Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Call number: QZ208:158
    Keywords: Neoplasms / genetics ; Genomics ; Precision Medicine ; Biomarkers, Tumor
    Pages: xxii, 698 pages : illustrations
    ISBN: 9780128117859
    Signatur Availability
    QZ208:158 available
    BibTip Others were also interested in ...
  • 2
    ISSN: 1573-2592
    Keywords: Idiotypes (Ids) ; anti-Ids ; anti-F(ab′)2 antibodies ; systemic lupus erythematosus ; autoantibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Human IgG antibodies reacting with antigenic determinants on F(ab′)2 fragments represent generic antiidiotypic antibodies present in the serum of normal individuals. Additionally, the titers of these antibodies in the sera of patients with systemic lupus erythematosus (SLE) are inversely related to disease activity. Because these autoantibodies recognize predominantly light chain-related epitopes, especially λ type, we synthesized constant (C)λ- and variable (V)λ-related overlapping 7-mer peptides on polypropylene pins to determine anti-F(ab′)2-reactive epitopes on humanλ light chains. ELISA reactivity of affinity-purified anti-F(ab′)2 antibodies obtained from normal individuals and from patients with SLE, as well as murine anti-human light-chain monoclonal antibodies specific for Cλ and Vλ subgroup-related determinants, was tested using the overlapping 7-mers of humanλ light-chain sequence. The patterns of reactivity against Cλ-related peptides were similar in both normal and SLE-derived anti-F(ab′)2 antibodies. However, reactivity profiles against Vλ-related peptides were distinctively different between the normal and the SLE-associated anti-F(ab′)2 autoantibodies. A decrease in reactivity among the SLE IgG anti-F(ab′)2 antibodies was noted for particular amino acid Vλ complementarity-determining region (CDR) residues, including glycine at positions 27 and 54, alanine at 16 and 37, and tyrosine at 28 and 91. This different pattern of reactivity from normal may indicate that in SLE there is a failure of antiidiotypic control mechanisms, as reflected by a defect in production of antibody to immunodominant Vλ CDR residues.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1573-2592
    Keywords: HIV infection ; CD4 receptor ; anti-T-cell antibodies ; T-helper defect
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Isotype and binding characteristics of T cell-reactive antilymphocyte antibodies (ALA) were investigated in 287 human immunodeficiency virus (HIV)+ sera from patients with CDC II to IVC clinical disease. Using purified soluble T-lymphoblast (CEM cell line) membranes and an ELISA method, 29 HIV+ sera showed significant reactions with this substrate and a selective expression of IgG-ALA was detected in 7 HIV+ sera. Subsequent microcytotoxicity assays, utilizing peripheral T lymphocytes and CEM cells as targets, demonstrated no significant cytotoxic capability in such sera, whereas 12 of 17 HIV+ serum samples with IgM-ALA ELISA reactivities showed a significant degree of killing in the Terasaki test. Further experiments of saturation of CD4 molecules on CEM extract by OKT4 monoclonal antibody (MoAb) induced a high inhibition of IgG-ALA binding to the T-cell membranes in only two IgG-ALA+ sera (No. 93, CDC III; No. 179, CDC II stage). Conversely, treatment of CEM membrane lysate with Leu3a MoAb, specific for the gp120 reactive domain of the HIV receptor, failed to prevent membrane binding in all seven of the IgG-ALA+ sera. Following the adsorption of serum 93 on a T-cell membrane antigen affinity column, SDS-PAGE analysis demonstrated that the predominant ALA material reacting with T-cell membranes was IgG with no detectable traces of IgM. These data provide evidence that ALA in HIV+ patients may be simultaneously or selectively expressed as IgG and/or IgM with different properties. While IgM-ALA show predominant cytotoxic activity, IgG-ALA may include anti-CD4 molecules. However, IgG binding to the C-terminal domain of native HIV receptor appears to occur at a lower rate than IgM-ALA in HIV infection.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1573-2592
    Keywords: Anti-F(ab′)2 ; 16/6 idiotype ; systemic lupus erythematosus (SLE) kindreds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Levels of serum anti-F(ab′)2 antibodies and expression of the 16/6 anti-DNA idiotype were studied in 103 sera from first-degree relatives of 17 systemic lupus erythematosus (SLE) kindreds. Among healthy SLE relatives, 35.9% showed anti-F(ab′)2 elevations and 24%, Id 16/6 expression. Forty-three and two-tenths percent of healthy SLE relatives with elevated anti-F(ab′)2 also showed expression of 16/6; when Id 16/6 was positive, 16 of 25 relatives (64%) showed parallel elevations of anti-F(ab′)2. However, within individual families, distribution patterns of elevated anti-F(ab′)2 and Id 16/6 often did not coincide. Affinity-isolated anti-F(ab′)2 from four members of a single SLE kindred showed relative enrichment for Id 16/6 in only two of the four individuals studied. Moreover, none of the isolated anti-F(ab′)2 antibodies within this kindred or another kindred showing 16/6 Id expression reacted directly with 16/6 Id. Our studies suggest that whereas both anti-F(ab′)2 and Id 16/6 are increased within SLE kindreds, expression of the two does not always coincide. Furthermore, anti-F(ab′)2 antibodies do not show direct reactivity with Id 16/6. A number of anti-DNA idiotypic markers may play a role in idiotypic networks among such SLE kindreds.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...