Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The relationship between lysozyme and sodium reabsorption by the kidney tubule was studied in the experimental Fanconi syndrome. Female, anesthetized Sprague-Dawley rats were injected intravenously with maleic acid (an inhibitor of sodium transport) neutralized with sodium hydroxide in doses of either 2 or 8 mmol/kg. Clearance studies were performed immediately afterward, and plasma and urine were analyzed for inulin, pH, sodium, glucose, and lysozyme. Two hours after the maleic acid injection, renal cortical tissue was removed and homogenized. Specific activity of Na-K-ATPase was assayed in the light microsomal fraction. The results showed that both concentrations of maleic acid caused significant increases in urinary volume, glucose excretion, and pH. There were significantly correlated decreases in TNafract and TLyfract. The slope of the regression line (TLyfract = 1.03 TNafract - 5.82; r = 0.92) approximated unity. Renal cortical Na-K-ATPase activity was significantly decreased by 25% in the animals receiving 2 mmol maleic acid and 43% in the animals receiving 8 mmol. The evidence suggests that lysozyme reabsorption in the proximal tubule might be mediated directly or indirectly by active tubular transport of sodium, a process that is related to the Na-K-ATPase transport system.
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PMID:Renal handling of lysozyme in experimental Fanconi syndrome. 14 77

The effect of mercury on renal lysosomal protein digestion was studied after administration of mercury in vitro and in vivo. Mercuric chloride or methylmercury chloride was added in vitro to lysosomal enzymes isolated from normal rats, and subsequently, digestion experiments were carried out using 125I-labeled lysozyme or cytochrome c as substrate proteins. Both mercury compounds produced a concentration-dependent inhibition of the degradation of the proteins, mercuric chloride being the strongest inhibitor. Mercuric chloride was also administered to rats in vivo for 5 to 8 months. Renal lysosomal enzymes from these animals also had a decreased ability to digest for the two substrate proteins. Furthermore, the digestion of lysozyme intravenously injected into mercury-intoxicated rats was decreased in renal cortical slices incubated in vitro. Electron microscope autoradiography showed that intravenously injected labeled lysozyme was located primarily over lysosomes in proximal tubule cells 1 hour after injection in both control animals and mercury-intoxicated rats. These results suggest a decreased catabolism of low molecular weight proteins in the kidney during chronic mercury intoxication.
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PMID:Effects of mercury on lysosomal protein digestion in the kidney proximal tubule. 20 71

The effects of dextran on renal ultrastructure and on the handling of protein by renal proximal tubules were evaluated in dextran-tolerant rats. In vivo and in vitro systems were studied by a combination of electron microscope and cell fractionation techniques. Dextran was demonstrated by electron microscopy in endocytic vacuoles and lysosomes ing a dextran-retaining fixative, and there was an increase in the number and size of the lysosomes in the proximal tubule cells using a dextran-retaining fixative, and there was an increase in the number and size of the lysosomes in dextran-treated rats. A lysosomal accumulation of dextran was also demonstrated when 3H-dextran T-80 was injected i.v. and the renal cortex analyzed by tissue fractionation. When radioactive lysozyme was injected into dextran-treated rats, there was less filtration of the protein in the kidneys than there was in the controls, but the rate of degradation of the labeled protein in slices prepared from the renal cortex and incubated in vitro was the same in the two groups. Electron microscope autoradiography revealed that radioactive lysozyme reabsorbed by the tubule cells had a similar location in both control- and dextran-treated rats. It is concluded that lysosomal protein catabolism is not altered by the presence of dextran despite pronounced ultrastructural changes in the lysosomal system. The decreased filtration of labeled protein after dextran infusion is probably related to the decreased GFR during and immediately after the dextran infusion.
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PMID:Effects of dextran on lysosomal ultrastructure and protein digestion in renal proximal tubule. 52 77

