[Index between mucoprotein hexose and mucoprotein tyrosine as element in the clinical evaluation of destructive processes].
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Adult↗
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[Influence of glandular mucoproteins on natural defense capacities. I. Glandular mucoproteins and complement levels].
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Complement System Proteins↗
[Influence of glandular mucoproteins on natural defense capacities. II. Glandular mucoproteins and lysozyme activity].
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Gastric Mucins↗
Characterization of gastric mucoproteins isolated by equilibrium density-gradient centrifugation in caesium chloride.
1. The mucoprotein from pig gastric mucus has been purified by equilibrium centrifugation in a CsCl gradient. 2. This procedure removes the non-covalently bound protein, which is closely associated with the mucoprotein and not easily removed from it by gel filtration. 3. The purified mucoprotein is separable by gel filtration into a high-molecular-weight mucoprotein A (mol.wt. 2.3x10(6)) and a low-molecular-weight mucoprotein B/C (mol.wt. 1.15x10(6)). 4. These two mucoproteins have the same chemical analysis namely fucose 11.3%, galactose 26%, glucosamine 19.5%, galactosamine 8.3% and protein 13.6%. 5. Mucoprotein A contains 3.1% ester sulphate. 6. These mucoproteins are isolated without enzymic digestion and have a higher protein content than the blood-group-substance mucoproteins from proteolytic digestion of gastric mucus. Detailed amino acid analysis shows that the extra protein in the non-enzymically digested material is composed of amino acids other than serine and threonine. 7. Mucoproteins A and B/C contain respectively 130 and 9 half-cystine residues per molecule of which about 78 and 6 residues are involved in disulphide linkages. 8. Cleavage of these disulphide linkages by mercaptoethanol splits both mucoproteins into four equally sized subunits of mol.wt. 5.2x10(5) for mucoprotein A and 2.8x10(4) for mucoprotein B/C. 9. The sole N-terminal amino acid of mucoprotein A is aspartic acid, whereas mucoprotein B/C has several different N-terminal amino acid residues.
Amino Acids↗
Tamm-Horsfall mucoprotein reduces promotion of calcium oxalate crystal aggregation induced by urate in human urine in vitro.
1. Increasing the concentration of dissolved urate promotes calcium oxalate crystallization in urine from which Tamm-Horsfall mucoprotein, an inhibitor of calcium oxalate crystal aggregation, has almost completely been removed. This study aimed to determine whether the effect of urate could be reduced or abolished by a physiological concentration of Tamm-Horsfall mucoprotein. This was approached in two ways. 2. The effect of Tamm-Horsfall mucoprotein on calcium oxalate crystallization induced by urate was tested in ultrafiltered (10 kDa) urine samples from 10 healthy men. Tamm-Horsfall mucoprotein (35 mg/l) was added to half of each specimen, the urate concentration was increased by the addition of sodium urate solution and crystallization was induced by a standard load of oxalate. The remainder of each urine specimen was used as a control; these specimens were treated with an identical amount of urate solution, but contained no Tamm-Horsfall mucoprotein. Tamm-Horsfall mucoprotein had no effect on the urinary metastable limit or on the deposition of calcium oxalate, but significantly reduced the size of the particles precipitated. 3. The effect of increasing the urate concentration in the presence of Tamm-Horsfall mucoprotein was tested. Tamm-Horsfall mucoprotein (35 mg/l) was added to 10 ultrafiltered urine samples as before, the samples were divided, and the concentration of urate was increased in half of each specimen. Compared with the control to which no urate was added, urate significantly reduced the amount of oxalate required to induce spontaneous calcium oxalate nucleation and increased the median volume and the particle size of the material deposited.(ABSTRACT TRUNCATED AT 250 WORDS)
Calcium Oxalate↗
Correlation between haptoglobin and sialic acid or mucoprotein in diseased bovine serum.
