PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 9122742

B-cell development and differentiation.

M A Duchosal
View original source ↗Export metadata ↓

Abstract

B-cell development is characterized by antigen-independent phases in fetal hematopoietic organs and adult bone marrow, which lead to naive recirculating B cells in the periphery. The diversity of the naive (primary) B-cell repertoire resides in somatic events where minigenes from a large available repertoire are imprecisely rearranged and encode antigen-binding sites of antibodies. Naive B cells expand upon antigenic stimulation, acquire somatic mutations leading to high-affinity antibodies, and switch immunoglobulin (Ig) isotype in peripheral lymphoid organs. This immune reaction leads to the generation of memory B cells, which are long-lived and capable of rapid generation of specific high-affinity antibodies upon recall antigenic stimulation, as well as plasma cells, which constitutively secrete a large amount of antibodies.

Explore related subjects

Antigens, DifferentiationB-LymphocytesCell DifferentiationCellular SenescenceEmbryonic and Fetal DevelopmentHumansLymphocyte ActivationReceptors, Antigen, B-CellStem CellsJournal ArticleResearch Support, Non-U.S. Gov'tReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

M A Duchosal. 1997. B-cell development and differentiation.. https://pubmed.ncbi.nlm.nih.gov/9122742/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1999

Identification of epithelial and myeloid-specific DNA elements regulating MRP14 gene transcription.

Macrophage migration inhibition factor-related protein 14 (MRP14) is a Ca2+-binding protein of the S-100 family highly abundant in myelomonocytic and epithelial cells. The expression pattern is restricted to myeloid and epithelial cells and therefore the MRP14 gene is ideally suited to study the regulation of gene expression in these cells. We characterized the human MRP14 promoter by using the chloramphenicol acetyltransferase reporter assay system. The analysis was performed in epithelial (TR146) and myeloid (HL-60) cells, and we were successful in mapping positive and negative regulatory elements. The region -114/-419 contains strong myeloid-specific regulatory elements, whereas the domain -600/-1000 enhances the MRP14 transcription in epithelial cells. The sequence -462/-600 accommodates a regulatory element that enhances the promoter activity in both myeloid and epithelial cells. Regions -114/-419 and -1000/-4500 reduce the expression of MRP14 only in epithelial cells, whereas the domains -419/-462 and -4500/-6500 contain down-regulating elements in both, epithelial and myeloid cells. The presented data demonstrate that transcription of the human MRP14 gene is regulated in a complex manner enabling the precise control of the MRP14 level in epithelial and myeloid cells.

Antigens, Differentiation↗
PubMed1999

Phage display cDNA cloning of protein with carbohydrate affinity.

Cell surface complex carbohydrate structures that are synthesized through the actions of glycosyltransferases play an important role in cell-to-cell and cell-to-extracellular matrix interactions. To examine the feasibility of phage display technique to clone cDNAs encoding glycosyltransferases, we performed biopanning experiments using human histo-blood group A transferase as a model enzyme and its substrate, blood group H-specific glycoproteins, as a bait ligand. Our attempts have been unsuccessful, possibly because of the enzyme's weak affinity with the target. However, we have selectively enriched several phage clones that expressed capsid proteins fused with galectin-3, a galactose/lactose-specific animal lectin of the galectin family. These results demonstrate that this novel approach of phage display is useful in cDNA cloning of proteins with carbohydrate-binding property.

Antigens, Differentiation↗
PubMed1999

Exogenous expression of a dominant negative RORalpha1 vector in muscle cells impairs differentiation: RORalpha1 directly interacts with p300 and myoD.

ROR/RZR is an orphan nuclear receptor that has no known ligand in the 'classical sense'. In the present study we demonstrate that RORalpha is constitutively expressed during the differentiation of proliferating myoblasts to post-mitotic multinucleated myotubes, that have acquired a contractile phenotype. Exogenous expression of dominant negative RORalpha1DeltaE mRNA in myogenic cells significantly reduces the endogenous expression of RORalpha1 mRNA, represses the accumu-lation and delays the activation of mRNAs encoding MyoD and myogenin [the muscle-specific basic helix-loop-helix (bHLH) proteins] and p21(Waf-1/Cip-1) (a cdk inhibitor). Immunohistochemistry demonstrates that morpho-logical differentiation is delayed in cells expressing the RORDeltaE transcript. Furthermore, the size and development of mutlinucleated myotubes is impaired. The E region of RORalpha1 interacts with p300, a cofactor that functions as a coactivator in nuclear receptor and MyoD-mediated transactivation. Consistent with the functional role of RORalpha1 in myogenesis, we observed that RORalpha1 directly interacts with the bHLH protein MyoD. This interaction was mediated by the N-terminal activation domain of the bHLH protein, MyoD, and the RORalpha1 DNA binding domain/C region. Furthermore, we demonstrated that p300, RORalpha1 and MyoD interact in a non-competitive manner. In conclusion, this study provides evidence for a biological role and positive influence of RORalpha1 in the cascade of events involved in the activation of myogenic-specific markers and cell cycle regulators and suggests that crosstalk between theretinoid-relatedorphan (ROR) nuclear receptors and the myogenic bHLH proteins has functional consequences for differentiation.

Antigens, Differentiation↗