Identification of apoptosis-associated proteins in a human Burkitt lymphoma cell line. Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3.

Brockstedt, Ekkehard; Rickers, Anke; Kostka, Susanne; Laubersheimer, Andreas; Dörken, Bernd; Wittmann‐Liebold, Brigitte; Bommert, Kurt; Otto, Albrecht

doi:10.1016/s0021-9258(19)88612-x

Cited by 20 publications

(20 citation statements)

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“…Additionally, PfP0 has been implicated in other cellular functions besides ribosomal assembly. In Drosophila melanogaster, P0 has been shown to possess DNA-binding activity, specifically apurinic/apyrimidinic endonuclease activity [45], and has been also implicated as a regulatory protein in apoptosis and carcinogenesis of mammalian cells [46,47].…”

Section: Discussionmentioning

confidence: 99%

Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

et al. 2009

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The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 ((1)MAKLSKQQKKQMYIEKLSSL(20)), HABP 33900 ((41)ASVRKSLRGKATILMGKNTRY(60)), HABP 33901 ((61)IRTALKKNLQAVPQIEKLLPY (80)), and HABP 33906 ((161)LIKQGEKVTASSATLLRKFNY(180)). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of alpha-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria.

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Section: Discussionmentioning

confidence: 99%

Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

et al. 2009

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“…It is not surprising that c-Jun/sc45 antibodies recognize a variety of proteins after caspase proteolysis because it is known that caspase-3 cleaves many different substrates including poly-(ADP-ribose) polymerase (PARP), fodrin, retinoblastoma protein, huntingtin, DNA-dependent protein kinase, gelsolin, ribonucleoprotein A1, vimentin and others (Fernandes-Alnemri et al 1995;Martin et al 1995;An and Dou 1996;Goldberg et al 1996;Song et al 1996;Kothakota et al 1997;Brockstedt et al 1998;Hashimoto et al 1998) that may share common epitopes at their cleavage sites.…”

Section: Discussionmentioning

confidence: 99%

c-Jun-like Immunoreactivity in Apoptosis Is the Result of a Crossreaction with Neoantigenic Sites Exposed by Caspase-3-mediated Proteolysis

Ribera¹,

Ayala²,

Esquerda³

2002

J Histochem Cytochem.

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Previous reports in various cells and species have shown that apoptotic cells are specifically and strongly labeled by certain c-Jun/N-terminal antibodies, such as c-Jun/sc45. This kind of immunoreactivity is confined to the cytoplasm. It is not due to c-Jun but appears to be related to c-Jun-like neoepitopes generated during apoptosis. This study was planned to gain further information about c-Jun-like immunostaining during apoptosis and to evaluate these antibodies as possible tools for characterizing cell death. Most of the experiments were performed in chick embryo spinal cord. When the apoptotic c-Jun-like immunoreactivity and caspase-3 immunostaining patterns were compared, we found that both antibodies immunostained the same dying cells in a similar pattern. In contrast to TUNEL staining, which reveals a positive reaction in both apoptotic and necrotic dying cells, active caspase-3 and c-Jun/sc45 antibodies are more selective because they stained only apoptotic cells. When cytosolic extracts from normal tissues were digested in vitro with caspase-3, c-Jun/sc45 immunoreactivity was strongly induced in several proteins, as demonstrated by Western blotting. Similar results were found when normal tissue sections were treated with caspase-3. Our results show that c-Jun/sc45 antibodies react with neoepitopes generated from cell proteins cleaved by activated caspases during apoptosis. We conclude that c-Jun/sc45 antibodies may be useful for detecting apoptosis. They can even be used in archival paraffin-embedded tissue samples.

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“…3 Antiribosomal-P protein (anti-P) antibodies are directed to three ribosomal phosphorylated proteins that belong to apoptosis-associated proteins in a human Burkitt lymphoma cell line. 4 These antibodies are highly specific serological markers of SLE, present in nearly 15-20% of patients with active disease, especially central nervous system involvement. 5 Recently, it has been reported that anti-P antibodies cross-react with phospholipids 6 and enhance production of tumour necrosis factor α (TNF-α) and interleukin 6 (IL-6), which increase proliferation of normal and clonal B cells.…”

Section: Introductionmentioning

confidence: 99%

Antiribosomal-P protein antibodies in a patient with systemic lupus erythematosus and non-Hodgkin’s lymphoma: more than coincidental finding?

Miljić¹,

Bonaci-Nikolic²,

Čolović³

et al. 2009

Lupus

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Patients with systemic lupus erythematosus (SLE) are at an increased risk of lymphomas, but mechanisms underlying this association are obscure. Recently, it has been shown that antiribosomal-P protein (anti-P) antibodies cross-react with phospholipids and enhance the production of cytokines which may influence lymphomagenesis. We report a 46-year-old woman who suffered high grade diffuse large B-cell non-Hodgkin's lymphoma (DLBCL) 28 months after the diagnosis of SLE. Development of lymphoma was associated with occurrence of serum monoclonal IgM, and pronounced prolongation of phospholipid-dependent clotting tests. Anti-P IgG antibodies were highly positive both on HEp-2 cells and in ELISA test. Anticardiolipin, anti-beta2 glycoprotein I, and antiprothrombin IgM antibodies have also been found in high concentrations. Complete remission of DLBCL and SLE, with normalisation of clotting tests, and disappearance of M component was achieved with administration of rituximab, cyclophosphamide, doxorubicin, vincristine and prednisone. The progression of SLE to DLBCL associated with presence of anti-P antibodies has not been previously reported. This association may not be coincidental, but further investigations are required to confirm this hypothesis.

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Identification of apoptosis-associated proteins in a human Burkitt lymphoma cell line. Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3.

Cited by 20 publications

References 0 publications

Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

c-Jun-like Immunoreactivity in Apoptosis Is the Result of a Crossreaction with Neoantigenic Sites Exposed by Caspase-3-mediated Proteolysis

Antiribosomal-P protein antibodies in a patient with systemic lupus erythematosus and non-Hodgkin’s lymphoma: more than coincidental finding?

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