The correlation between haptoglobin (Hp) and mucoprotein or sialic acid in sera from diseased cattle was examined to evaluate the clinical application of serum Hp. First, the ranges of mucoprotein, sialic acid and hemoglobin binding capacity (HbBC) of 46 healthy cattle were determined. Then, levels of these reactants in 35 cattle suffering from various diseases were measured. The frequency of the abnormal values was 94.3% in mucoprotein, 45.7% in sialic acid and 82.9% in HbBC in diseased cattle. There was a significant correlation between mucoprotein and sialic acid, and between HbBC and mucoprotein or sialic acid. Some correlation between mucoprotein and neutrophils or alpha-globulin was also observed. In spite of high levels of mucoprotein and sialic acid, lower HbBC than expected levels were often observed in inflammatory disorders. Such cases might be complicated with some hemolytic disorders such as piroplasmosis. Determining serum HbBC together with other acute phase reactants might be useful for evaluating inflammatory diseases complicated with hemolytic disorders.
Animals↗
Conformational changes in gastric mucoproteins induced by caesium chloride and guanidinium chloride.
1. Caesium chloride and guanidinium chloride were shown to cause conformational changes in the high-molecular-weight mucoprotein A of water-soluble gastric mucus with no change in molecular weight. 2. Increasing concentrations of CsCl decrease the viscosity of the mucoprotein bringing about a transition which is essentially complete in 0.1m-CsCl. The shear-dependence of viscosity of the mucoprotein is abolished by low concentrations of CsCl. The normally highly expanded molecule becomes contracted in CsCl to a molecule having the same symmetry but a smaller volume and decreased solvation, in keeping with an increased sedimentation coefficient (18.7S-->33S). 3. This contracted form does not revert to the native conformation on removal of the CsCl. 4. A mechanism is discussed in terms of the effect of the Cs(+) and Cl(-)ions on water structure and the water-mucoprotein interaction. 5. Guanidinium chloride causes the CsCl-treated material to expand, in keeping with a decrease in s(0) (25,w) (33S-->26S). This is analogous to the known unfolding effect of guanidinium chloride on proteins and suggests that guanidinium chloride solubilizes groups involved in stabilizing the contracted structure. Removal of the guanidinium chloride results in a limited aggregation of four mucoprotein molecules. 6. These results show that caution must be exercised before interpreting the physical properties of mucoproteins which have been treated with CsCl and/or guanidinium chloride.
Animals↗
A mucoprotein with colon-specific determinants.
The tissue specificity of colonic mucoprotein antigen (CMA) was examined to determine whether the antigen might have a role as a tissue marker. The immunofluorescent technique, using a rabbit anti-CMA antiserum, was employed to examine a wide range of tissues. Gastrointestinal mucosae as well as non-gastrointestinal mucin producing tissues were positive; however, non-gastrointestinal reactivity could be eliminated by the appropriate absorptions. Mucoproteins were purified separately from each gastrointestinal anatomic region and used to absorb the antiserum. This analysis demonstrated the existence of a family of mucoproteins with a common gastrointestinal specific determinant(s). Mucoproteins from neighboring regions, as seen by this antiserum, showed a greater structural similarity than did mucoproteins from distant regions. Absorption of the antiserum with ileal or cecal mucoprotein allowed the detection of a colon specific determinant present on CMA.
Colon↗
Bovine-associated mucoprotein: de novo synthesis by nonmammary tissues.
Bovine tissues were cultured in vitro in the presence of carbon-14 amino acids and tritiated hexosamine to examine the de novo synthesis of the milk fat globule glycoprotein bovine-associated mucoprotein, by selected tissues. Among tissues examined, the relative synthesis of bovine-associated mucoprotein was highest in mammary tissue. The de novo synthesized bovine-associated mucoprotein in mammary and lacrimal gland cultures when examined for incorporation of carbon-14, had similar sedimentation profiles in sucrose density gradients and incorporated the same relative amount of carbohydrate. The bovine-associated mucoprotein synthesized by lung and spleen cultures sedimented in similar fashion to mammary gland bovine-associated mucoprotein when incorporation of carbon-14 was used as the marker, but it displayed greater heterogeneity when evaluated for tritium incorporation. Bovine-associated mucoprotein in the lung and spleen incorporated relatively less carbohydrate than that synthesized by mammary tissue. These findings support the concept of intertissue heterogeneity, which had been suggested by previous studies.
