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Biomedical subjects

I Olsen

Publications and source records attributed to I Olsen.

At least 181 records · Page 10Linked to original sources
PubMed1988

Ultrastructural localization of a lysosomal enzyme in resin-embedded lymphocytes.

The intracellular distribution of lysosomal enzymes in lymphocytes has previously been only poorly defined, mainly by cytochemical procedures of low resolution. In the present study we have used a post-embedding immunogold technique to identify the precise ultrastructural localization of a lysosomal enzyme, beta-glucuronidase, in activated lymphocytes embedded in Lowicryl K4M resin. We show that this enzyme is present in the rough endoplasmic reticulum, in the Golgi complex, and in vesicular organelles which probably include lysosomes.

Animals↗
PubMed1988

Lymphocytes transfer only the lysosomal form of alpha-D-mannosidase during cell-to-cell contact.

We have examined the changes in the activities of the different types of alpha-D-mannosidase when fibroblasts from patients deficient in the lysosomal form of the enzyme are cultured together with normal lymphocytes. Our results show that whereas the mannosidosis cells acquired high levels of this enzyme, the activities of both the Golgi and the endoplasmic reticulum forms of alpha-D-mannosidase remained the same as in the fibroblasts cultured alone in the absence of lymphocytes. The increase in the activity of the lysosomal enzyme in the cocultured fibroblasts was not affected by the presence of mannose 6-phosphate or alpha-methyl mannoside, inhibitors of receptor- and lectin-mediated uptake of lysosomal enzymes, respectively, but it did require cell-to-cell contact. Ion-exchange HPLC and electrophoresis in polyacrylamide gradient gels showed that the acquired enzyme had the same elution profile and molecular size as the lysosomal form of the enzyme present in the lymphocytes. Immunoprecipitation studies using antibody specific for the lymphocyte type of lysosomal alpha-D-mannosidase confirmed that the increased activity in the cocultured mannosidosis cells resulted from the acquisition of the lymphocyte enzyme. Cytochemical examination revealed, however, that the transferred lymphocyte enzyme was localized in cytoplasmic organelles in the peripheral regions of the recipient fibroblasts. These results show that lymphocytes transfer only the lysosomal form of alpha-D-mannosidase during cell-to-cell contact with mannosidosis cells.

Animals↗
PubMed1988

Forms and intracellular distribution of alpha-D-mannosidases in murine liver and spleen.

1. The intracellular distribution of alpha-D-mannosidase in homogenates of murine liver and spleen was investigated by differential and gradient density centrifugation. 2. In both tissues an enzyme with a neutral pH optimum was found in the cytosol together with an alpha-D-mannosidase with optimal activity between pH 5.5 and 6.0 which was also partially membrane-bound. 3. In liver the acidic alpha-D-mannosidase was obtained almost entirely in a particulate form distributed equally between a heterogeneous low density region and heavy density lysosomes. 4. The lysosomal form of the liver enzyme was purified to electrophoretic homogeneity and shown to be a glycoprotein composed of four identical subunits of molecular weight 65 kDa. 5. Antibody raised against the purified liver alpha-D-mannosidase immunoprecipitated a polypeptide from spleen which had the same molecular size. This acidic enzyme was the predominant type of alpha-D-mannosidase in spleen, but in contrast to liver, it was obtained mainly in a cytosoluble form, the remaining activity being present in the heterogeneous light density compartment. 6. Although both tissues contain the same molecular form of the acidic alpha-D-mannosidase, in murine spleen this enzyme does not appear to be associated with stable heavy density lysosomes.

Animals↗
PubMed1988

Ultrastructural studies of a lysosomal enzyme during lymphocyte activation.

A post-embedding immunogold technique has been used for the ultrastructural localization of a lysosomal enzyme, beta-glucuronidase, in resting and activated T- and B-lymphocytes. The results presented here show that mitogen-induced stimulation of T- and B-cells was associated with an increase in the amount of enzyme in the Golgi complex and rough endoplasmic reticulum, organelles which were rarely present in the resting lymphocytes.

Animals↗
PubMed1988

Adhesion of T and B lymphocytes to fibroblasts in tissue culture.

We have examined the direct interaction of lymphocytes with human fibroblasts in vitro. The results of our study, using radiolabelled lymphocytes, show that activated T cells rapidly adhered to the fibroblasts when the two types of cell were cultured together at 37 degrees, and that the residency time of lymphocyte-fibroblast contact was approximately 30 min. Lymphoblast adhesion did not require the presence of divalent cations, but it was temperature-dependent. Although the binding of the lymphocytes was not prevented by the presence of monosaccharides or by treatment with exoglycosidases, it was highly sensitive to low concentrations of trypsin. Attachment was also inhibited partially in the presence of the sulphated fucose polysaccharide, fucoidan. These results suggest that at least two distinct receptors are involved in lymphocyte adhesion to fibroblasts. The binding of B lymphoblasts to fibroblasts was much greater than that of the activated T cells. Resting, non-stimulated, B and T lymphocytes both bound only very poorly, showing that only mature lymphocytes express high levels of functionally effective adhesion proteins. Moreover, the results of competition experiments suggest that different cell surface components mediate the interaction of T and B cells with fibroblasts.

