يعرض 1 - 10 نتائج من 27 نتيجة بحث عن '"Brouns, Gaby"', وقت الاستعلام: 0.98s تنقيح النتائج
  1. 1
    دورية أكاديمية
  2. 2
    دورية أكاديمية

    مصطلحات موضوعية: Articles

    الوصف: The B cell antigen receptor (BCR) complex consists of transmembrane (m) Ig, in non-covalent association with a disulphide-linked heterodimer of mb-1 and B29 gene products. The MB-1—B29 heterodimer is required for deposition of the BCR at the plasma membrane, as well as for coupling of the antigen receptor to intracellular signal transduction cascades. We have performed biosynthetic labelling studies using the mature B cell line Ramos to investigate the process of assembly of the BCR components. We conclude that association of the four components, Ig-heavy chain (HC) and -light chain (LC), MB-1 and B29, is required and sufficient to permit exit of the BCR complex out of the endoplasmic reticulum (ER). With the short pulse labelling procedures used, no evidence was found for transient participation of other molecules in complex formation. A 32 kDa glycoprotein was identified, which is serologically related to MB-1, but has a more acidic isoelectrlc point (pl) and a protein backbone of 21 kDa, as compared with 25 kDa for MB-1. This protein did not appear to participate in BCR complex formation and is most likely degraded prior to reaching the cis -Golgi. The MB-1 component was found to be the rate-limiting step in BCR complex formation, while Ig-HC, -LC and B29 are synthesized in excess. Ig-HC and -LC form disulphidelinked tetrameric complexes within 3 min after biosynthesis, with which B29 and MB-1 components associate independently, followed by disulphide bond formation between these heterodimeric partners. While partial BCR complexes containing B29 and mIg-H 2 L 2 tetramers are rapidly formed and have a half-life of a few hours in the ER, entry of MB-1 into these complexes controls exit out of this compartment.

    وصف الملف: text/html

  3. 3
    دورية أكاديمية

    العلاقة: Schwickerath, Oliver, Brouns, Gaby, Thrasher, Adrian, Kinnon, Christine, Roes, Jürgen and Casimir, Colin (2004) Enhancer-deleted retroviral vectors restore high levels of superoxide generation in a mouse model of CGD. Journal of Gene Medicine, 6(6), pp. 603-615. ISSN (print) 1099-498X

  4. 4
    دورية أكاديمية
  5. 5
    دورية أكاديمية
  6. 6
    دورية أكاديمية
  7. 7
    دورية أكاديمية
  8. 8
    دورية أكاديمية
  9. 9
    دورية أكاديمية

    المصدر: European Journal of Immunology ; volume 23, issue 5, page 1088-1097 ; ISSN 0014-2980 1521-4141

    الوصف: Prior to immunoglobulin (Ig) light (L) chain rearrangement, pre‐B cells can express μ heavy (H) chains at the cell surface in association with pseudo (ψ) L chains. This complex may be essential for B cell development. We have investigated the composition of the μ/ψL chain complex of a human pre‐B cell line, in view of its potential role in transmembrane signal transduction. The μ/λ. receptor of a mature B cell line was analyzed in comparison. The μ/ψL chain complex is associated with disulfide‐linked molecules that are homologous or identical to the mb‐1 and B29 proteins, known to be integral components of membrane Ig receptors on mature B cells. Both receptors contain tyrosine (Tyr) kinase activity. In the μ/λ receptor, the lyn and lck Tyr kinases could clearly be identified. The mb‐1 and B29 proteins in both μ/λ and μ/ψL chain receptors are substrates for in vitro phosphorylation on Tyr, but also on serine (Ser) and threonine (Thr) residues. The undefined μ‐associated Ser/Thr kinase also phosphorylates the sre‐related kinases in the μ/λ, receptor and a 43‐kDa μ‐associated protein that is present in both complexes. The 43‐kDa protein may be an integral part of both receptor types, or a transiently associated molecule instrumental in the signaling process. We conclude that the μ/ψL receptor on human pre‐B cells fulfills the presently known criteria to function as a signal transduction unit.

  10. 10
    دورية أكاديمية