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M Sternberg

Publications and source records attributed to M Sternberg.

At least 55 records · Page 3Linked to original sources
PubMed1984

Cleavage of oligosaccharides by rat kidney sialidase. Influence of substrate structure.

The specificity of the sialidase activity present in rat kidney cortex (12 000 X g pellet) was studied with various tritiated oligosaccharidic substrates: (i) alpha NeuAc2----3 beta Gal1----4Glc-itol[3H], alpha NeuAc2----6 beta Gal1----4Glc-itol[3H]. and alpha NeuAc2----8 alpha NeuAc2----3 beta Gal1----4Glc-itol[3H] from bovine colostrum; (ii) alpha NeuAc2----6 beta Gal1----4 beta GlcNAc-itol[3H], alpha NeuAc2----3 beta Gal1----4 beta GlcNAcl----2 alpha Man1----3 beta Man1----4 GlcNAc-itol[3H] alpha NeuAc2----6 beta Gal1----4 beta GlcNAc1----2 alpha Man1----3(beta Gal 1----4GlcNAc1----2 alpha Man 1----6)beta Man1----4GlcNAc-itol[3H]et alpha NeuAc2----6 beta Gal1----4 beta GlcNAc1----2 alpha Man1----3(alpha NeuAc2----6 beta Gal1----4 beta GlcNAc1----2 alpha Man1----6)beta Man1 4GlNAc-itol[3H] isolated from the urine of a patient with mucolipidosis I. The enzyme cleaves alpha 2----3 and alpha 2----8 linkages at a greater rate than the alpha 2----6 bonds. Its activity decreases with the length of the oligosaccharidic chain. Substitution of a glucose moiety by Nacetylglucosamine results in diminished activity. The specificity of rat kidney sialidase differs from that reported for other mammalian of viral sialidases.

Animals↗
PubMed1983

Inhibition of alkaline phosphatase activity by glucose.

Non-enzymatic glycosylation (NEG) of alkaline phosphatase (AP) was studied after short- and long-term incubation with glucose and other carbohydrates. Glucose and amino sugars clearly inhibited the enzyme activity; this was in contrast to reducing and non-reducing disaccharides, which had an enhancing effect. After AP had been incubated with 18 nmol/l glucose for 180 minutes (short-term incubation), a subsequent extensive dialysis revealed full recovery of the enzymatic activity. This, plus the demonstration of a [3H]sodium borohydride-reducible glucose-protein adduct, indicated that initially a labile aldimine (Schiff base) had been formed. Binding experiments with [14C]glucose and failure of dialysis to achieve a recovery of enzymatic activity after long-term incubation suggested that subsequently a stable ketoamine product had been formed. This was further confirmed by the thiobarbituric acid test, which revealed 0.65 nmol 5-hydroxymethylfurfural/mg protein for glycosylated AP compared to 0.11 for the non-glycosylated control. Preliminary results further suggest that NEG of AP also occurs in vivo. Streptozotocin diabetic rats had significantly lower serum AP activities than did non-diabetic controls (mean +/- SD: 153.7 +/- 28.4 vs. 760.5 +/- 95.7 U/l; p less than 0.001). Blood glucose levels and serum AP activity, which had been determined simultaneously during an oral glucose tolerance test, showed without exception an inverse relationship in each of 32 healthy children studied. The biological significance of these findings remains to be established.

Adolescent↗
PubMed1983

Inhibition of the alpha-glucosidase specific for collagen disaccharide units in diabetic rat kidney by in vivo glucose levels: possible contribution to basement membrane thickening.

The activity of the alpha-glucosidase specific for collagen disaccharide units has been measured in kidney cortex homogenates of streptozotocin-diabetic rats under three different conditions: (1) in dialyzed homogenates; (2) in non-dialyzed homogenates; (3) in non-dialyzed homogenates to which glucose was added to compensate for dilution due to homogenization and to reach the glucose concentration determined in kidney cortex (37.5 +/- 2.8 mmol/kg diabetic cortex versus 6.8 +/- 0.3 mmol/kg normal cortex). Under the latter condition, the enzyme activity was markedly decreased in diabetic kidney cortex when compared with that of normal age-matched controls: 4.03 +/- 0.25 versus 6.82 +/- 0.29 units/mg protein (p less than 0.001). Inhibition of enzyme activity was also significant in non-dialyzed diabetic homogenates without additional glucose. In the absence of glucose (in the dialyzed homogenates), it is confirmed that the enzyme activity is elevated in diabetic kidney. The glucose inhibition of the enzyme activity has been shown to be important under in vivo conditions. It may therefore contribute to kidney basement membrane thickening.

