A proposed structure of chondroitin 6-sulfate proteoglycan of human normal and adjacent atherosclerotic plaque.

A proposed structure of chondroitin 6-sulfate proteoglycan of human normal and adjacent atherosclerotic plaque.
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人类正常和邻近动脉粥样硬化斑块的软骨素 6-硫酸盐蛋白多糖的拟议结构。

DOI:
10.1161/01.atv.6.4.407
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发表时间:
1986
期刊:
Arteriosclerosis (Dallas, Tex.)
影响因子:
--
通讯作者:
Rowe,HA
Rowe,HA
中科院分区:
--
文献类型:
--
作者:
Wagner,WD;Salisbury,GJ;Rowe,HA

文献摘要

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硫酸软骨素蛋白聚糖单体是从大体正常的人主动脉和邻近的脂肪纤维动脉粥样硬化斑块的内膜中层切碎物中制备的。从正常主动脉的单体制备的糖胺聚糖链在Ultrogel ACA 54上显示正态分布,Kav为0.48,而动脉粥样硬化主动脉的糖胺聚糖链显示双峰分布(主峰,Kav 0.35;次峰,Kav 0.70)。正常主动脉糖胺聚糖的Mr估计为1.5 × 10(4)。对于动脉粥样硬化主动脉,大多数链为2.0 × 10(4),而较小的群体为1.2 × 10(4)。所有糖胺聚糖均被鉴定为在C-6位硫酸化的硫酸软骨素。两种核心蛋白的氨基酸组成相似,Mr约为1.6 X 10(5)。在酸水解之前在硼氢化钠存在下进行β-消除后,来自正常主动脉的硫酸软骨素蛋白聚糖的丝氨酸从109减少到68,苏氨酸从117减少到55。对于来自动脉粥样硬化斑块的单体,丝氨酸和苏氨酸的减少分别为103至81和107至77个残基/1000。结果表明,动脉粥样硬化斑块蛋白多糖中硫酸软骨素链和核心蛋白上的寡糖较少。与正常主动脉相比,动脉粥样硬化斑块蛋白多糖中丝氨酸和苏氨酸的取代率分别为38%和21%,53%和28%。据估计,在动脉粥样硬化斑块中,每个核心蛋白的硫酸软骨素链较少但较长,转化为动脉粥样硬化斑块中较小的总体单体尺寸。
Chondroitin sulfate proteoglycan monomers were prepared from intima media minces of grossly normal human aorta and adjacent fatty fibrous atherosclerotic plaques. Glycosaminoglycan chains prepared from monomer from normal aorta displayed a normal distribution profile on Ultrogel ACA 54 with a Kav of 0.48, whereas those of atherosclerotic aorta displayed a bimodal distribution (major peak, Kav 0.35; minor peak, Kav 0.70). The Mr of glycosaminoglycans from normal aorta was estimated to be 1.5 X 10(4). For atherosclerotic aorta, the majority of chains were 2.0 X 10(4) while the smaller population was 1.2 X 10(4). All glycosaminoglycans were identified as chondroitin sulfate sulfated at the C-6 position. The amino acid compositions of both core proteins were similar with Mr of about 1.6 X 10(5). After beta-elimination in the presence of sodium borohydride prior to acid hydrolysis, chondroitin sulfate proteoglycan from normal aorta had reductions in serine from 109 to 68 and in threonine from 117 to 55. For the monomer from atherosclerotic plaque, reductions in serine and threonine, respectively, were from 103 to 81 and from 107 to 77 residues per 1000. The results suggested fewer chondroitin sulfate chains and oligosaccharides on the core protein in the proteoglycan of atherosclerotic plaque. Compared to normal aorta, substituted serines and threonines in the proteoglycan of atherosclerotic plaque were about half, respectively, 38% vs 21% for serine, 53% vs 28% for threonine. It is estimated that in atherosclerotic plaque there are fewer, but longer, chondroitin sulfate chains per core protein, translating into a smaller overall monomer size in atherosclerotic plaque.