulin-like calcium-binding sequences.) Islet mGPD activity and amount of protein were not changed by culturing islets at various concentrations of the insulin secretagogues, glucose, leucine, glutamine, or methyl succinate, which are conditions that alter the amounts of other enzymes in the islet. Unlike mGPD in tissues, such as liver, where mGPD activity is low, the high amount of islet mGPD was not further induced in hyperthyroid rats or by adding T3to cultured islets or rat insulinoma cells. This suggests that the islet mGPD is under different regulation than the enzyme in tissues where its activity is low.