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Start Over Author "Lucibello, M" Topic mitogen-activated protein kinases
4 results on '"Lucibello, M"'

1. Nerve growth factor inhibits apoptosis in memory B lymphocytes via inactivation of p38 MAPK, prevention of Bcl-2 phosphorylation, and cytochrome c release.

Author

Torcia M, De Chiara G, Nencioni L, Ammendola S, Labardi D, Lucibello M, Rosini P, Marlier LN, Bonini P, Dello Sbarba P, Palamara AT, Zambrano N, Russo T, Garaci E, and Cozzolino F

Subjects
Animals, Cell Nucleus metabolism, Cells, Cultured, Cytosol metabolism, DNA Fragmentation, Enzyme Inhibitors pharmacology, Humans, Imidazoles pharmacology, Immunologic Memory, MAP Kinase Kinase 4, Microscopy, Fluorescence, Mitochondria metabolism, Mitogen-Activated Protein Kinase Kinases metabolism, Mitogen-Activated Protein Kinases metabolism, Phosphorylation, Precipitin Tests, Protein Binding, Protein Transport, Pyridines pharmacology, Rats, Recombinant Proteins metabolism, Serine chemistry, Threonine chemistry, Time Factors, p38 Mitogen-Activated Protein Kinases, Apoptosis, B-Lymphocytes pathology, Cytochrome c Group metabolism, JNK Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinases antagonists & inhibitors, Nerve Growth Factor metabolism, Nerve Growth Factor physiology, Proto-Oncogene Proteins c-bcl-2 metabolism
Abstract

Survival of memory B lymphocytes is tightly linked to the integrity of the Bcl-2 protein and is regulated by a nerve growth factor (NGF) autocrine circuit. In factor-starved memory B cells, the addition of exogenous NGF promptly induced p38 mitogen-activated protein kinase (MAPK), but not c-Jun N-terminal kinase (JNK), dephosphorylation. Conversely, withdrawal of endogenous NGF was followed by p38 MAPK activation and translocation onto mitochondria, whereby it combined with and phosphorylated Bcl-2, as assessed by co-immunoprecipitation and kinase assays in vivo and in vitro. Mitochondria isolated from human memory B cells, then exposed to recombinant p38 MAPK, released cytochrome c, as did mitochondria from Bcl-2-negative MDCK cells loaded with recombinant Bcl-2. Apoptosis induced by NGF neutralization could be blocked by the specific p38 MAPK inhibitor SB203580 or by Bcl-2 mutations in Ser-87 or Thr-56. These data demonstrate that the molecular mechanisms underlying the survival factor function of NGF critically rely upon the continuous inactivation of p38 MAPK, a Bcl-2-modifying enzyme.

Published
2001
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2. NGF withdrawal induces apoptosis in CESS B cell line through p38 MAPK activation and Bcl-2 phosphorylation.

Author

Rosini P, De Chiara G, Lucibello M, Garaci E, Cozzolino F, and Torcia M

Subjects
Apoptosis physiology, B-Lymphocytes, Carbazoles pharmacology, Cell Division drug effects, Enzyme Activation, Enzyme Inhibitors pharmacology, Genes, bcl-2, Humans, Indole Alkaloids, JNK Mitogen-Activated Protein Kinases, Kinetics, Phosphorylation, Receptor, trkA genetics, Receptor, trkA physiology, Receptors, Nerve Growth Factor genetics, Receptors, Nerve Growth Factor physiology, Sequence Deletion, Signal Transduction drug effects, Signal Transduction physiology, Tumor Cells, Cultured, Tyrphostins pharmacology, p38 Mitogen-Activated Protein Kinases, Apoptosis drug effects, Mitogen-Activated Protein Kinases metabolism, Nerve Growth Factor pharmacology, Proto-Oncogene Proteins c-bcl-2 metabolism
Abstract

The sIgG(+) lymphoblastoid B cell line CESS spontaneously produces a high amount of NGF and expresses both high affinity (p140(Trk-A)) and low affinity (p75(NTR)) NGF receptors. Blocking NGF signals with neutralizing antibodies or specific Trk-A inhibitors induces a rapid phosphorylation of antiapoptotic Bcl-2 protein, followed by caspase activation, and apoptotic death of CESS cells. Bcl-2 phosphorylation in several sites within a approximately 60 aa "loop" domain of protein is known to regulate its antiapoptotic function. Accordingly, CESS cells expressing the loop deletional mutant cDNA constructs Bcl-2 Delta40-91 were completely resistant to apoptosis induced by NGF withdrawal, indicating that Bcl-2 phosphorylation is a critical event. NGF withdrawal induces p38 MAPK, but not JNK, activation in CESS cells, and SB203580, a specific inhibitor of p38 MAPK, is able to prevent both Bcl-2 phosphorylation and apoptosis, indicating that p38 MAPK is the enzyme responsible for these events., (Copyright 2000 Academic Press.)

