Urinary Excretion of Glycosaminoglycans and Brush Border and Lysosomal Enzymes as Markers of Glomerular and Tubular Involvement in Kidney Diseases

2015 ◽  
pp. 107-110 ◽  
Author(s):  
B. Baggio ◽  
G. Gambaro ◽  
G. Briani ◽  
S. Favaro ◽  
A. Borsatti
Keyword(s):  
Urinary Excretion ◽  
Brush Border ◽  
Lysosomal Enzymes ◽  
Kidney Diseases

Localization of brush-border and lysosomal enzymes in HT29 cells

1990 ◽  
Vol 14 ◽  
pp. 235
Author(s):  
H BRIL ◽  
J KLUMPERMAN ◽  
J FRANSEN ◽  
L GINSEL
Keyword(s):  
Brush Border ◽  
Lysosomal Enzymes ◽  
Ht29 Cells

Human parathyroid hormone (1–34) increases urinary excretion of lysosomal enzymes in rats

Life Sciences ◽  
1999 ◽  
Vol 65 (17) ◽  
pp. 1725-1732 ◽  
Author(s):  
Takanori Iwata ◽  
Shunya Uchida ◽  
Masayuki Hori ◽  
Kentaro Sakai ◽  
Takae Towatari ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Urinary Excretion ◽  
Lysosomal Enzymes ◽  
Human Parathyroid Hormone

scholarly journals Urinary excretion of brush-border enzymes of the proximal renal tubules in pregnant women with hypertensive disorders

2015 ◽  
Vol 86 (7) ◽  
pp. 494-498
Author(s):  
Andrzej Torbé ◽  
Ewelina Chłapowska ◽  
Jolanta Szymańska-Pasternak ◽  
Joanna Bober ◽  
Ewa Kwiatkowska ◽  
...  
Keyword(s):  
Urinary Excretion ◽  
Pregnant Women ◽  
Brush Border ◽  
Renal Tubules ◽  
Brush Border Enzymes ◽  
Hypertensive Disorders

Increased β-N-Acetyl-Glucosaminidase Activity in Diabetes Mellitus

1974 ◽  
Vol 20 (9) ◽  
pp. 1229-1230 ◽  
Author(s):  
Francesco Belfiore ◽  
Luigi Lo Vecchio ◽  
Elena Napoli ◽  
Vito Borzi
Keyword(s):  
Diabetes Mellitus ◽  
Blood Glucose ◽  
Urinary Excretion ◽  
Lysosomal Enzymes ◽  
Renal Excretion ◽  
Control Subjects ◽  
Enhanced Activity ◽  
Blood Glucose Concentrations

Abstract In 45 diabetics the 24-h urinary excretion of β-N-acetylglucosaminidase (E.C. 3.2.1.30) was increased by 40% (P < 0.05) compared to 35 control subjects. The enzyme excretion was correlated with glycemia (r = 0.58, P < 0.001), being little changed in diabetics with blood glucose concentrations of less than 200 mg/dl, and markedly elevated (+ 123%, P < 0.001) in those whose blood glucose was greater than 200 mg/dl. The rate of diuresis seemed to have no effect. These data indicate that the enhanced activity previously described in sera of diabetics for β-N-acetyl-glucosaminidase (as well as for other lysosomal enzymes) cannot be attributed to impairment of renal excretion, and support the hypothesis that in diabetes there is an "activation" of lysosomal enzymes in tissues that causes an increase in their activity in serum and, consequently, in urine.

scholarly journals Changes in the Expression of Renal Brush Border Membrane N-Glycome in Model Rats with Chronic Kidney Diseases

Biomolecules ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 1677
Author(s):  
Aiying Yu ◽  
Jingfu Zhao ◽  
Shiv Pratap S. Yadav ◽  
Bruce A. Molitoris ◽  
Mark C. Wagner ◽  
...  
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Kidney Diseases ◽  
Protein Glycosylation ◽  
Chronic Kidney Diseases ◽  
Renal Brush Border Membrane ◽  
Protein Functions ◽  
Liquid Chromatography Tandem Mass ◽  
The Stability

