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burkitt lymphoma/protease
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Ligation of CD40 rescues Ramos-Burkitt lymphoma B cells from calcium ionophore- and antigen receptor-triggered apoptosis by inhibiting activation of the cysteine protease CPP32/Yama and cleavage of its substrate PARP.
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The new and growing family of interleukin-1beta-converting enzyme (ICE) cysteine proteases are now recognised to be major effectors of cellular death by apoptosis. Like other members of this family, the CPP32/Yama proform is activated by processing to its active heterodimeric enzyme or apopain when
Ligation of CD40 potentiates Fas-mediated activation of the cysteine protease CPP32, cleavage of its death substrate PARP, and apoptosis in Ramos-Burkitt lymphoma B cells.
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The proliferation and survival of a B cell population is necessarily tightly controlled to prevent the arisal of malignancy or autoimmunity. The expansion or elimination of a B cell clone is determined through a complex interaction of the tumour necrosis factor receptor/nerve growth factor receptor
A trypsin-like serine protease activity on activated human B cells and various B cell lines.
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We have studied the trypsin-like serine protease activity of human tonsillar B lymphocytes. The lysate of the low-density, in vivo activated B cells as well as the lysate of cells stimulated with anti-human IgM F(ab')2 show elevated trypsin-like serine protease activity compared to the resting
Met-ase: cloning and distinct chromosomal location of a serine protease preferentially expressed in human natural killer cells.
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A cDNA clone encoding a human NK serine protease was obtained by screening a lambda-gt10 library from the Lopez NK leukemia with the rat natural killer Met-ase (RNK-Met-1) cDNA clone. In Northern blot analysis human Met-ase (Hu-Met-1) cDNA hybridized with a 0.9-kb mRNA in two human NK leukemia cell
Epstein-Barr virus independent dysregulation of UBP43 expression alters interferon-stimulated gene expression in Burkitt lymphoma.
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Epstein-Barr virus (EBV) persists as a life-long latent infection within memory B cells, but how EBV may circumvent the innate immune response within this virus reservoir is unclear. Recent studies suggest that the latency-associated non-coding RNAs of EBV may actually induce type I (antiviral)
Inhibition of CPP32 blocks surface IgM-mediated apoptosis and D4-GDI cleavage in human BL60 Burkitt lymphoma cells.
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Apoptosis (programmed cell death) is instrumental in the process of controlling lymphocyte growth and selection. Negative selection, mediated by surface IgM (sIgM) signaling after encountering self antigen, eliminates autoreactive B cells. To identify proteins which are potentially involved in
Plasma membrane sequestration of apoptotic protease-activating factor-1 in human B-lymphoma cells: a novel mechanism of chemoresistance.
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Burkitt lymphoma (BL) is a highly aggressive B-cell neoplasm harboring chromosomal rearrangements of the c-myc oncogene. BL cells frequently resist apoptosis induction by chemotherapeutic agents; however, the mechanism of unresponsiveness has not been elucidated. Here, we show that cytochrome c
Increased expression and altered subunit composition of proteasomes induced by continuous proteasome inhibition establish apoptosis resistance and hyperproliferation of Burkitt lymphoma cells.
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The proteasome is the main protease for extralysosomal protein degradation in eukaryotic cells, and constitutes a sophisticated high molecular mass proteinase complex underlying a tightly coordinated expression and assembly of multiple subunits and subcomplexes. Here we show that continuous
Enzymatic and organizational difference in expression of a Burkitt lymphoma-associated antigen (globotriaosylceramide) in Burkitt lymphoma and lymphoblastoid cell lines.
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In our previous study, a Burkitt lymphoma-associated antigen defined by a monoclonal antibody, designated 38.13, was characterized as globotriaosylceramide (Gb3, Gal alpha 1----4 Gal beta 1----4 Glc beta 1----1 Cer) (Nudelman, E., Kannagi, R., Hakomori, S., Parsons, M., Lipinski, M., Wiels, J.,
Down-regulation of SENP1 expression increases apoptosis of Burkitt lymphoma cells.
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OBJECTIVE
To investigate the effect of down-regulation of Sentrin/SUMO-specific protease 1 (SENP1) expression on the apoptosis of human Burkitt lymphoma cells (Daudi cells) and potential mechanisms.
METHODS
Short hairpin RNA (shRNA) targeting SENP1 was designed and synthesized and then cloned into a
SLLP1, a unique, intra-acrosomal, non-bacteriolytic, c lysozyme-like protein of human spermatozoa.
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We report the presence of a unique, non-bacteriolytic, c (chicken or conventional type) lysozyme-like protein, SLLP1, in the acrosome of human sperm. C lysozymes are bacteriolytic and can also bind to N-acetylglucosamines linked by beta-1,4 glycosidic bonds. Most of the invariant residues (17 out of
Supernatants of stored polymorphonuclear neutrophils exhibit growth-promoting activity in several cell lines: perforin expression in polymorphonuclear neutrophils and its role in down-regulation of growth-promoting activity.
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OBJECTIVE
Polymorphonuclear neutrophils (PMNs) play important roles in the host immune defence. This study was performed to identify roles of PMNs other than those already known.
METHODS
PMNs were separated from the peripheral blood of healthy individuals and stored in vitro for 24 h in the presence
Expression of the serpin centerin defines a germinal center phenotype in B-cell lymphomas.
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Centerin (SERPINA9/GCET1) is a protease inhibitor with expression restricted to germinal center B cells and lymphoid malignancies with germinal center B-cell maturation. Expression of the centerin gene transcript, along with bcl-6 and GCET2/HGAL, constitutes a molecular signature associated with a
Dissection of pathways leading to antigen receptor-induced and Fas/CD95-induced apoptosis in human B cells.
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To dissect intracellular pathways involved in B cell Ag receptor (BCR)-mediated and Fas-induced human B cell death, we isolated clones of the Burkitt lymphoma cell line Ramos with different apoptosis sensitivities. Selection for sensitivity to Fas-induced apoptosis also selected for clones with
Protein kinase activity of the intracellular but not of the membrane-associated form of the Ki-1 antigen (CD30).
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The Hodgkin-associated Ki-1 antigen (CD30) consists of a 120-kDa membrane-associated glycosylated phosphoprotein (Ki-1/120) and a 57-kDa non-glycosylated phosphoprotein (Ki-1/57) which only occurs intracellularly. Both molecules are phosphorylated at serine residues. An analysis of the peptide
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