HISTOCHEMICAL LOCALIZATION OF β-GLUCURONIDASE AND N-ACETYL-β-GLUCOSAMINIDASE
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چکیده
منابع مشابه
Quantification of Lysosomal Membrane Permeabilization by Cytosolic Cathepsin and β-N-Acetyl-Glucosaminidase Activity Measurements.
Programmed cell death involving lysosomal membrane permeabilization (LMP) is an alternative cell death pathway induced under various cellular conditions and by numerous cytotoxic stimuli. The method presented here to quantify LMP takes advantage of the detergent digitonin, which creates pores in cellular membranes by replacing cholesterol. The difference in cholesterol content between the plasm...
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BACKGROUND Diabetic nephropathy is a clinical diagnosis where proteinuria is present in a patient with diabetes. Early intervention can significantly improve the prognosis. However, imprecision of the currently available biomarkers have impaired effective therapies in a timely manner. Urinary N-acetyl-β-D-glucosaminidase (NAG) is excreted in abnormally high amounts in many renal diseases. The a...
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O-GlcNAcylation is a common and dynamic modification of intracellular proteins in which β-N-acetyl-glucosamine moieties are attached to hydroxyl groups of serine or threonine residues (O-GlcNAc). Accumulating evidence suggests the critical role of protein O-GlcNAcylation in signal transduction, transcriptional control, cell cycle regulation and protein degradation. However, the exact role of O-...
متن کاملUrinary Activities of N-acetyl-β-D-glucosaminidase and Its Isoenzyme B in Cadmium-Exposed Rats
This paper aims to assess the relationship between the urinary activity of N-acetyl-β-D-glucosaminidase (NAG) and its isoenzyme B (NAG-B) and cadmium (Cd) concentration in the urine as well as to evaluate which of these lysosomal enzymes may be a more useful biomarker for the monitoring of Cd-induced tubular damage. For this purpose we have used an experimental model in rats chronically exposed...
متن کاملStudies on glucosaminidase. 2. Substrates for N-acetyl-beta-glucosaminidase.
the oxygen uptake and acetoacetate oxidation when added alone or with fumarate, but not in the presence of a-oxoglutarate. The reasons for these differences are discussed. Anaerobically, relatively slight inhibitions of the reduction of acetoacetate were observed. 6. The oxidation of L( + )-p-hydroxybutyrate is inhibited by dinitrophenol, whereas that of the D(-)-form is not. This is related to...
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ژورنال
عنوان ژورنال: Journal of Histochemistry & Cytochemistry
سال: 1961
ISSN: 0022-1554,1551-5044
DOI: 10.1177/9.1.105