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Biomedical subjects

E Shapira

Publications and source records attributed to E Shapira.

At least 55 records · Page 3Linked to original sources
PubMed1985

The "muscular variant" of Pompe disease: clinical, biochemical and histologic characteristics.

We report on a 2-yr-old boy with progressive muscular weakness and respiratory failure. There was no clinical evidence of heart muscle involvement. Autopsy showed marked intralysosomal glycogen deposition in skeletal muscle and liver with no histological evidence of glycogen deposition in cardiac muscle. The activity of the lysosomal enzyme alpha-1,4-glucosidase was deficient in skin fibroblasts, skeletal muscle, cardiac muscle, and liver; however, the enzymatic activity in peripheral blood leukocytes was in the low normal range. The child's mother had normal enzymatic activity in leukocytes but heterozygote levels in skin fibroblasts.

Child, Preschool↗
PubMed1985

Alterations in the time of X chromosome replication induced by 5-azacytidine in a patient with 48,XXXY/47,XXY.

It has recently been shown that 5-azacytidine (5-azaC) can induce altered replication patterns of the late-replicating X chromosome in normal female cells. This has been demonstrated by bromodeoxyuridine labelling of cells late in the S phase. In the present study the same method was applied to the lymphocytes of a Klinefelter patient (48,XXXY/47,XXY). Significant 5-azaC-induced changes in the replication of the entire inactive X chromosome, from late to early, were found in the lymphocytes of this patient. These results indicate that hypomethylating agents can not only alter the replication of individual bands, but also change the gross replication schedule of multiple inactive X chromosomes in the presence of a Y chromosome.

Azacitidine↗
PubMed1985

Marinesco-Sjögren syndrome: evidence for a lysosomal storage disorder.

The inherited abnormality of the Marinesco-Sjögren syndrome is not known. We studied four patients from two different families and ethnic groups. Electron microscopic studies revealed numerous, abnormally enlarged lysosomes that contained whorled lamellar or amorphous inclusion bodies. Enzyme studies excluded previously described lysosomal storage disorders.

Cataract↗
PubMed1984

A purified serum glycopeptide from controls and cystic fibrosis patients. III. The association of the ciliary dyskinetic activity with the oligosaccharide component.

We have previously described the purification and partial characterization of a serum glycopeptide with mucociliary activity from cystic fibrosis patients and a normal counterpart from sera of controls (3, 4). After removal of its oligosaccharide component by beta-elimination, the peptide portion of the glycopeptide from cystic fibrosis patients did not reveal any mucociliary activity on rabbit tracheal explants. This mucociliary activity was shown to be inhibited by mannose, glucose, and N-acetyl-galactosamine as well as by the glycopeptide purified from controls. It was not affected by xylose, fucose, galactose, or N-acetyl-glucosamine.

Animals↗
PubMed1982

Increased binding of limulin to alpha 2-macroglobulin and immunoglobulin M from cystic fibrosis patients.

In the present study the binding of limulin, a lectin with sialic acid specificity, to three serum glycoproteins from controls and cystic fibrosis patients was compared. alpha 2-Macroglobulin from patients with cystic fibrosis was shown to have significantly increased binding to the lectin limulin when compared to that from healthy controls (t = 3.6, p less than 0.01). The binding of limulin to immunoglobulin M (IgM) from cystic fibrosis patients was also shown to be significantly higher than the binding to IgM from controls (t = 3.6, p less than 0.01), whereas no detectable binding of fluorescein-conjugated limulin to immunoglobulin G from either cystic fibrosis patients or controls was observed. These findings support the hypothesis that the underlying inherited defect in cystic fibrosis might be an abnormal synthesis or degradation of glycoproteins and glycopeptides.

Binding, Competitive↗
PubMed1982

A purified serum glycopeptide from controls and cystic fibrosis patients. I. Comparison of their mucociliary activity on rabbit tracheal explants.