Adrenal Glands↗
A comparison of serum mucoprotein with serum alpha 1 acid glycoprotein, haptoglobin, and alpha 1 antitrypsin assays in monitoring inflammatory bowel disease.
Serum mucoprotein level is a monitor for inflammatory bowel disease activity although its method of measurement is laborious. An easier assay of alpha 1 acid glycoprotein is described. The ability of the two proteins to differentiate active from non-active cases was evaluated and the results compared with acute inflammatory reactants such as alpha 1 antitrypsin and haptoglobin. Amongst 79 patients with inflammatory bowel disease linear discriminant analysis was used to segregate overlapping ranges for patients with and without active disease and thus enabling the evaluation of sensitivity and specificity of each test. Predictive values of 78.6% for mucoprotein and 76.7% for alpha 1 acid glycoprotein were achieved and were due to the fact that there is a very strong linear correlation between these two proteins (r = 0.83, p less than 0.01). Furthermore the mucoprotein fraction is predominantly comprised of alpha 1 acid glycoprotein by as much as 91.5%. alpha 1 antitrypsin and haptoglobin showed poor predictive values. Pairing up all the proteins each with mucoprotein improved the sensitivity, specificity, and predictive value slightly. As a single test alpha 1 acid glycoprotein gave highest specificity, proved easy to assay and was automatable. It was therefore recommended as a substitute for serum mucoprotein in routine assays and as an effective monitor and predictor of inflammatory bowel disease.
Colitis, Ulcerative↗
Tamm Horsfall mucoprotein in urine of potential bladder stone formers.
The excretion rate of Tamm Horsfall mucoprotein was determined in normal and endemic boys. This latter group of boys showed presumptive signs of bladder stone, which include oxalate crystalluria, and difficult and sometimes painful voiding. At least 2 distinct forms of this mucoprotein are present in the urine. Semiquantitatively, there was no apparent difference in the excretion rate of this mucoprotein between the 2 groups of boys. The kidney function of these 2 groups was comparable and within the normal range. Furthermore, the presence of 5 mg. per cent of this mucoprotein in the solution of calcium and oxalate did not increase the ability of the solution to form more calcium oxalate precipitate nor did it induce precipitation of calcium oxalate from the dilute solution. We conclude that Tamm Horsfall mucoprotein may not have a role in the formation of oxalate crystalluria or bladder stone.
Child↗
Histochemical studies on mucoproteins in nerve cells of the dog.
Autonomic and sensory ganglion cells in the senile dog contain a deposition of PAS-positive substances which has been shown to be mucoprotein in nature. Data are presented to show that this PAS-positive mucoprotein can be demonstrated by metachromatic staining with toluidine blue after the mucoprotein is sulfated. This procedure indicates that mucoprotein is also present in a granular form in all nerve cells in both senile and young dogs. The evidence for this is further substantiated by the use of the aldehyde-fuchsin stain following both periodic acid oxidation and sulfation. The granular and non-granular deposition can be demonstrated by the periodic acid-aldehyde-fuchsin method due to the affinity of the aldehyde-fuchsin stain for aldehydes. It can be demonstrated following the sulfation-aldehyde-fuchsin method owing to the affinity of the stain for the sulfuric group. The evidence for this latter phenomenon has been reported by Scott and Clayton (6). It is concluded that mucoprotein is present in a granular form in all nerve cells in both senile and young dogs but is not concentrated enough in the latter to be demonstrated by the PAS method.
