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10.1128/JVI.72.4.3018-3028.1998 http://scihub22266oqcxt.onion/10.1128/JVI.72.4.3018-3028.1998 9525624!109749!9525624     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Virol 1998 ; 72 (4): 3018-28 Nephropedia Template TP {{tp|p=9525624|t=1998. Human parvovirus B19 nonstructural (NS1) protein induces apoptosis in erythroid lineage cells |pdf=|usr=}}{{9525624}} gab.com Text Human parvovirus B19 nonstructural (NS1) protein induces apoptosis in erythroid lineage cells JO: J Virol http://www.kidney.de/pget.php?&tw=1&pmid=9525624 #FOAvip Infection of erythroid-lineage cells by human parvovirus B19 is characterized by a gradual cytocidal effect. Accumulating evidence now implicates the nonstructural (NS1) protein of the virus in cytotoxicity, but the mechanism underlying the NS1-induced cell death is not known. Using a stringent regulatory system, we demonstrate that NS1 cytotoxicity is closely related to apoptosis, as evidenced by cell morphology, genomic DNA fragmentation, and cell cycle analysis with the human erythroleukemia cell line K562 and the erythropoietin-dependent megakaryocytic cell line UT-7/Epo. Apoptosis was significantly inhibited by an interleukin-1beta (IL-1beta)-converting enzyme (ICE)/CED-3 family protease inhibitor, Ac-DEVD-CHO (CPP32; caspase 3), whereas a similar inhibitor of ICE (caspase 1), Ac-YVAD-CHO, had no effect. Furthermore, stable expression of the human Bcl-2 proto-oncogene resulted in near-total protection from cell death in response to NS1 induction. Mutations engineered into the nucleoside triphosphate-binding domain of NS1 significantly rescued cells from NS1-induced apoptosis without having any effect on NS1-induced activation of the IL-6 gene expression which is mediated by NF-kappaB. Furthermore, using pentoxifylline, an inhibitor of NF-kappaB activation, we demonstrate that the NF-kappaB-mediated IL-6 activation by NS1 is uncoupled from the apoptotic pathway. This functional dissection indicates a complexity underlying the biochemical function of human parvovirus NS1 in transcriptional activation and induction of apoptosis. Our findings indicate that NS1 of parvovirus B19 induces cell death by apoptosis in at least erythroid-lineage cells by a pathway that involves caspase 3, whose activation may be a key event during NS1-induced cell death. Twit Text FOAVip Human parvovirus B19 nonstructural (NS1) protein induces apoptosis in erythroid lineage cells ????J Virol http://www.kidney.de/pget.php?&tw=1&pmid=9525624 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=9525624 #FOAvip English Wikipedia <ref>{{Cite pmid|9525624}}</ref> Human parvovirus B19 nonstructural (NS1) protein induces apoptosis in erythroid lineage cells #MMPMID9525624 Moffatt S; Yaegashi N; Tada K; Tanaka N; Sugamura K J Virol 1998[Apr]; 72 (4): 3018-28 PMID9525624show ga Infection of erythroid-lineage cells by human parvovirus B19 is characterized by a gradual cytocidal effect. Accumulating evidence now implicates the nonstructural (NS1) protein of the virus in cytotoxicity, but the mechanism underlying the NS1-induced cell death is not known. Using a stringent regulatory system, we demonstrate that NS1 cytotoxicity is closely related to apoptosis, as evidenced by cell morphology, genomic DNA fragmentation, and cell cycle analysis with the human erythroleukemia cell line K562 and the erythropoietin-dependent megakaryocytic cell line UT-7/Epo. Apoptosis was significantly inhibited by an interleukin-1beta (IL-1beta)-converting enzyme (ICE)/CED-3 family protease inhibitor, Ac-DEVD-CHO (CPP32; caspase 3), whereas a similar inhibitor of ICE (caspase 1), Ac-YVAD-CHO, had no effect. Furthermore, stable expression of the human Bcl-2 proto-oncogene resulted in near-total protection from cell death in response to NS1 induction. Mutations engineered into the nucleoside triphosphate-binding domain of NS1 significantly rescued cells from NS1-induced apoptosis without having any effect on NS1-induced activation of the IL-6 gene expression which is mediated by NF-kappaB. Furthermore, using pentoxifylline, an inhibitor of NF-kappaB activation, we demonstrate that the NF-kappaB-mediated IL-6 activation by NS1 is uncoupled from the apoptotic pathway. This functional dissection indicates a complexity underlying the biochemical function of human parvovirus NS1 in transcriptional activation and induction of apoptosis. Our findings indicate that NS1 of parvovirus B19 induces cell death by apoptosis in at least erythroid-lineage cells by a pathway that involves caspase 3, whose activation may be a key event during NS1-induced cell death. |*Apoptosis[MESH] |*Caspases[MESH] |Caspase 1[MESH] |Caspase 3[MESH] |Cell Line[MESH] |Cysteine Endopeptidases/metabolism[MESH] |Cysteine Proteinase Inhibitors/pharmacology[MESH] |Erythroid Precursor Cells/pathology/*virology[MESH] |Humans[MESH] |Interleukin-6/genetics[MESH] |NF-kappa B/antagonists & inhibitors[MESH] |Oligopeptides/pharmacology[MESH] |Parvovirus B19, Human/*metabolism[MESH] |Pentoxifylline/pharmacology[MESH] |Proto-Oncogene Mas[MESH] |Proto-Oncogene Proteins c-bcl-2/genetics/metabolism[MESH] |Transcriptional Activation[MESH] |Tumor Cells, Cultured[MESH]Human parvovirus B19 nonstructural (NS1) protein induces apoptosis in (epmc).pdf DeepDyve Pubget Overpricing