Animals↗
PubMed1982

Studies on the alpha-glucosidase specific for collagen disaccharide units: variations associated with capillary basement membrane thickening in kidney and brain of diabetic and aged rats.

The alpha-glucosidase specific for the hydroxylysine-linked disaccharide units of collagens (or 2-0-alpha-D-glucopyranosyl-5-0-beta-D-galactopyranosylhydroxy-L-lysine glucohydrolase) has been measured in kidney cortex and brain cortical tissue of streptozotocin diabetic rats after 19, 23 or 28 weeks of diabetes and of aged rats 22 months old. Increased specific activities of the enzyme have been found repeatedly in the dialyzed homogenates and the 7.2 X 10(6) g.min supernatants of kidney and brain at the various stages of diabetes when compared with age-matched controls; the specific activities returned to a normal level after insulin treatment. Similar increased specific activities were observed in kidney and brain of the aged normoglycemic rats when compared with young adult rats. In diabetic kidney cortex, beta-galactosidase and p-nitrophenyl-alpha-D-glucoside glucosidase specific activities were decreased in contrast to the increase of glucosyl-galactosyl-hydroxy-lysine glucohydrolase. In kidney cortex of the aged rats, beta-galactosidase activity was also decreased, but p-nitrophenyl-alpha-D-glucoside glucosidase was increased. In both diabetic and aged rats, thickening of the kidney glomerular basement membranes was confirmed; thickening of the brain cortical capillary basement membranes was also observed. Thus in the diabetic and aged animals, the increased glucosyl-galactosyl-hydroxylysine glucohydrolase specific activity was associated with basement membrane thickening in the kidney and the brain.

Aging↗
PubMed1982

Reduced collagenolytic activity of rat kidneys with steptozotocin diabetes.

Collagenolytic activity of rat kidneys with streptozotocin diabetes was estimated by means of a biological collagenase assay and compared to healthy controls. Collagenolytic activity was found significantly decreased in rat kidneys with diabetes correlating with blood glucose levels (r = -0.82, p less than 0.001). Elevated blood glucose levels seem to be responsible for the inhibition. This is supported by our experiment of incubating bacterial collagenase with several carbohydrates as glucose, galactose and saccharose: glucose and galactose significantly inhibited the collagenolytic activity, while saccharose failed to inhibit the enzymatic reaction. The interpretation of the results is that glucose is able to bind to the enzyme as Schiff base, which could be shown by tritiated sodium borohydride reduction of the Schiff base formed between collagenase and glucose. Another support of the hypothesis is that blocking of the amino group of lysine at the active site either by glucose or trifluoroacetylation of collagenase is reducing the collagenolytic activity. The biological significance could be the decreased catabolism of collageneous material of the extracellular matrix, as, e.g., the glomerular basement membrane, which was reported in a previous publication.

Animals↗
PubMed1982

Aluminum phosphate visualisation of acid phosphatase activity: a biochemical and x-ray microanalysis study.

A new method is described that demonstrates acid phosphatase activity in the cells of the proximal tubules of the rat kidney. The method is based on the formation of an insoluble aluminum phosphate precipitate. Microanalysis was used to demonstrate the presence of intracellular aluminum and determine the quantity present under the probe. Parallel biochemical studies showed that the aluminum precipitate was indeed due to acid phosphatase activity.

Acid Phosphatase↗
PubMed1982

[Enzyme activities of native non-enzymatically glucosylated trypsin, chymotrypsin and papain].

The proteases trypsin, alpha-chymotrypsin and papain were incubated with glucose for a period of 10 days at 37 degrees C and activity was tested in comparison to the enzymes incubated with the puffer solution only without glucose addition. Papain additionally was incubated for 10 days at 37 degrees C with the carbohydrates galactose, sucrose, lactose, glucosamine, galactosamine and mannosamine. While trypsin and chymotrypsin showed no change in enzymatic activity after incubation with glucose, the activity of papain was reduced by 70% to 90% (mean 84%). Incubation with galactose also inhibited papain activity but to a lesser extent (25% to 60%, mean 43%). Incubation with the other carbohydrates failed to inhibit papain activity. The mechanism inferred is nonenzymatic glucosylation of papain possibly as ketoamine linkage at the lysine residues situated close to the active site of papain causing steric or allosteric hindrance of the papain activity. The serine hydrolases trypsin and chymotrypsin without lysine residues near their active sites revealed unchanged activity after incubation with glucose.

Carbohydrate Metabolism↗
PubMed1981

The in vitro biosynthesis of taxiphyllin and the channeling of intermediates in Triglochin maritima.