Published
2000
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3. Nerve Growth Factor-dependent Survival of CESS B Cell Line Is Mediated by Increased Expression and Decreased Degradation of MAPK Phosphatase

Author

Rosini, P, De Chiara, G, Bonini, P, Lucibello, M, Marcocci, Me, Garaci, E, Cozzolino, F, and Torcia, M

Subjects
antisense oligonucleotide, mitogen activated protein kinase p38, Enzymologic, mitogen activated protein kinase phosphatase 1, Apoptosis, Cell Cycle Proteins, Biochemistry, p38 Mitogen-Activated Protein Kinases, Nerve Growth Factor, mitochondrion, Phosphorylation, transcription initiation, Biodegradation, Catalysis, Cells, Enzymes, Nerve growth factors (NGF), Neutralization, caspase, cytochrome c, nerve growth factor, nerve growth factor receptor, proteasome, protein bcl 2, apoptosis, article, autocrine effect, B lymphocyte, catalysis, cell survival, controlled study, dephosphorylation, enzyme activation, enzyme degradation, enzyme inactivation, enzyme synthesis, gene overexpression, human, human cell, lymphoblastoid cell, priority journal, protein expression, protein localization, protein phosphorylation, protein protein interaction, protein stability, B-Lymphocytes, Cell Line, Cell Survival, Cysteine Endopeptidases, Gene Expression Regulation, Enzymologic, Humans, Immediate-Early Proteins, Mitochondria, Mitogen-Activated Protein Kinases, Multienzyme Complexes, Phosphoprotein Phosphatase, Proteasome Endopeptidase Complex, Protein-Tyrosine-Phosphatase, Settore MED/07 - Microbiologia e Microbiologia Clinica, Gene Expression Regulation
Published
2004

4. Nerve Growth Factor Inhibits Apoptosis in Memory B Lymphocytes via Inactivation of p38 MAPK, Prevention of Bcl-2 Phosphorylation, and Cytochrome c Release

Author

Serena Ammendola, Maria Lucibello, Lionel N. J.L. Marlier, Persio Dello Sbarba, Nicola Zambrano, Paolo Bonini, Enrico Garaci, Tommaso Russo, Giovanna De Chiara, Federico Cozzolino, Danilo Labardi, Anna Teresa Palamara, Maria Torcia, Paolo Rosini, Lucia Nencioni, Torcia, M, De Chiara, G, Nencioni, L, Ammendola, S, Labardi, D, Lucibello, M, Rosini, P, Marlier, Ln, Bonini, P, Dello Sbarba, P, Palamara, At, Zambrano, Nicola, Russo, Tommaso, Garaci, E, and Cozzolino, F.

Subjects
mitogen activated protein kinase p38, MAPK/ERK pathway, MAP Kinase Kinase 4, Pyridines, Apoptosis, animal cell, stress activated protein kinase, Biochemistry, Cytosol, mitochondrion, Enzyme Inhibitors, Cells, Cultured, serodiagnosis, Cultured, mitogen activated protein kinase, phosphorylation, Kinase, Cytochrome c, protein function, cytochrome c, priority journal, protein transport, Bioassay, Cells, Enzymes, Mutagenesis, Nerve growth factor (NGF), 4 (4 fluorophenyl) 2 (4 methylsulfinylphenyl) 5 (4 pyridyl)imidazole, Janus kinase, nerve growth factor, protein bcl 2, serine, synaptophysin, threonine, DNA fragment, enzyme inhibitor, imidazole derivative, mitogen activated protein kinase kinase, mitogen activated protein kinase kinase 4, pyridine derivative, recombinant protein, apoptosis, article, autocrine effect, B lymphocyte, cell survival, controlled study, enzyme activation, enzyme inactivation, human, human cell, immunoprecipitation, in vitro study, in vivo study, memory cell, molecular biology, nonhuman, protein phosphorylation, protein secretion, animal, cell culture, cell nucleus, chemistry, cytosol, drug antagonism, fluorescence microscopy, immunological memory, metabolism, pathology, physiology, protein binding, rat, time, Animalia, Janus, Animals, B-Lymphocytes, Cell Nucleus, Cytochrome c Group, DNA Fragmentation, Humans, Imidazoles, Immunologic Memory, JNK Mitogen-Activated Protein Kinases, Microscopy, Fluorescence, Mitochondria, Mitogen-Activated Protein Kinase Kinases, Mitogen-Activated Protein Kinases, Nerve Growth Factor, p38 Mitogen-Activated Protein Kinases, Phosphorylation, Precipitin Tests, Protein Binding, Protein Transport, Proto-Oncogene Proteins c-bcl-2, Rats, Recombinant Proteins, Serine, Threonine, Time Factors, p38 mitogen-activated protein kinases, Fluorescence, Protein kinase A, Molecular Biology, NGF, apoptosis, B lymphocytes, Microscopy, biology, Settore MED/07 - Microbiologia e Microbiologia Clinica, Autocrine signalling, Cell Biology, Molecular biology, Nerve growth factor, biology.protein
Abstract

Survival of memory B lymphocytes is tightly linked to the integrity of the Bcl-2 protein and is regulated by a nerve growth factor (NGF) autocrine circuit. In factor-starved memory B cells, the addition of exogenous NGF promptly induced p38 mitogen-activated protein kinase (MAPK), but not c-Jun N-terminal kinase (JNK), dephosphorylation. Conversely, withdrawal of endogenous NGF was followed by p38 MAPK activation and translocation onto mitochondria, whereby it combined with and phosphorylated Bcl-2, as assessed by co-immunoprecipitation and kinase assays in vivo and in vitro. Mitochondria isolated from human memory B cells, then exposed to recombinant p38 MAPK, released cytochrome c, as did mitochondria from Bcl-2-negative MDCK cells loaded with recombinant Bcl-2. Apoptosis induced by NGF neutralization could be blocked by the specific p38 MAPK inhibitor SB203580 or by Bcl-2 mutations in Ser-87 or Thr-56. These data demonstrate that the molecular mechanisms underlying the survival factor function of NGF critically rely upon the continuous inactivation of p38 MAPK, a Bcl-2-modifying enzyme.

Published
2001
Full Text
View/download PDF

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