Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation.

Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation. Research Abstract Details 

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Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation. Abstract Text:

Ji-Young Kim,Myoung-Hee Ahn,Hye-Sun Jun,Jai-Won Jung,Jae-Sook Ryu,Duk-Young Min,

Our experiments aimed to clarify the mechanism by which host cell apoptosis is inhibited by infection with the intracellular protozoan parasite, Toxoplasma gondii (T. gondii). Mouse spleen cells were cultured in 6-well plates with RPMI 1640/ 10% FBS at 37?, in a 5% CO2 atmosphere. Apoptosis of spleen cells was induced by actinomycin-D (AD) treatment for 1 h prior to infection with T. gondii. A variety of assays were used to assess the progression of apoptosis: DNA size analysis on agarose gel electrophoresis, flow cytometry with annexin V/PI staining, and analysis of expression levels of Bcl-2 family and NF-kappaB mRNA and proteins by RT-PCR, Western blotting, and EMSA. Additionally, transmission electron microscopy (TEM) was performed to observe changes in cell morphology. Fragmentation of DNA was inhibited in spleen cells treated with AD and T. gondii 5 h and 18 h post infection, respectively, and flow cytometry studies showed a decreased apoptotic rates in AD and T. gondii treated spleen cells. We observed decreased expression of Bax mRNA and protein, while levels of Bcl-2 mRNA remained constant in spleen cells treated with AD and T. gondii. Caspase 3 and PARP were inactivated in cells treated with AD and T. gondii, and increased levels of cleaved caspase 8 were also observed. Analysis of EMSA and Western blot data suggests that activation of transcription factor NF-kappaB may be involved in the blockade of apoptosis by T. gondii. TEM analysis showed nuclear fragmentation and chromatin condensation occurring in spleen cells treated with AD; however, such apoptosis- associated morphological changes were not observed in cells treated with both AD and T. gondii tachyzoites. Together, these data show that T. gondii infection inhibits AD induced apoptosis via caspase inactivation and NF-kappaB activation in mouse spleen cells.

Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation. Publishing Authors By Initials

JY Kim,MH Ahn,HS Jun,JW Jung,JS Ryu,DY Min,

For similar peptides: intracellular signaling peptides and proteins: apoptosis regulatory proteins: proto-oncogene proteins c-bcl-2: bcl-2-associated x protein research abstracts see: peptides: intracellular signaling peptides and proteins: apoptosis regulatory proteins: proto-oncogene proteins c-bcl-2: bcl-2-associated x protein research

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Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Yonsei medical journal

VOLUME: 47

Page Numbers: 862-9

Journal Abbreviation: Yonsei Med. J.

ISSN: 0513-5796

DAY: 31

MONTH: Dec

YEAR: 2006

Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 414003

Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation. Keywords Mesh Terms:

KEYWORDS: bcl-2-Associated X Protein

MESH TERMS: metabolism

Chemical & Substance for Abstract: Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation. Information

Substance Name: Caspase 3

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation.

AFFILIATION: Department of Parasitology, Institute of Biomedical Science, Hanyang University College of Medicine, Seoul, Korea.

Country: Korea (South)

AGENCY: United States PHS

GRANT: NIH 348-6111-215

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MEDLINETA: Yonsei Med J

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