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Tumor necrosis factor receptor-mediated apoptosis in Trichinella spiralis-infected muscle cells

Published online by Cambridge University Press:  21 April 2005

Z. WU ,
I. NAGANO ,
T. BOONMARS  and
Y. TAKAHASHI
Z. WU
Affiliation:
Department of Parasitology, Gifu University Graduate School of Medicine, Yanagito 1-1, Gifu 501-1194, Japan
I. NAGANO
Affiliation:
Department of Parasitology, Gifu University Graduate School of Medicine, Yanagito 1-1, Gifu 501-1194, Japan
T. BOONMARS
Affiliation:
Department of Parasitology, Gifu University Graduate School of Medicine, Yanagito 1-1, Gifu 501-1194, Japan
Y. TAKAHASHI
Affiliation:
Department of Parasitology, Gifu University Graduate School of Medicine, Yanagito 1-1, Gifu 501-1194, Japan
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Abstract

In order to reveal the mechanisms underlying nurse cell formation during Trichinella spiralis infection, the expression of the factors of tumor necrosis factor-alpha (TNF-α)/TNF receptor 1 (TNFR-1) signalling pathway mediating apoptosis was investigated. The analysed factors included TNF-α, TNFR-1, TNF receptor-associated death-domain (TRADD), caspase 3, caspase 8, TNF receptor associated factor-2 (TRAF2) and receptor interactive protein (RIP), all of which are involved in the TNF-α/TNFR-1 signalling pathway-mediated apoptosis. The quantitative RT-PCR indicated that the infected muscle tissues up-regulate the expression of pro-apoptosis genes (TNF-α, TNFR-1 and TRADD, caspase 3 and caspase 8), and anti-apoptosis genes (TRAF2 and RIP) at the beginning of cyst formation. The expression returned to the normal level after cyst formation. The quantitative RT-PCR analysis of mRNA from tissue samples isolated by laser capture micro-dissection confirmed that the up-regulation of these genes was restricted in infected muscle cells, was not in the inflammation cells around infected muscle cells nor in normal muscle cells. The in situ localization study of pro-apoptosis (TRADD, caspase 3) and anti-apoptosis gene products (TRAF2) indicated that these were expressed in the basophilic cytoplasm (infected muscle cell origin) of the nurse cells. Thus the present study suggests that the TNF-α/TNFR-1 signalling pathway is involved in nurse cell formation.

Keywords

Trichinella spiralisTNF-αdeath receptorapoptosis
Type
Research Article
Information
Parasitology , Volume 131 , Issue 3 , September 2005 , pp. 373 - 381
Copyright
© 2005 Cambridge University Press

