The human (PsiL+mu-) proB complex: cell surface expression and biochemical structure of a putative transducing receptor
| Autor: | B, Lemmers, L, Gauthier, V, Guelpa-Fonlupt, M, Fougereau, C, Schiff |
|---|---|
| Přispěvatelé: | Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM) |
| Jazyk: | angličtina |
| Rok vydání: | 1999 |
| Předmět: |
MESH: Immunoglobulin Light Chains
MESH: Immunoglobulin mu-Chains Immunoglobulin Light Chains Surrogate Antigens CD19 MESH: Membrane Glycoproteins MESH: Mice Inbred BALB C Antigens CD34 Bone Marrow Cells MESH: Flow Cytometry [SDV.CAN]Life Sciences [q-bio]/Cancer MESH: Stem Cells [SDV.BC]Life Sciences [q-bio]/Cellular Biology MESH: Antibodies Monoclonal MESH: Recombinant Proteins Mice Antibody Specificity Precursor B-Cell Lymphoblastic Leukemia-Lymphoma MESH: B-Lymphocytes Animals Humans MESH: Animals [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: Antibody Specificity MESH: Mice B-Lymphocytes Mice Inbred BALB C Membrane Glycoproteins MESH: Humans MESH: Antigens CD19 Immunoglobulin mu-Chains Stem Cells MESH: Bone Marrow Cells [SDV.BA]Life Sciences [q-bio]/Animal biology Cell Membrane Antibodies Monoclonal MESH: Immunoglobulin Light Chains Surrogate MESH: Antigens CD34 Flow Cytometry Recombinant Proteins MESH: Precursor B-Cell Lymphoblastic Leukemia-Lymphoma [SDV.IMM]Life Sciences [q-bio]/Immunology Immunoglobulin Light Chains MESH: Cell Membrane |
| Zdroj: | Blood Blood, American Society of Hematology, 1999, 93 (12), pp.4336-46 |
| ISSN: | 0006-4971 1528-0020 |
| Popis: | International audience; The surrogate light chain (PsiL) associates with mu and Igalpha-Igbeta chains to form the preB-cell receptor that plays a critical role in early B-cell differentiation. Discrepancies exist in human concerning the existence of PsiL+mu- proB cells and the biochemical structure of such a proB-cell complex remains elusive. Among new antihuman VpreB monoclonal antibodies (MoAbs), 5 of the gamma kappa isotype bound to recombinant and native VpreB protein with high affinity. They recognized 4 discrete epitopes, upon which 2 were in the extra-loop fragment. Such MoAbs detected the PsiL at the cell surface of either preB or on both proB and preB cells. The previously reported SLC1/SLC2 MoAbs recognize a conformational epitope specific for the mu/PsiL association in accordance with their preB-cell reactivity. Using the proB/preB 4G7 MoAb, PsiL cell surface expression was detected on normal bone marrow, not only on CD34(-)CD19(+) preB but also on CD34(+)CD19(+) proB cells. Futhermore, this MoAb identified PsiL+mu- fresh proB leukemic cells of the TEL/AML1 type. Biochemical studies showed that, at the proB stage, the PsiL is associated noncovalently with two proteins of 105 and 130 kD. Triggering of this complex induces intracellular Ca2+ flux, suggesting that the PsiL may be involved in a new receptor at this early step of the B-cell differentiation. |
| Databáze: | OpenAIRE |
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