Weiss C, Cahill A L, Laslop A, Fischer-Colbrie R, Perlman R L, Winkler H
Department of Pharmacology, University of Innsbruck, Austria.
Neurosci Lett. 1996 Jun 14;211(1):29-32. doi: 10.1016/0304-3940(96)12712-9.
Several constituents of chromaffin granules were quantitatively determined in noradrenaline and adrenaline cells purified from bovine adrenal medulla. As far as secretory peptides are concerned noradrenaline granules contained slightly more secretogranin II, but much less chromogranin A than adrenaline granules. This can be explained by the dependence of the biosynthesis of chromogranin A on corticosteroids. Proteolytic processing of chromogranin A and secretogranin II was higher in noradrenaline cells which was paralleled by a higher content of the prohormone convertase PC2. Noradrenaline granules also contained a higher concentration of the vesicular monoamine transporter (vMAT2). No differences were found for dopamine beta-hydroxylase, prohormone convertase PC1, carboxypeptidase H and synaptophysin. These results indicate that the secretory cocktail of peptides released from these cells differs significantly between adrenaline and noradrenaline storing cells.
对从牛肾上腺髓质纯化的去甲肾上腺素细胞和肾上腺素细胞中嗜铬颗粒的几种成分进行了定量测定。就分泌肽而言,去甲肾上腺素颗粒中分泌粒蛋白II的含量略高,但嗜铬粒蛋白A的含量比肾上腺素颗粒少得多。这可以通过嗜铬粒蛋白A的生物合成对皮质类固醇的依赖性来解释。去甲肾上腺素细胞中嗜铬粒蛋白A和分泌粒蛋白II的蛋白水解加工更高,这与激素原转化酶PC2的含量更高相平行。去甲肾上腺素颗粒中囊泡单胺转运体(vMAT2)的浓度也更高。在多巴胺β-羟化酶、激素原转化酶PC1、羧肽酶H和突触素方面未发现差异。这些结果表明,这些细胞释放的肽分泌混合物在储存肾上腺素和去甲肾上腺素的细胞之间存在显著差异。