H J Haga, K J Andersen, B M Iversen, J Ofstad, M Dobrota, R Matre
{"title":"被动海曼肾小球肾炎所致大鼠肾皮质溶酶体数量的变化。","authors":"H J Haga, K J Andersen, B M Iversen, J Ofstad, M Dobrota, R Matre","doi":"10.1159/000173133","DOIUrl":null,"url":null,"abstract":"<p><p>Acute passive Heymann glomerulonephritis in rats induced heavy proteinuria and highly increased urinary activity of N-acetyl-beta-D-glucosaminidase, acid beta-galactosidase and acid phosphatase. The cortical activity of these acid hydrolases was increased essentially in the large lysosomes as demonstrated by subfractionation of the lysosome-rich mitochondrial-lysosomal fraction, by rate zonal centrifugation. Banding density of small lysosomes shifted or reduced to slightly lower value (1.225 g/ml), which is between the banding densities of small 'light' (1.20 g/ml) and small 'dense' lysosomes (1.235 g/ml) in normal rat kidney cortex. Labelled protein reabsorbed in the proximal tubule is recovered in these populations of small lysosomes as well as in the large lysosomes or 'protein droplets'. Glomerulonephritis also induced a new population of small 'light' lysosomes (density 1.185-1.195 g/ml) enriched in cathepsin D. The previously demonstrated morphological, biochemical, and physiological heterogeneity of renal lysosomes was confirmed and emphasized in the kidney cortex of glomerulonephritic rats. The main changes in the lysosomal populations appear to reflect the increased protein reabsorption as confirmed by the proteinuria.</p>","PeriodicalId":77779,"journal":{"name":"Renal physiology","volume":"10 5","pages":"249-60"},"PeriodicalIF":0.0000,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000173133","citationCount":"3","resultStr":"{\"title\":\"Changes in lysosome populations in the rat kidney cortex induced by passive Heymann glomerulonephritis.\",\"authors\":\"H J Haga, K J Andersen, B M Iversen, J Ofstad, M Dobrota, R Matre\",\"doi\":\"10.1159/000173133\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Acute passive Heymann glomerulonephritis in rats induced heavy proteinuria and highly increased urinary activity of N-acetyl-beta-D-glucosaminidase, acid beta-galactosidase and acid phosphatase. The cortical activity of these acid hydrolases was increased essentially in the large lysosomes as demonstrated by subfractionation of the lysosome-rich mitochondrial-lysosomal fraction, by rate zonal centrifugation. Banding density of small lysosomes shifted or reduced to slightly lower value (1.225 g/ml), which is between the banding densities of small 'light' (1.20 g/ml) and small 'dense' lysosomes (1.235 g/ml) in normal rat kidney cortex. Labelled protein reabsorbed in the proximal tubule is recovered in these populations of small lysosomes as well as in the large lysosomes or 'protein droplets'. Glomerulonephritis also induced a new population of small 'light' lysosomes (density 1.185-1.195 g/ml) enriched in cathepsin D. The previously demonstrated morphological, biochemical, and physiological heterogeneity of renal lysosomes was confirmed and emphasized in the kidney cortex of glomerulonephritic rats. The main changes in the lysosomal populations appear to reflect the increased protein reabsorption as confirmed by the proteinuria.</p>\",\"PeriodicalId\":77779,\"journal\":{\"name\":\"Renal physiology\",\"volume\":\"10 5\",\"pages\":\"249-60\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1987-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1159/000173133\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Renal physiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1159/000173133\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Renal physiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000173133","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
摘要
大鼠急性被动海曼肾小球肾炎引起大量蛋白尿,尿中n -乙酰- β - d -氨基葡萄糖苷酶、酸性-半乳糖苷酶和酸性磷酸酶活性显著升高。这些酸性水解酶的皮质活性基本上在大溶酶体中增加,这是通过速率区离心对富含溶酶体的线粒体-溶酶体部分进行分划所证明的。小溶酶体带密度移位或降低至略低值(1.225 g/ml),介于正常大鼠肾皮质小“轻”溶酶体(1.20 g/ml)和小“密”溶酶体(1.235 g/ml)的带密度之间。在近端小管中重新吸收的标记蛋白在这些小溶酶体群体中以及在大溶酶体或“蛋白滴”中被恢复。肾小球肾炎还诱导了一种新的富含组织蛋白酶d的小“轻”溶酶体(密度1.185-1.195 g/ml)。先前证实的肾溶酶体形态、生化和生理异质性在肾小球肾炎大鼠肾皮质中得到证实和强调。溶酶体群的主要变化似乎反映了蛋白尿所证实的蛋白质重吸收的增加。
Changes in lysosome populations in the rat kidney cortex induced by passive Heymann glomerulonephritis.
Acute passive Heymann glomerulonephritis in rats induced heavy proteinuria and highly increased urinary activity of N-acetyl-beta-D-glucosaminidase, acid beta-galactosidase and acid phosphatase. The cortical activity of these acid hydrolases was increased essentially in the large lysosomes as demonstrated by subfractionation of the lysosome-rich mitochondrial-lysosomal fraction, by rate zonal centrifugation. Banding density of small lysosomes shifted or reduced to slightly lower value (1.225 g/ml), which is between the banding densities of small 'light' (1.20 g/ml) and small 'dense' lysosomes (1.235 g/ml) in normal rat kidney cortex. Labelled protein reabsorbed in the proximal tubule is recovered in these populations of small lysosomes as well as in the large lysosomes or 'protein droplets'. Glomerulonephritis also induced a new population of small 'light' lysosomes (density 1.185-1.195 g/ml) enriched in cathepsin D. The previously demonstrated morphological, biochemical, and physiological heterogeneity of renal lysosomes was confirmed and emphasized in the kidney cortex of glomerulonephritic rats. The main changes in the lysosomal populations appear to reflect the increased protein reabsorption as confirmed by the proteinuria.