B-Lymphocytes↗
PubMed1987

Multiple transfer of lysosomal enzymes from normal lymphocytes to I-cell disease fibroblasts.

Cells from patients with inherited lysosomal deficiency diseases can acquire the missing lysosomal enzyme by direct cell-to-cell transfer from normal lymphocytes. Cells from I-Cell Disease (Mucolipidosis type II; ICD) patients are simultaneously deficient in many lysosomal enzymes due to an inborn error of glycoprotein processing. In this study we show that such cells acquire high levels of several of the missing lysosomal enzymes when they are cultured in contact with lymphocytes. Moreover, the present results also show that enzyme levels in the donor lymphocytes are not depleted but increase during cell contact with the fibroblasts.

Animals↗
PubMed1987

Association between bacteriophage-infected Actinobacillus actinomycetemcomitans and rapid periodontal destruction.

Actinobacillus actinomycetemcomitans was isolated from periodontal pockets in a patient suffering from prepubertal periodontitis. Electron microscopy revealed 3 different groups of bacteriophages in filtrates of subgingival plaque from all the active periodontal lesions. Phage infected A. actinomycetemcomitans in this patient was restricted to periodontal pockets which, according to standardized roentgenograms, had shown bone destruction during the past 12 months. A follow-up study of 7 months revealed that a "burned out" site which harbored noninfected A. actinomycetemcomitans, turned into an active site at the same time as the A. actinomycetemcomitans of that site became infected with the phages. These findings indicate a relationship between rapid prepubertal periodontal destruction and phage-infected A. actinomycetemcomitans.

Actinobacillus↗
PubMed1987

The presence of phage-infected Actinobacillus actinomycetemcomitans in localized juvenile periodontitis patients.

Electron microscopy revealed 2 different types of bacteriophages isolated from Actinobacillus actinomycetemcomitans colonizing exclusively diseased sites in 4 patients with localized juvenile periodontitis (LJP). All sites infected with phage were undergoing periodontal destruction, as judged from consecutive routine radiographs. The phages isolated had a wide host range as assessed from their ability to infect a series of reference strains of A. actinomycetemcomitans. A 5th patient harboured non-infected A. actinomycetemcomitans in a surgically treated site which had undergone no bone destruction during the last 12 months. The present findings suggested that the pathogenic potential of A. actinomycetemcomitans in LJP may increase due to phage infection.

Actinobacillus↗
PubMed1987

Salivary IgG, a parameter of periodontal disease activity? High responders to Actinobacillus actinomycetemcomitans Y4 in juvenile and adult periodontitis.

The concentration of salivary IgG and IgA and the levels of salivary IgG and IgA antibodies to Actinobacillus actinomycetemcomitans Y4 were measured by ELISA in 205 persons including patients with juvenile and adult periodontitis as well as healthy subjects. Compared to the concentration observed in subjects with a healthy periodontium, a significantly increased concentration of salivary IgG was found in 34% of the patients with moderate adult periodontitis and in 57% of the patients with severe adult periodontitis. The level of salivary IgA was less influenced by the periodontal condition. The level of salivary IgG antibody to A. actinomycetemcomitans was significantly elevated in 55% of the patients with untreated juvenile periodontitis and in 28% of the patients treated for JP. 28% of the patients with adult periodontitis had a significantly elevated level of IgG antibody to A. actinomycetemcomitans Y4. Significantly elevated levels of IgA antibody to this bacteria was found less frequently, 27% in untreated JP, 20% in treated JP and 17% in adult periodontitis.

Actinobacillus↗
PubMed1987

Bacteriophage infection--a possible mechanism for increased virulence of bacteria associated with rapidly destructive periodontitis.

We have recently isolated several groups of bacteriophages infecting Actinobacillus actinomycetemcomitans from periodontal lesions in patients with rapidly destructive periodontitis. Bacteriophage infection of these bacteria in these patients was restricted to periodontal pockets showing radiographic evidence of recent bone loss and suggests an association between phage-infected A. actinomycetemcomitans and active periodontal disease. On the basis of the biological activity of bacteriophages we propose a working hypothesis to explain the mechanism by which a phage may increase bacterial virulence in periodontal disease.

Actinobacillus↗
PubMed1986

Chemotaxonomy of selected species of the Actinobacillus-Haemophilus-Pasteurella group by means of gas chromatography, gas chromatography-mass spectrometry and bioenzymatic methods.

Instrumental analytical and bioenzymatic methods were used to differentiate between species of the Actinobacillus-Haemophilus-Pasteurella group. Long-chain fatty acids were analysed directly with gas chromatography (GC) without derivatization. GC of trifluoroacetylated whole-cell methanolysates was a rapid method for differentiation. Cellular sugars were more suitable for differentiation than fatty acids. D-Glycero-D-mannoheptose, the major localization of which was lipopolysaccharide, distinguished H. aphrophilus from A. actinomycetemcomitans, H. paraphrophilus, H. influenzae type b, P. haemolytica, P. multocida, and P. ureae. GC of single colonies, which is a new chemotaxonomic method, was preferable to GC of liquid-grown cells. Lysozyme-and EDTA-induced bacteriolysis and reduction of methylene blue by cellular hydrogenase served as additional criteria for differentiation.

Actinobacillus↗