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Titolo:
IgM expressed by leukemic CD5(+) B cells binds mouse immunoglobulin light chain
Autore:
Weston, KM; Tangye, SG; Dunn, RD; Smith, A; Morris, MB; Raison, RL;
Indirizzi:
Univ Technol Sydney, Dept Cell & Mol Biol, Immunobiol Unit, St Leonards, NSW 2065, Australia Univ Technol Sydney St Leonards NSW Australia 2065 s, NSW 2065, Australia
Titolo Testata:
JOURNAL OF MOLECULAR RECOGNITION
fascicolo: 4, volume: 14, anno: 2001,
pagine: 245 - 253
SICI:
0952-3499(200107/08)14:4<245:IEBLCB>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHRONIC LYMPHOCYTIC-LEUKEMIA; RHEUMATOID-FACTOR; ANTIGEN-BINDING; CD5+B CELLS; AUTOANTIBODIES; REPERTOIRE; ANTIBODIES; MECHANISM;
Keywords:
B-CLL; CD5(+) B cells; polyreactive IgM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Raison, RL Univ Technol Sydney, Dept Cell & Mol Biol, Immunobiol Unit, Sydney, NSW 2007, Australia Univ Technol Sydney Sydney NSW Australia 2007 2007, Australia
Citazione:
K.M. Weston et al., "IgM expressed by leukemic CD5(+) B cells binds mouse immunoglobulin light chain", J MOL RECOG, 14(4), 2001, pp. 245-253

Abstract

Mouse immunoglobulin (Ig) molecules have previously been shown to bind to the surface of CD5(+) B cells from patients with B-cell chronic lymphocyticleukemia (B-CLL). The results indicated that surface IgM was involved in the interaction and suggested the phenomenon was an example of the polyreactive binding capacity of the surface Ig (sIg) expressed by these malignant cells. This article describes the further characterization of the interaction between human IgM and mouse Ig molecules and subunits. Mouse Ig moleculesof both kappa and lambda light chain classes bound to the B-CLL cell surface. The dissociation constant for the interaction of mouse IgG1 (K121) withthe B-CLL cell surface was 3.6 x 10(-7) m. To confirm the involvement of the human IgM expressed by the B-CLL cells in the interaction, the malignantcells were stimulated in vitro to induce secretion of human IgM. Enzyme immunoassay was used to show that secreted human IgM bound to intact mouse Ig, as occurred with the cell surface analysis. The mouse Ig epitope recognized by the purified secreted human IgM was shown by Western blot analysis tobe located on the light chain of the mouse Ig molecule and to be conformationally dependent. K121 light chain was cloned and expressed in E. coli andthe recombinant light chain bound to the surface of CLL B cells. The results confirm that human IgM is the reactive ligand in the interaction with mouse Ig and indicate that the interaction of polyreactive IgM with mouse IgGoccurs via the light chain component of IgG. Copyright (C) 2001 John Wiley& Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 06:42:38