A glycopeptide with a molecular weight of approximately 5000 was purified from sera of controls and cystic fibrosis patients. Both the cystic fibrosis and control glycoproteins revealed the absence of aromatic amino acids. The effect of the purified glycopeptide on rabbit tracheal explants was examined in a double-blind fashion. The purified fraction from cystic fibrosis patients caused marked ciliary dyskinetic activity and profound mucus secretion. The equivalent fraction from controls, even in a 50-fold higher concentrations, showed no apparent biological activity on rabbit tracheal explants.

Adolescent↗
PubMed1982

Enzymatic and immunologic quantitation of erythrocyte superoxide dismutase in adults and in neonates of different gestational ages.

Human erythrocyte superoxide dismutase (SOD) was purified and specific antiserum was raised in rabbits. Enzyme preparations from adults and from newborns were shown to be indistinguishable in their immunologic and electrophoretic properties. Erythrocyte SOD was quantitated in blood specimens from adults and in cord blood specimens from neonates of different gestational ages, using both an immunologic and an activity assay. The mean values of SOD concentration and SOD activity for adults and for newborns of average size for gestational age (AGA) showed no significant difference. Adult red cells contained 28.0 +/- 8.3 SOD units/mg hemoglobin (Hgb) whereas AGA neonatal red cells had 28.5 +/- 8.3 SOD units/mg Hgb. Immunologic quantitation by single radial immunodiffusion revealed 0.69 +/- 0.07 micrograms SOD/mg Hgb in adults and 0.70 +/- 0.14 micrograms SOD/mg Hgb in the AGA neonates; however, the SOD concentrations from both small for gestational age (SGA) and large for gestational age (LGA) neonates were significantly lower than those of the AGA neonates and the adults (SGA: 0.57 +/- 0.24 micrograms SOD/mg Hgb, P less than 0.05; LGA: 0.59 +/- 0.16 micrograms SOD/mg Hgb, P less than 0.05).

Adult↗
PubMed1982

A purified serum glycopeptide from controls and cystic fibrosis patients. II. Comparison of their immunologic properties using monoclonal antibodies.

The immunogenic and antigenic properties of the cystic fibrosis glycopeptide and its normal counterpart were compared. BALB/c mice were immunized with either the cystic fibrosis glycopeptide or its normal counterpart and their spleen cells fused with X63NS1/1-Ag-4 (NS1) mouse myeloma cells. Four hybridization experiments (two with each glycopeptide) were performed in which different plating methods and screening assays were evaluated. Although an identical immunization procedure was used, 51 hybridoma cultures producing specific antibodies to the control glycopeptide and only 11 producing antibodies to the cystic fibrosis glycopeptide were obtained. Many of the monoclonal antibody preparations showed specificity toward the carbohydrate moiety of the glycopeptides and crossreacted immunologically with various glycoprotein preparations, whereas some were specific to the glycopeptides. The antibodies from the cloned hybridomas specific to the glycopeptide were used to compare serum fractions from controls and cystic fibrosis patients (10 samples in each group). Indistinguishable immunologic reactivity (antigenicity) between the controls and cystic fibrosis patients was demonstrated with the various monoclonal antibodies so far evaluated.

Adolescent↗
PubMed1980

Cell-directed inhibition of polymorphonuclear leukocyte chemotaxis in a patient with mucocutaneous candidiasis.

A patient with mucocutaneous candidiasis and impaired polymorphonuclear leukocyte (PMN) chemotaxis is described. The patient's PMN chemotaxis was markedly decreased in the presence of autologous plasma but normal in control plasma. Cell-directed inhibitory activity was found in whole patient plasma as well as the 40% ammonium sulfate precipitate fraction of both the patient's and the control plasma. The inhibitor was heat stable, reversible, nondialyzable, eluted from DEAE cellulose with 0.005 M sodium phosphate buffer, and migrated with IgG on immunoelectrophoresis. The supernate from 40% ammonium sulfate-fractionated patient and control plasma contained a cell-directed enhancer of PMN chemotaxis that antagonized the cell-directed inhibitor activity. It is possible that the patient's chemotactic defect may be caused by imbalance between plasma factors that regulate chemotaxis.