The in vitro biosynthesis of the cyanogenic glucoside taxiphyllin has recently been demonstrated in Triglochin maritima (Hösel, W., and Nahrstedt, A. (1980) Arch. Biochem. Biophys. 203, 753-757). We have now studied in more detail the multistep conversion of tyrosine into p-hydroxymandelonitrile, the immediate precursor of taxiphyllin, catalyzed by microsomes isolated from dark-grown seedlings. The biosynthetic pathway involves N-hydroxytyrosine, p-hydroxyphenylacetaldoxime, and p-hydroxyphenylacetonitrile. In marked contrast to an analogous pathway in Sorghum bicolor, p-hydroxyphenylacetonitrile is the best substrate for cyanide production (Vmax = 224 nmol/h/g, fresh wt) and the physiological substrate tyrosine is the poorest (Vmax = 18.8 nmol/h/g, fresh wt). The substrates exhibit alkaline pH optima between 7.5 and 9, and all except tyrosine show pronounced substrate inhibition. We have found that p-hydroxyphenylacetonitrile generated in situ from tyrosine is free to equilibrate by diffusion with exogenous material. On the other hand, neither N-hydroxytyrosine nor p-hydroxyphenylacetaldoxime will readily exchange with exogenous intermediates. We consider both N-hydroxytyrosine and p-hydroxyphenylacetaldoxime to be channeled in T. maritima, whereas in S. bicolor N-hydroxytyrosine and p-hydroxyphenylacetonitrile are channeled and the aldoxime is freely exchangeable.

Carbon Radioisotopes↗
PubMed1979

Excretion and synthesis of basement membrane disaccharide units in Masugi nephritis.

During nephrotoxic nephritis in the rat, an increased urinary excretion of glucosyl-galactosyl hydroxylysine and of galactosyl-hydroxylysine has been observed in the autologous phase of the disease. This due mainly to an elevation of the polypeptide-bound fraction of these hydroxylysyl glucosides with a molecular weight over 1,000 daltons. The levels of both urinary hydroxylysyl glucosides were correlated with proteinuria. Their increased excretion appears to originate in the lysed glomerular basement membrane. At the same stage of nephrotoxic nephritis, an increased glucosyl transferase activity could be demonstrated in the isolated glomeruli, correlated with albuminuria, attesting a higher turn-over of the disaccharide units of the glomerular basement membrane.

Albuminuria↗
PubMed1976

[Action of pyridinol carbamate on hetero-immune Masugi nephritis in the rat (author's transl)].

Pyridinol-carbamate (P.C.) is a new substance with various properties including an anti-inflammatory (anti-kinin) and an antiplatelet aggregation activity. Since a coagulation process has been demonstrated in Masugi nephritis in Rats, we investigated the effect of P.C. in this experimental model. P.C. (150 mg/kg/day) was given orally from day 1 to day 28. It prevented partially the G.N.: proteinuria was significantly lower than in nephritic untreated animals with a reduction of seromucoid blood levels and B.U.N. Histological examination revealed that glomerular injury was limited in treated animals specially with regards to G.B.M. alterations and deposits.

Animals↗
PubMed1975

Lysinoalanine: presence in foods and food ingredients.

Lysinoalanine, N6-(DL-2-amino-2-carboxyethyl)-L-lysine, an unusual amino acid implicated as a renal toxic factor in rats, has been found in proteins of home-cooked and commercial foods and ingredients. Although it has been reported to occur in both edible and nonfood proteins only after alkali treatment, it has now been identified in food proteins that had not been subjected to alkali. Lysinoalanine is generated in a variety of proteins when heated under nonalkaline conditions.

Dietary Proteins↗
PubMed1975

Biochemical criteria for the evaluation of drug efficiency on adjuvant arthritis and nephrotoxic serum nephritis in the rat: studies with phenylbutazone, L-Asparaginase, colchicine, lysine acetylsalicylate, and pyridinol carbamate.

The levels of serum orosomucoid, haptoglobin, and seromucoid were evaluated as possible quantitative criteria for the estimation of drug efficiency in adjuvant arthritis and nephrotoxic serum nephritis. In adjuvant arthritis, haptoglobin, seromucoid, and chiefly orosomucoid serum levels were generally very sensitive to anti-inflammatory agents such as phenylbutazone and pyridinol carbamate, and to immunosuppressive agents such as L-asparaginase. There was a significant correlation between the serum levels of these glycoproteins and the arthritis scores. In nephrotoxic serum nephritis, seromucoid levels were correlated with the proteinuria of the autologous phase and were found to be a good complementary criterion for the analysis of the efficiency of pyridinol carbamate, colchicine, iysine acetylsalicylate, and L-asparaginase.

Animals↗