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References

REFERENCES

Beg, A. A. and Baltimore, D. ( 1996). An essential role for NF-kappaB in preventing TNF-alpha-induced cell death. Science 274, 782–784.CrossRefGoogle Scholar
Boonmars, T., Wu, Z., Nagano, I., Nakada, T. and Takahashi, Y. ( 2004 a). Differences and similarities of nurse cells in cysts of T. spiralis and T. pseudospiralis. Journal Helminthology 78, 7–16.Google Scholar
Boonmars, T., Wu, Z., Nagano, I. and Takahashi, Y. ( 2004 b). Expression of apoptosis-related factors in muscles infected with T. spiralis. Parasitology 128, 323–332.Google Scholar
Bratton, S. B., Walker, G., Srinivasula, S. M., Sun, X. M., Butterworth, M., Alnemri, E. S. & Cohen, G. M. ( 2001). Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes. EMBO Journal 20, 998–1009.CrossRefGoogle Scholar
Collins, R. A. and Grounds, M. D. ( 2001). The role of tumor necrosis factor-alpha (TNF-alpha) in skeletal muscle regeneration. Studies in TNF-alpha(−/−) and TNF-alpha(−/−)/LT-alpha(−/−) mice. Journal of Histochemistry and Cytochemistry 49, 989–1001.CrossRefGoogle Scholar
Cosulich, S. C., Savory, P. J. and Clarke, P. R. ( 1999). Bcl-2 regulates amplification of caspase activation by cytochrome c. Current Biology 9, 147–150.CrossRefGoogle Scholar
De Bleecker, J. L., Meire, V. I., Declercq, W. and Van Aken, E. H. ( 1999). Immunolocalization of tumor necrosis factor-alpha and its receptors in inflammatory myopathies. Neuromuscular Disorders 9, 239–246.Google Scholar
Dempsey, P. W., Doyle, S. E., He, J. Q. and Cheng, G. ( 2003). The signaling adaptors and pathways activated by TNF superfamily. Cytokine and Growth Factor Review 14, 193–209.CrossRefGoogle Scholar
Despommier, D. D. ( 1975). Adaptive changes in muscle fibers infected with Trichinella spiralis. American Journal of Pathology 78, 477–496.Google Scholar
Despommier, D. D., Symmans, W. F. and Dell, R. ( 1991). Changes in nurse cell nuclei during synchronous infection with Trichinella spiralis. Journal of Parasitology 77, 290–295.CrossRefGoogle Scholar
Gupta, S. ( 2003). Molecular signaling in death receptor and mitochondrial pathways of apoptosis (Review). International Journal of Oncology 22, 15–20.CrossRefGoogle Scholar
Hsu, H., Xiong, J. and Goeddel, D. V. ( 1995). The TNF receptor-1 associated protein TRADD signal cell death and NF-kB activation. Cell 81, 495–504.CrossRefGoogle Scholar
Jasmer, D. P. ( 1993). Trichinella spiralis infected skeletal muscle cells arrest in G2/M and cease muscle gene expression. Journal of Cell Biology 121, 785–793.CrossRefGoogle Scholar
Korner, H. and Sedgwick, J. D. ( 1996). Tumour necrosis factor and lymphotoxin: molecular aspects and role in tissue-specific autoimmunity. Immunology and Cell Biology 74, 465–472.CrossRefGoogle Scholar
Li, Y. ( 2003). TNF-α is a mitogen in skeletal muscle. American Journal of Physiology: Cell Physiology 285, C370–C376.Google Scholar
Liu, Z. G., Hsu, H., Goeddel, D. V. and Karin, M. ( 1996). Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. Cell 87, 565–576.CrossRefGoogle Scholar
Matsuo, A., Wu, Z., Nagano, I. and Takahashi, Y. ( 2000). Five types of nuclei present in the capsule of Trichinella spiralis. Parasitology 121, 203–210.CrossRefGoogle Scholar
Tews, D. S. and Goebel, H. H. ( 1996). Cytokine expression profile in idiopathic inflammatory myopathies. Journal of Neuropathology and Experimental Neurology 55, 342–347.CrossRefGoogle Scholar
Tracey, K. J. and Cerami, A. ( 1990). Metabolic responses to cachectin/TNF. A brief review. Annals of the New York Academy of Sciences 587, 325–331.CrossRefGoogle Scholar
Vilcek, J. and Lee, T. H. ( 1991). Tumor necrosis factor: New insights into the molecular mechanisms of its multiple actions. Journal of Biological Chemistry 266, 7313–7316.Google Scholar
Vousden, K. H. and Woude, G. F. ( 2000). The ins and outs of p53. Nature, Cell Biology 2, E178–E180.CrossRefGoogle Scholar
Wajant, H., Pfizenmaier, K. and Scheurich, P. ( 2003). Tumor necrosis factor signaling. Cell Death and Differentiation 10, 45–65.CrossRefGoogle Scholar
Warren, G. L., Hulderman, T., Jensen, N., Mckinstry, M., Mishra, M., Luster, M. I. and Simeonova, P. P. ( 2002). Physiological role of tumor necrosis factor alpha in traumatic muscle injury. FASEB Journal 16, 1630–1632.CrossRefGoogle Scholar
Wu, Z., Matsuo, A., Nakada, T., Nagano, I. and Takahashi, Y. ( 2001). Different response of satellite cells in the kinetics of myogenic regulatory factors and ultrastructural pathology after Trichinella spiralis and T. pseudospiralis infection. Parasitology 123, 85–94.CrossRefGoogle Scholar
Wu, Z., Nagano, I., Boonmars, T. and Takahashi, Y. ( 2005). A spectrum of functional genes mobilized after Trichinella spiralis infection in skeletal muscle. Parasitology 130.CrossRefGoogle Scholar
Yao, C. and Jasmer, D. P. ( 2001). Trichinella spiralis-infected muscle cells: abundant RNA polymerase II in nuclear speckle domains colocalizes with nuclear antigens. Infection and Immunity 69, 4065–4071.CrossRefGoogle Scholar
Zador, E., Mendler, L., Takacs, V., De Bleecke, R. J. and Wuytack, F. ( 2001). Regenerating soleus and extensor digitorum longus muscles of the rat show elevated levels of TNF-alpha and its receptors, TNFR-60 and TNFR-80. Muscle and Nerve 24, 1058–1067.CrossRefGoogle Scholar