Distinct systemic distribution of salusin-α and salusin-β in the rat
Distinct systemic distribution of salusin-α and salusin-β in the rat
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DOI：
10.1016/j.peptides.2010.12.012
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发表时间：
2011-04-01
期刊：
影响因子：
3
通讯作者：
Hirata, Yukio
中科院分区：
文献类型：
--
作者：
Suzuki, Noriko;Shichiri, Masayoshi;Hirata, Yukio
Salusin-α和Salusin-beta是最初在电子分析中预测的多功能生物活性多肽。这些多肽应该同时从人体内的Prosalusin生物合成。然而，关于Salusin-α和salusin-beta在非人类物种中的生物合成和存在方式的信息还很少。在目前的研究中，我们检查了Salusin-α和salusin-beta在大鼠体内是否保守，以及salusin-α和salusin-beta是否允许不同的全身分布。用一种特定的抗大鼠Salusin-α抗体对大鼠组织进行免疫组织化学分析，发现免疫反应广泛存在于神经细胞和纤维中，并在整个器官的上皮组织中大量存在。这一分布与salusin-beta的分布形成鲜明对比。它主要定位于神经内分泌和造血系统。大鼠脾提取液的Western印迹分析表明，存在与大鼠Salusin-α相对应的切割片段。反相和凝胶过滤高效液相色谱分析与放射免疫分析相结合的大鼠尿提取物的检测显示，一个主要的免疫活性成分与合成的大鼠Salusin-beta共洗脱。这些数据支持将大鼠prosalusin加工成salusin-α和salusin-beta，尽管两者之间缺少二碱性氨基酸。(C)2010 Elsevier Inc.保留所有权利。
Salusin-alpha and salusin-beta are multifunctional bioactive peptides that were initially predicted using in silico analyses. These peptides should be concomitantly biosynthesized from prosalusin in humans. However, little information is available yet on the biosynthesis and mode of presence of salusin-alpha and salusin-beta in non-human species. In the present study, we examined whether salusin-alpha and salusin-beta are conserved in the rat and whether salusin-alpha and salusin-beta allow distinct systemic distributions. Immunohistochemical analysis of rat tissues using a specific anti-rat salusin-alpha antibody detected immunoreactivity extensively in neuronal cells and fibers, and abundantly in the epithelial tissues throughout the organs. This distribution contrasts sharply with that of salusin-beta. which is mainly localized to the neuroendocrine and hematopoietic systems. Western blot analysis of rat spleen extracts showed the presence of cleaved fragments corresponding to putative rat salusin-alpha. Reverse-phase and gel filtration high performance liquid chromatography analyses coupled with radioimmunoassay detection of rat urine extracts revealed a major immunoreactive component that co-eluted with synthetic putative rat salusin-beta. These data support the processing of rat prosalusin into salusin-alpha and salusin-beta despite absent dibasic amino acids between the two. (C) 2010 Elsevier Inc. All rights reserved.