Klein D J, Dehnel P J, Oegema T R, Brown D M
Lab Invest. 1984 May;50(5):543-51.
The synthesis of intact proteoglycans and their glycosaminoglycan (GAG) side chains by isolated rat glomeruli in vitro were studied both at the onset (5 days) and at the point of maximal proteinuria (7 days) of the nephrotic syndrome induced with the aminonucleoside of puromycin. Glomeruli from nephrotic animals incorporated 1.5-fold and 3.0-fold more 35SO4 label into GAG than glomeruli from control animals at 5 and 7 days, respectively, with heparan-35SO4 GAG being responsible for the majority of the increment. Both nephrotic and control incubations contained 60% of the label in the incubation medium, 40% in the glomerular fractions, and less than 1% in the glomerular basement membrane. Glomerular basement membrane from nephrotic rats had no change in their total heparan-35SO4 GAG content. The majority of intact proteoglycan(s) from the glomerular matrix and from the incubation medium of nephrotic and control animals was found in the most buoyantly dense fraction of CsCl gradients (fraction 1). 35S-labeled material isolated from glomeruli of nephrotic animals showed a consistent shift toward lower density gradient fractions, indicating a decrease in their overall carbohydrate to protein ratio. Diethylaminoethyl chromatography of fraction 1 proteoglycan showed a single biphasic peak with the nephrotic rat having an increase in the proportion contributed by the earlier component of the peak. Fraction 1 proteoglycan(s) from the nephrotic experiment was found to have a smaller average hydrodynamic size by Sepharose CL-2B chromatography without a significant change in the corresponding 35S-GAG chain sizes (molecular weight 14,000) by Sepharose CL-6B chromatography. 35S-macromolecules from glomeruli of nephrotic and control rats that appeared in the middle of the CsCl gradients (fraction 3) had similar Sepharose CL-2B elution volumes, whereas the corresponding 35S-GAG chains from incubations of glomeruli from nephrotic animals were smaller. Increased synthesis of heparan sulfate proteoglycan by glomeruli from puromycin aminonucleoside-induced nephrotic rats may be compensatory to loss of another component of the glomerular filtration barrier or may result from abnormal interaction of proteoglycan(s) from nephrotic animals with other glomerular matrix constituents.
在嘌呤霉素氨基核苷诱导的肾病综合征发病初期(5天)和蛋白尿高峰期(7天),研究了离体大鼠肾小球体外合成完整蛋白聚糖及其糖胺聚糖(GAG)侧链的情况。在第5天和第7天,肾病动物的肾小球分别比对照动物的肾小球将多1.5倍和3.0倍的35SO4标记掺入GAG中,其中硫酸乙酰肝素-35SO4 GAG占增加量的大部分。肾病组和对照组的孵育物中,60%的标记物存在于孵育培养基中,40%存在于肾小球部分,而肾小球基底膜中的含量不到1%。肾病大鼠的肾小球基底膜中硫酸乙酰肝素-35SO4 GAG的总含量没有变化。肾病组和对照组动物肾小球基质及孵育培养基中的大多数完整蛋白聚糖存在于CsCl梯度中浮力密度最大的部分(第1部分)。从肾病动物肾小球中分离出的35S标记物质显示向较低密度梯度部分的一致转移,表明其总碳水化合物与蛋白质的比例降低。对第1部分蛋白聚糖进行二乙氨基乙基色谱分析显示出一个单一的双相峰,肾病大鼠的峰中早期成分所占比例增加。通过Sepharose CL - 2B色谱分析发现,肾病实验中第1部分蛋白聚糖的平均流体力学尺寸较小,而通过Sepharose CL - 6B色谱分析,相应的35S - GAG链尺寸(分子量14,000)没有显著变化。出现在CsCl梯度中间部分(第3部分)的肾病组和对照组大鼠肾小球中的35S - 大分子具有相似的Sepharose CL - 2B洗脱体积,而肾病动物肾小球孵育物中相应的35S - GAG链较小。嘌呤霉素氨基核苷诱导的肾病大鼠肾小球中硫酸乙酰肝素蛋白聚糖合成增加,可能是对肾小球滤过屏障另一成分丢失的代偿,也可能是肾病动物的蛋白聚糖与其他肾小球基质成分异常相互作用的结果。