Aldehydes↗
A mucoprotein derived from human urine which reacts with influenza, mumps, and Newcastle disease viruses.
A mucoprotein, present in normal human urine, has been isolated and obtained in a state of a high degree of purity. A number of the biological, chemical, and physicochemical properties of the substance have been studied. From the results obtained in the present investigation and those reported in succeeding papers (34, 35) it appears that the mucoprotein has a high molecular weight, i.e., of the order of 7.0 x 10(6), consists of thread-like molecules which have axial ratios of approximately 100, and is specifically antigenic. This substance, which appears to be free of contaminating material, possesses in extraordinary degree the capacity to react with influenza, mumps, and Newcastle disease viruses. At equilibrium, with influenza virus, the minimal amount of the substance capable of giving a demonstrable reaction with one hemagglutinating unit of virus appears to be about 0.0003 microg. The mucoprotein is altered by preparations of influenza viruses and its capacity to react with these agents or others is lost. The kinetics of the inactivation process brought about by influenza viruses is in accord with those of well known enzyme-substrate systems. With the exception of the capacity to react with viruses, altered mucoprotein did not differ from the native substance relative to any of the properties examined in the present study. That certain physicochemical properties of the altered mucoprotein are different from those of the native substance is demonstrated in succeeding papers (34, 35).
Animals↗
Studies on serum mucoproteins in patients with urinary calculi.
A significant increase in serum mucoproteins in stone patients has been observed previously. The present study describes the variation of the constituents of mucoproteins obtained on hydrolysis. The serum mucoproteins of 31 patients with urinary calculi (13 with kidney stone, 7 with bladder stone and 11 with stones in other sites) were analysed and compared with that of 15 healthy control subjects, who had no personal or family history of calculi. The mucoproteins, glycosylated serum proteins, hexosamine and sialic acid were increased in all patients irrespective of the site of stone, while uronic acid decreased as compared with the control subjects. Serum fucose increased in all patients except in kidney stone formers. Uronic acid decreased in all stone formers irrespective of the site of the stone. It is suggested that a different type of mucoprotein is present in such patients.
Adolescent↗
Effects of chondroitin sulphate, human serum albumin and Tamm-Horsfall mucoprotein on calcium oxalate crystallization in undiluted human urine.
The effects of physiological concentrations of chondroitin sulphate, human serum albumin and Tamm-Horsfall mucoprotein on the crystallization of calcium oxalate in undiluted, ultrafiltered human urine were investigated using particle size analysis and scanning electron microscopy. Neither the amount of oxalate required to induce detectable calcium oxalate crystal nucleation nor crystal morphology was affected by the presence of any of these macromolecules. Chondroitin sulphate had no effect on the amount of crystalline material deposited or on the size of the particles precipitated in response to a standard oxalate load. Human serum albumin slightly reduced the size of the crystal aggregates and caused a small increase in the amount of crystal matter precipitated. By contrast, Tamm-Horsfall mucoprotein significantly inhibited crystal aggregation and markedly increased the volume of matter deposited, although this could not be attributed to a promotion of solute precipitation. It was concluded that chondroitin sulphate, human serum albumin and Tamm-Horsfall mucoprotein cannot account for the inhibitory effects of macromolecules with a relative mass greater than 10 kDa in spun and filtered urine. Nonetheless, Tamm-Horsfall mucoprotein is likely to inhibit crystal aggregation in whole urine in vivo and may therefore be instrumental in preventing calcium oxalate stone formation.
Adult↗
Biosynthesis of intestinal mucins. Effect of puromycin on mucoprotein biosynthesis by sheep colonic mucosal tissue.