Proteins filtered in the renal glomeruli are reabsorbed by the proximal tubule and catabolized in the lysosomes. On the basis of studies on isolated flounder tubules it has been suggested that, in addition to this catabolism, a transtubular transport of intact protein (lysozyme) also occurs. The present study demonstrates that significant amounts of lysozyme are reversibly bound to the peritubular side of isolated tubules. Electron microscopic autoradiography demonstrates that the protein is located in the basement membrane and intercellular spaces. After in vivo injection, 125I-lysozyme is mainly located in endocytic vacuoles of the first proximal segment, but also over the basal part of the cells. Since a significant peritubular binding of lysozyme is demonstrated in vitro, it is suggested that a similar binding of tracer protein originating from the peritubular capillaries might occur in vivo and that subsequent release of this protein in vitro might simulate transtubular transport. It is therefore concluded that release of tracer protein from isolated kidney tubules does not conclusively demonstrate transtubular transport of intact protein in experimental systems in which peritubular binding of protein can be demonstrated.
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PMID:Reversible peritubular binding of a cationic protein (lysozyme) to flounder kidney tubules. 72 61

Hypophysectomy is known to cause a rise in the renal lysozyme levels and atrophy of the proximal tubules of the kidney. The present study describes the relationship of serum, urinary, and renal lysozyme levels in hypophysectiomized animals. The renal lysozyme level continued to rise during the first 4 weeks after hypophysectomy and then remained constant while the serum level increased immediately after hypophysectomy and plateaued. Hypophysectomy did not produce lysozymuria for the time periods used in these experiments despite obvious tubular atrophy by the end of the 1st week after hypophysectomy. These data suggest that tubular atrophy must progress to a severe stage before a lysozymuria is produced. Thus the absence of urinary lysozyme activity does not exclude the possibility of proximal tubule injury.
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PMID:Serum, renal, and urinary lysozyme levels after hypohysectomy. 118 45

Renal extraction of low molecular weight proteins (LMWP) accounts for 30% to 80% of their total metabolic clearance. Extraction includes glomerular filtration, proximal tubular uptake, and intralysosomal proteolysis. To characterize the anatomic sites and enzymes involved in digestion of reabsorbed LMWP, the lysosomal proteases, cathepsin B and L, were measured by ultramicroassay in isolated S1, S2 and S3 segments of the proximal tubule of proteinuric rats. Increased glomerular filtration and tubular uptake of LMWP were induced by i.v. and i.p. injections of myoglobin and cationic and anionic lysozyme. Both cationic lysozyme and myoglobin increased cathepsin B and L activities in the proximal tubule, while anionic lysozyme had no effect. Morphologic examination of kidney tissue suggested that proximal tubular uptake of anionic lysozyme was negligible in comparison with the cationic form. Hence, only LMWP absorbed by the proximal tubule cells stimulated cathepsin B and L activities. Proximal tubular uptake of cationic lysozyme was determined by measurement of lysozyme activities in S1, S2, and S3. S1 segments contained the highest lysozyme activity, while S2 and S3 had much lower activities, and cathepsin B and L activity following cationic lysozyme injection was stimulated only in S1 segments. These results suggest that cathepsin B and L participate in lysosomal digestion of certain LMWP. Furthermore, the activities of cathepsin B and L adapt to increased uptake of LMWP. To gain additional insight into the mechanism of cathepsin adaptation, the cathepsin B and L activities were measured following injection of dextran with a similar low molecular weight.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of low molecular weight proteins and dextran on renal cathepsin B and L activity. 169 Mar 11

1. In the kidney, filtered proteins are rapidly reabsorbed by the proximal tubule via adsorptive endocytosis. This process starts with the protein binding to the luminal brush-border membrane. 2. The binding of 125I-labelled albumin to rat renal brush-border membrane vesicles and the effect of a low molecular weight protein lysozyme on that binding was assessed by the filtration method. 3. The Scatchard plot revealed a one-component binding-type curve with a dissociation constant Kd of 430.9 nM and 39.6 pmol/mg membrane protein for the number of binding sites. 4. Albumin binding was saturable and reversible, time and temperature dependent and the initial rate enhanced by increasing amounts of lysozyme. 5. The fact that association of albumin with the brush-border membrane vesicles was dependent upon the intravesicular space suggested a double process, binding of the ligand to the membrane surface and its internalization. These data suggest that albumin has a different binding site than that of a low-molecular weight protein lysozyme, with a constant affinity value near physiological loads. That specificity may confer selectivity upon the endocytic uptake process.
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PMID:Binding of 125I-labelled albumin by isolated rat renal brush-border membrane vesicles. Evidence for uptake and internalization process. 228 25