Ammonium Sulfate↗
PubMed1980

Immunoquantitation of Hageman factor in urine and plasma of children with nephrotic syndrome.

Children with nephrotic syndrome frequently have decreased plasma levels of Hageman factor (factor XII). Studies were designed to determine whether this finding results primarily from a loss of Hageman factor in the urine or is related to an alteration in the Hageman factor protein itself. A monospecific anti-Hageman factor goat antibody was prepared and used for quantitative measurements of Hageman factor in urine and plasma by a radial immunodiffusion method. Samples of 24 hr urine collections from 14 children with nephrotic syndrome were examined by this immunoassay technique; no Hageman factor was detected in the urine in 13/14 patients. Comparative studies using plasma from the nephrotic syndrome patients and nine normal controls demonstrated: (1) a significantly reduced level of Hageman ACT in the nephrotic syndrome patients (p < 0.001); (2) a reduction to a lesser degree of the levels of CRM in the same group (p < 0.001); and (3) a significantly increased CRM/ACT ratio in the plasma of the patients with nephrotic syndrome (p < 0.01) indicating partial inactivation of the Hageman factor enzymatic function. However, no inhibitory activity to added Hageman factor could be detected in the plasma or urine of the patients. These findings indicate that the decreased plasma Hageman factor activity that accompanies the nephrotic syndrome cannot be adequately explained by simple urinary loss of Hageman factor as has previously been suggested.

Adolescent↗
PubMed1979

Is multiple sulphatase deficiency due to defective regulation of sulphohydrolase expression?

Multiple sulphatase deficiency disease is an unusual autosomal recessive disorder characterised biochemically by a deficiency of several sulphohydrolase activities. The laboratory diagnosis of this combined neurological connective tissue disorder is made on the basis of decreased activities of the lysosomal enzymes, arylsulphatase A and arylsulphatase B and the microsomal enzyme, arylsulphatase C. The primary defect in this multi-enzyme deficiency has not been identified. Using immunological techniques to characterise further the residual activities of arylsulphatases A and B in the multiple sulphatase deficiency disease, we have examined the levels of cross-reaching material (CRM) to arylsulphatases A and B in cultured skin fibroblasts from controls and patients with multiple sulphatase deficiency, metachromatic leukodystrophy (deficiency of only arylsulphatase A activity) and Maroteaux-Lamy syndrome (deficiency of only arylsulphatase B activity). We report here results indicating that arylsulphatases A and B in multiple sulphatase deficiency are reduced in their levels of CRM while retaining a normal activity/CRM ratio. Because the two enzymes are apparently structurally unrelated, these data are consistent with the possibility that their combined deficiencies in this disorder may result from a defect in the coordinated expression of sulphohydrolases.

Arylsulfatases↗
PubMed1979

The effect of some protease substrates and inhibitors on chemotaxis and protease activity of human polymorphonuclear leukocytes.

Both low- and high-molecular-weight inhibitors of serine proteases were found to inhibit chemotaxis by human polymorphonuclear leukocytes totally at widely varying concentrations. Synthetic low-molecular-weight substrates with trypsin-like or chymotrypsin-like specificity were also shown to be potent inhibitors of chemotaxis. Chemotactic inhibition was reversible except with a titrant for the active site of a serine protease. N-acetyl-L-tyrosine ethyl ester was found to be a suitable substrate for measuring protease activity of polymorphonuclear leukocyte. Concentrations of the various protease inhibitors that caused 100% chemotactic inhibition caused 80%-100% inhibition of protease activity of polymorphonuclear leukocytes.

Benzamidines↗
PubMed1978

Immunologic studies of arylsulfatase A in normal and metachromatic leukodystrophy liver.

Purified human liver arylsulfatase A on polyacrylamide gel electrophoresis at pH 4.0 is separated into two protein forms with enzymatic activity and two distinct inactive subunits. All of these components were immunologically distinguishable using different antisera preparations. In late infantile metachromatic leukodystrophy, only one of the two inactive subunits was immunologically detected, whereas in the juvenile form of metachromatic leukodystrophy, both inactive subunits were antigenically present.

Antibody Specificity↗