1. Surviving sheep colonic mucosal tissue incorporated l-[U-(14)C]threonine when incubated in Krebs medium III at 37 degrees in an atmosphere of oxygen, into a well-characterized mucoprotein fraction, isolated by papain digestion of the incubated scrapings. 2. Acidic hydrolysis and chromatography of the labelled mucoprotein showed that threonine was the only constituent to become labelled. In the presence of puromycin the incorporation of l-[U-(14)C]threonine was considerably diminished (6.7 and 18.5% of control in duplicate experiments). Furthermore, puromycin also decreased incorporation of radioactivity from d-[U-(14)C]-glucose (48.0 and 31.6% of control) and (35)SO(4) (2-) (21.2 and 23.6% of control) into the mucoprotein fraction. 3. In a puromycin-inhibited system, with d-[U-(14)C]-glucose, where the overall specific radioactivity of the mucoprotein was 48% of control, the labelling of the individual monosaccharide constituents (as% of control) was: N-acetylneuraminic acid, 44%; N-glycollylneuraminic acid, 61%; hexosamines, 46%; fucose, 68%; galactose, 34%.
Animals↗
[N-acetyl-beta-D-glucosaminidase (NAG) activity in human semen: its relation to gamma-glutamyl transpeptidase (gamma-GTP) activity in seminal plasma and reproductive tissues, and relation between seminal mucoprotein concentration and seminal NAG, and gamma-GTP activities].
N-Acetyl-beta-D-glucosaminidase (NAG) and gamma-glutamyl transpeptidase (gamma-GTP) activities in seminal plasma obtained from male infertile patients and these activities in reproductive tissues obtained from cryptorchids and patients with bladder tumors were studied. Seminal mucoprotein concentration was also measured. The mean NAG and gamma-GTP activity in seminal plasma was 2,092 +/- 794 mU/ml and 10,942 +/- 4,179 mIU/ml, respectively. The mean seminal mucoprotein concentration was 28.0 +/- 5.7 mg/ml. In seminal plasma, a significant correlation was obtained between NAG and gamma-GTP (p less than 0.001). and between gamma-GTP and mucoprotein concentration (p less than 0.05). However, there was no correlation between NAG and mucoprotein concentration. In the reproductive tissue high gamma-GTP activity was observed in the testicular tissue and in the external gland of the prostate. The activity in the epididymis was higher in the tail than in the head. High NAG activity was observed in the epididymal head and in the internal gland of the prostate. In the testicular tissue, NAG activity was low. These findings showed that in the seminal plasma NAG and gamma-GTP activities were closely related but in the reproductive tissue, these activities located in different areas.
Acetylglucosaminidase↗
Co-purification of gastric mucoproteins with DNA: an explanation for the reported 'interaction' of omeprazole with DNA in rat tissues.
Recently, Phillips et al. reported that small amounts of radioactivity derived from [14C]omeprazole were 'associated' with DNA purified from gastrointestinal tissues of treated rats (Mutagenesis 7, 277-283, 1992). We hypothesized that this radioactivity arose from omeprazole bound to contaminating protein in the DNA fraction (Mutagenesis 7, 395-396, 1992). Using rats injected with 35S-labeled amino acids, we found significant protein contamination (0.06 microgram of protein per microgram of DNA) in DNA purified from gastrointestinal tissues. Gastric mucous proteins represent likely candidates for binding of omeprazole in the rat model used by Phillips et al. To investigate this, we partially purified proteins from gastric mucus, incubated them with [14C]omeprazole, and then added these radiolabeled mucoproteins to homogenates of rat colon and duodenum before starting the DNA purification. Detectable amounts of the added mucoproteins remained in the DNA fraction, but none of the control protein, bovine serum albumin, remained with the DNA. Further characterization of the mucoproteins by hydroxyapatite chromatography indicated that a certain population of these proteins survived the DNA purification procedures. These data indicate that the association of omeprazole with DNA reported by Phillips et al. most probably is explained by binding of omeprazole to mucous glycoproteins (or other proteins present in the GI tract) that selectively survive DNA purification protocols.
Amino Acids↗