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1

Digitale Medien

Polyclonal Activation of Human Peripheral Blood B Lymphocytes by Formaldehyde-Fixed Salmonella paratyphi B (1982)

CHEN, W.-Y. ; FUDENBERG, H. H. ; ADES, E. W.

Oxford, UK : Blackwell Publishing Ltd

Scandinavian journal of immunology 15 (1982), S. 0

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ISSN: 1365-3083

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: B-cell ‘activation’ in cultures stimulated with pokeweed mitogen (PWM), Staphylococcus aureus strain Cowan I, or formaldehyde-fixed Salmonella paratyphi B (SPB) was evaluated by enumeration of cells secreting immunoglobulin (Ig) and by quantitation of Ig released into culture supernatants. A dissociation between these two values was found after day 6 in cultures activated with PWM or SPB, suggesting that Ig-secreting cells (ISC) are heterogeneous in terms of Ig secretion rate. Generation of ISC in cultures activated with PWM or SPB was partially inhibited by hydroxyurea, but [g levels in culture supernatants were not affected. These results indicate that there are at least two subpopulations of ISC in stimulated peripheral blood lymphocyte cultures, one sensitive to, and the other resistant to, hydroxyurea. The hydroxyurea-resistant subpopulation appeared to be more mature and to release almost all of the Ig detected in culture supernatants. Furthermore, time-course studies of ISC numbers and Ig levels showed that each ISC in SPB-stimulted cultures (but not in PWM-stimulated cultures) was more active in Ig synthesis and secretion after day 8 than before day 6, indicating that after day 8 most of the ISC in cultures activated with SPB were hydroxyurea-resistant. These studies suggest that SPB is another useful polyclonal B-cell ‘activator’ for studies of human B-cell differentiation and function, and that SPB defines two distinct subsets of B cells.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-3083.1982.tb00646.x

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2

Digitale Medien

Immunochemical Characterization of a Human B Lymphocyte Differentiation Antigen (p65) (1980)

ADES, E. W. ; FERRONE, S. ; BALCH, C. M.

Oxford, UK : Blackwell Publishing Ltd

Scandinavian journal of immunology 12 (1980), S. 0

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ISSN: 1365-3083

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: A human B-cell differentiation antigen (BDA-1) with a molecular weight of 65,000 was Identified by use of an anti-B-cell xenoantiserum. BDA-1 was isolated by immunoprecipitation of cell lysates from a B-lymphoblastoid cell line (SB) and from blood B lymphocytes (sIg+ER−) of four normal individuals. It was not detectable in cell membrane lysates from two T-lymphoblastoid cell lines (HSB-2 and MOLT-3) or from enriched normal T cells (sIg−ER+). BDA is a singlechain molecule since its migration in SDS-PAGE gels was not altered by heating the protein to 100 C or by treatment with 2-mercaptoetbanol. Immunodepletion experiments demonstrated that the antigen recognized by anti-BDA xenoantiserum has neither structural nor antigenic relationships with la-like antigen or β-microglobulin.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-3083.1980.tb00101.x

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3

Digitale Medien

Modulation of the Immune Response by Plasma Protease Inhibitors (1982)

ADES, E. W. ; HINSON, A. ; CHAPUIS-CELLIER, C. ; [weitere]

Oxford, UK : Blackwell Publishing Ltd

Scandinavian journal of immunology 15 (1982), S. 0

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ISSN: 1365-3083

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: The two major protease inhibitors in human serum, alpha1-antitrypsin (α1AT) and alpha2-macroglobulin (α2m), were analysed for their effects on antibody-dependent cell-mediated cytotoxocity (ADCC) and natural killing (NK). The results indicate that both α1AT and α2m decrease ADCC and NK in a dose-responsive pattern.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-3083.1982.tb00628.x

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4

Digitale Medien

Modulation of the Immune Response by Plasma Protease Inhibitors (1982)

GRAVAGNA, P. ; GIANAZZA, E. ; ARNAUD, P. ; [weitere]

Oxford, UK : Blackwell Publishing Ltd

Scandinavian journal of immunology 15 (1982), S. 0

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ISSN: 1365-3083

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: In two different cytolytic assays, dose-dependent inhibition of antibody-dependent cellmediated cytotoxicity and natural killing by alpha2-macroglobulin (α2m) and its subunits was observed. α2m subunits were approximately four times more inhibitory in both assays than the native 2m molecule on a molar basis. Analysis of trypsin protein esterase activity demonstrated that α2m subunits were four times more active than the parent molecule.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-3083.1982.tb00629.x

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5

Digitale Medien

Murine Thymocytes Mediate a Natural Killer-Like Activity against Herpes Virus-Infected Target Cells but Not YAC-1 Target Cells (1986)

TANG, J. ; DELONG, D. C. ; BUTLER, L. D. ; [weitere]

Oxford, UK : Blackwell Publishing Ltd

Scandinavian journal of immunology 24 (1986), S. 0

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ISSN: 1365-3083

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: In this report, we demonstrated a natural killer (NK)-like activity against HSV-1 infected ceils mediated by CD-1 mouse thymocytes. This cytolytic activity is specific for HSV-1-infected MCN cells, since both uninfected MCN and Y AC-1 target cells are not susceptible to thymocyte lysis. Antibody plus complement depletion experiments indicate that a portion of the activity is associated with the Lyt 2 /L3T4− thymocyte subpopulation. This NK-like activity cannot be enhanced by addition of interleukin 2 in vitro.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-3083.1986.tb02075.x

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6

Digitale Medien

BIOCHEMICAL CHARACTERIZATION OF HUMAN THY-1 (1984)

Bonewald, L. ; Ades, E. W. ; Tung, E. ; [weitere]

Oxford, UK : Blackwell Publishing Ltd

International journal of immunogenetics 11 (1984), S. 0

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ISSN: 1744-313X

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Biologie , Medizin

Notizen: The human Thy-1 homologue (p25) was characterized biochemically for amino acid composition, sequence and carbohydrate content. Two other forms of the human Thy-1 molecule were detected and partially characterized. A 40,000 mol.wt. molecule (p40) is the dimer of p25 and its formation is increased by the presence of sodium dodecyl sulphate (SDS). The second form of 16,000 mol.wt. (p16) appears to be a cryptic or breakdown form of p25. Comparison of the amino acid compositions of p25, p40 and p16 isolated from MOLT-3 cells, with that deduced from the nucleotide sequence of the gene coding for part of the putative T cell antigen receptor, also from MOLT-3 cells, shows that the Thy-1 homologue is distinct from, but evolutionary related to, one of the putative T cell antigen receptor polypeptide chains.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1744-313X.1984.tb00815.x

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