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Nuclear factors in B lymphoma enhance splicing of mouse membrane-bound mu mRNA in Xenopus oocytes (1988)

N. Tsurushita ; L. Ho ; L. J. Korn

American Association for the Advancement of Science (AAAS)

In: Science. 239(4839): 494-7.

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Publication Date: 1988-01-29

Description: Regulation of the synthesis of membrane-bound and secreted immunoglobulin mu heavy chains at the level of RNA processing is an important element for B cell development. The precursor mu RNA is either polyadenylated at the upstream poly(A) site (for the secreted form) or spliced (for the membrane-bound form) in a mutually exclusive manner. When the mouse mu gene linked to the SV40/HSV-TK hybrid promoter was microinjected into Xenopus oocytes, the mu messenger RNA (mRNA) was altered by coinjection of nuclei of mouse surface IgM-bearing B-lymphoma cells to include the synthesis of the membrane-bound form. An increase in the membrane-bound form was not observed when nuclei of IgM-secreting hybridoma cells or fibroblast cells were coinjected. Deletion of the upstream poly(A) site did not eliminate the effect of B-lymphoma nuclei suggesting that membrane-specific splicing is stimulated. Further, splicing of other mu gene introns was not affected by coinjection of B-lymphoma nuclei. These results suggest that mature B cells contain one or more transacting nuclear factors that stimulate splicing specific for membrane-bound mu mRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsurushita, N -- Ho, L -- Korn, L J -- AI21298/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 29;239(4839):494-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3124268" target="_blank"〉PubMed〈/a〉

Keywords: Animals ; B-Lymphocytes/immunology/ultrastructure ; Cell Membrane/metabolism ; Cell Nucleus/*physiology ; DNA, Recombinant ; Female ; Hybridomas/ultrastructure ; Immunoglobulin M/genetics ; Immunoglobulin mu-Chains/*genetics ; Introns ; Lymphoma/*immunology/ultrastructure ; Mice ; Microinjections ; Nuclear Transfer Techniques ; Oocytes/*metabolism ; Plasmids ; Promoter Regions, Genetic ; *RNA Splicing ; RNA, Messenger/*genetics ; Tumor Cells, Cultured ; Xenopus

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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Antibodies cross-reactive with E- and P-selectin block both E- and P- selectin functions (1995)

Berg, EL ; Fromm, C ; Melrose, J ; [et al.]

American Society of Hematology

In: Blood. 1995; 85(1): 31-37. Published 1995 Jan 01. doi: 10.1182/blood.v85.1.31.bloodjournal85131.

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Publication Date: 1995-01-01

Description: E- and P-selectin are inflammation-induced cell adhesion molecules that mediate leukocyte-endothelial cell and leukocyte-platelet interactions. Monoclonal antibodies (MoAbs) specific for either E-selectin or P- selectin are protective in several animal models of inflammatory disease. To generate an MoAb with broader therapeutic potential, MoAbs that bind to both E- and P-selectin were generated by immunization of mice with mouse pre-B cell lines transfected with human E- and P- selectin. Interestingly, although the only selection criterion was the ability to bind both E- and P-selectin, all three antibodies obtained efficiently block both E- and P-selectin-mediated functions. The inhibited functions include neutrophil or HL-60 cell binding to tumor necrosis factor-alpha-activated human umbilical vein endothelial cells, E- or P-selectin transfectant cell lines, and platelet-HL-60 rosetting. These antibodies, EP-5C7, EP-2C9, and EP-1D8, recognize the same or overlapping epitope within the lectin domains of E- and P-selectin. The data suggest that functionally important epitopes of homologous proteins can be targeted by selecting for antibodies with reactivity toward both proteins. Furthermore, a potent blocking antibody specific for both E- and P-selectin may provide a more effective and broadly useful reagent for treating acute and potentially certain chronic inflammatory conditions.

Print ISSN: 0006-4971

Electronic ISSN: 1528-0020

Topics: Biology , Medicine