To address whether a renal tubular dysfunction is encountered in a particular patient subgroup with urolithiasis, the following parameters of tubular function were measured in urine taken in the morning from 214 stone formers after fasting: pH, excretion of lysozyme and gamma-glutamyl transferase (gamma-GT); fractional excretion (FE) of glucose, insulin, Mg, K, and HCO3 after an alkali loading; and the renal threshold for phosphate (TmP/GFR). The following diagnoses were made in the patient group: primary hyperparathyroidism (N = 8), medullary sponge kidneys (N = 21), hyperuricemia (N = 10), cystinuria (N = 2), struvite stone disease (N = 6), idiopathic hypercalciuria of the absorptive (N = 25), dietary (N = 69) or renal (N = 7) type, and normocalciuric idiopathic urolithiasis (N = 66). In 31% of the patients TmP/GFR was below 0.80 mmole/liter and in 13% of the patients, FE HCO3 after alkali loading was above normal. Urinary excretion of lysozyme and that of gamma-GT both were elevated in 17% of the patients. FE glucose, FE insulin, FE Mg, and FE K were elevated in 8, 9, 3, and 7% of the patients, respectively. This study demonstrates that a significant number of stone formers present with signs of renal tubular dysfunction, primarily involving the proximal tubule since apparent leaks of phosphate and of bicarbonate were most frequently encountered. The defects were not specific for a given etiologic group of patients; on the other hand, occurrence was related to the presence of large stones in the pyelocaliceal system at the time data were gathered. Taken together these data suggest that the tubulopathy in nephrolithiasis is the consequence rather than the cause of the stone.
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PMID:Tubulopathy in nephrolithiasis: consequence rather than cause. 287 Dec 16

During the acute renal tubular dysfunction of Fanconi syndrome and type 2 renal tubular acidosis (FS/RTA2) induced by maleic acid in the unanesthetized dog, we observed: 30 minutes after the onset of FS/RTA2, the urinary excretion of lysosomal enzymes, N-acetyl-beta-glucosaminidase (NAG), beta-glucuronidase (beta-gluc) and beta-galactosidase (beta-galac), increased simultaneously with the anticipated increase in renal clearance of lysozyme; the severities of all these hyperenzymurias increased rapidly, progressively, and in parallel, all reaching a peak some 60 to 80 minutes after their onset; thereafter, while the FS/RTA2 continued undiminished in severity, the severity of the hyperenzymurias decreased rapidly, greatly, progressively, and in parallel; and sodium phosphate loading strikingly attenuated the FS/RTA2 and the hyperenzymurias. Thus, the maleic acid-induced FS/RTA2 is attended by an acute reversible-complex derangement in the renal tubular processing of proteins that: affects not only lysozyme which is normally filtered, but also NAG and other lysosomal enzymes, which are not; and is to some extent functionally separable from that of FS/RTA2. The findings suggest that the derangements in renal processing of lysozyme and lysosomal enzymes are linked, and that a phosphate-dependent metabolic abnormality in the proximal tubule can participate in the pathogenesis of both these derangements and the FS/RTA2.
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PMID:Coordinately increased lysozymuria and lysosomal enzymuria induced by maleic acid. 310 28

The presence of different serum proteins in the cells of the proximal tubule of both meso- and metanephric nephrons in human embryos (7th-12th week of intrauterine life) was investigated using immunohistochemistry. Endogenous lysozyme, alpha-1-antitrypsin and ferritin were detected in mesonephric proximal tubules and, starting from the 8th week, also in metanephric proximal tubules. Our observations provide information concerning the appearance and distribution of tubular protein reabsorption during the early stages of development.
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PMID:Protein absorption by tubular mesonephric and metanephric structures in the human embryo. An immunohistochemical study. 349 Sep 18


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