Library

feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 55 (2002), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Several models are proposed for T-cell antigen receptor (TCR) assembly and structure. However, there is little experimental data favouring directly either one or the other(s). The minimal complex appears to be composed of a TCRαβ/CD3δε,γε/ζ2 structure but at the cell membrane, multimers of this minimal structure may be formed. Quantitative cytofluometry has suggested three CD3ε chains for two TCRβ (or TCRδ) chains/complex. Such data should be repeated with monoclonal antibodies (MoAb) against extracellular (EC) parts of CD3δ or CD3γ chains. In the present review, we have compared the TCR/CD3 assembly of pre-TCR, TCRγδ and TCRαβ containing complexes, and analysed the reactivity of antibodies (Abs) against the EC part of CD3δ chains. Our data suggest an alternative assembly pathway and structure of TCR/CD3 complexes.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 54 (2001), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The present study was performed in order to analyze whether T-cell receptor (TCR)/CD3 assembly, intracellular transport and surface expression are carried in a similar way in αβ-and γδ-T cells. By means of optimal immunoprecipitation conditions with 35S-methionine/cysteine- or biotin-labelled TCR/CD3 proteins from αβ- or γδ-T-lymphoma-cell lines, as well as TCRγδ cDNA transfectants, it was found that CD3δ chains associate less strongly with TCRγδ heterodimers compared to TCRαβ heterodimers. This preferential reactivity of CD3δ chains appears to be structural and not owing to differences in γδ- versus αβ-T-cell intracellular environments. Our results are in accordance firstly, with data from CD3δ-deficient mice, which have γδ-T cells but no αβ-T cells, secondly with the suggested role of CD3δ chains in the positive selection of αβ-T cells, a process apparently not followed by γδ-T cells, and lastly with the differential roles of CD3δ chains versus CD3γ chains, explaining the maintenance of two CD3δ and CD3γ genes after the duplication from a CD3δ/γ gene present in avians. The impaired reactivity of CD3δ chains with TCRγδ heterodimers seems to be owing to a less efficient association with TCRγ chains. In contrast, CD3δ chains interact as strongly with TCRδ chains as do CD3γ chains with both TCRγ and TCRδ chains. These data may explain, at the molecular levels, why surface TCR/CD3 expression levels are impaired in γδ-T cells from CD3γ-deficient mice but not from CD3δ-deficient mice.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...