Chronic kidney disease (CKD) is defined by a reduced renal function i.e., glomerular filtration rate (GFR), and the presence of kidney damage is determined by measurement of proteinuria or albuminuria. Albuminuria increases with age and can result from glomerular and/or proximal tubule (PT) alterations. Brush-border membranes (BBMs) on PT cells play an important role in maintaining the stability of PT functions. The PT BBM, a highly dynamic, organized, specialized membrane, contains a variety of glycoproteins required for the functions of PT. Since protein glycosylation regulates many protein functions, the alteration of glycosylation due to the glycan changes has attracted more interests for a variety of disease studies recently. In this work, liquid chromatography-tandem mass spectrometry was utilized to analyze the abundances of permethylated glycans from rats under control to mild CKD, severe CKD, and diabetic conditions. The most significant differences were observed in sialylation level with the highest present in the severe CKD and diabetic groups. Moreover, high mannose N-glycans was enriched in the CKD BBMs. Characterization of all the BBM N-glycan changes supports that these changes are likely to impact the functional properties of the dynamic PT BBM. Further, these changes may lead to the potential discovery of glycan biomarkers for improved CKD diagnosis and new avenues for therapeutic treatments.

Urinary excretion of brush-border antigen and plasma proteins in early stages of diabetic nephropathy

1990 ◽  
Vol 188 (2) ◽  
pp. 93-100 ◽  
Author(s):  
Antonio Mutti ◽  
Rossella Alinovi ◽  
Gian Marco Ghiggeri ◽  
Enrico Bergamaschi ◽  
Giovanni Candiano ◽  
...  
Keyword(s):  
Diabetic Nephropathy ◽  
Urinary Excretion ◽  
Brush Border ◽  
Plasma Proteins ◽  
Early Stages

Oligopeptides: mechanism of renal clearance depends on molecular structure

1992 ◽  
Vol 263 (1) ◽  
pp. F109-F115 ◽  
Author(s):  
H. Minami ◽  
H. Daniel ◽  
E. L. Morse ◽  
S. A. Adibi
Keyword(s):  
Molecular Structure ◽  
Urinary Excretion ◽  
Renal Clearance ◽  
Brush Border ◽  
Hydrolytic Activity ◽  
Renal Tubular Cells ◽  
Relative Contribution ◽  
Perfusion Studies ◽  
Renal Tubular ◽  
Hydrolysis Of

We have investigated the relative contribution of hydrolysis, intact transport and urinary excretion to the renal clearance of Gly-Sar, Gly-Sar-Sar, and Gly-Gly-Sar in fed and starved rats. The results obtained from isolated kidney perfusion studies are summarized as follows: 1) clearance was fastest for Gly-Gly-Sar and slowest for Gly-Sar-Sar, 2) urinary excretion of Gly-Sar-Sar exceeded that of Gly-Gly-Sar or Gly-Sar, 3) there was accumulation of products of hydrolysis of Gly-Gly-Sar in the perfusate but not of Gly-Sar or Gly-Sar-Sar, 4) isolated brush-border and basolateral membranes of renal tubular cells lacked hydrolytic activity against Gly-Sar and Gly-Sar-Sar but possessed hydrolytic activity against Gly-Gly-Sar, 5) an excess amount of Gly-Sar-Sar reduced the rate of clearance of Gly-Gly-Sar by approximately 40% and significantly increased urinary excretion of this peptide, 6) the nonfiltering kidney cleared Gly-Gly-Sar at a rate which was 50% of that of the filtering kidney but did not clear Gly-Sar, and 7) starvation for 96 h was without a significant effect on the renal clearance of either Gly-Sar or Gly-Sar-Sar but significantly reduced the renal clearance of Gly-Gly-Sar and the brush-border membrane hydrolase activity against this peptide. We conclude that the molecular structure determines the affinity of oligopeptides for the membrane transport and hydrolytic systems, which, in turn, determines their efficiency for clearance by the kidney.

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