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Differences and similarities of nurse cells in cysts of Trichinella spiralis and T. pseudospiralis

Published online by Cambridge University Press:  12 April 2024

T. Boonmars ,
Z. Wu ,
I. Nagano ,
T. Nakada  and
Y. Takahashi
T. Boonmars
Affiliation:
Department of Parasitology, Gifu University School of Medicine, Tsukasa 40, Gifu, 500-8705, Japan
Z. Wu
Affiliation:
Department of Parasitology, Gifu University School of Medicine, Tsukasa 40, Gifu, 500-8705, Japan
I. Nagano
Affiliation:
Department of Parasitology, Gifu University School of Medicine, Tsukasa 40, Gifu, 500-8705, Japan
T. Nakada
Affiliation:
Department of Parasitology, Gifu University School of Medicine, Tsukasa 40, Gifu, 500-8705, Japan
Y. Takahashi*
Affiliation:
Department of Parasitology, Gifu University School of Medicine, Tsukasa 40, Gifu, 500-8705, Japan
*
*Author for correspondence Fax: 058 267 2960 Email: yu3@cc.gifu-u.ac.jp
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Abstract

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The nurse cell in the cyst of Trichinella spiralis comprises at least two kinds of cytoplasm, derived from muscle or satellite cells, as indicated by the pattern of staining using regular dye (haematoxylin and eosin, or toluidine blue), alkaline phosphatase (ALP) expression, acid phosphatase (ACP) expression and immunostaining with an anti-intermediate filament protein (desmin or keratin). Muscle cells undergo basophilic changes following a T. spiralis infection and transform to the nurse cells, accompanied by an increase in ACP activity and the disappearance of desmin. Satellite cells are activated, transformed and joined to the nurse cells but remain eosinophilic. The eosinophilic cytoplasm is accompanied by an increase in desmin and ALP expression but not an increase in ACP activity. Differences in the staining results for ALP or ACP suggest that the two kinds of cytoplasm have different functions. Trichinella pseudospiralis infection results in an increase of ACP activity at a later stage than T. spiralis. There is also a difference in the location pattern of ACP in the cyst of T. spiralis compared with T. pseudospiralis. In T. spiralis, ACP is diffused within the cell, but in T. pseudospiralis, ACP distribution is spotty corresponding to the location of the nucleus. Trichinella pseudospiralis infection is accompanied by a slight increase in ALP activity. Activated satellite cells following a T. pseudospiralis infection exhibit an increase in desmin expression. The present study therefore reveals that nurse cell cytoplasm differs between the two Trichinella species and between the two origins of cytoplasm in the cyst of T. spiralis.

Type
Review Article
Information
Journal of Helminthology , Volume 78 , Issue 1 , March 2004 , pp. 7 - 16
Copyright
Copyright © Cambridge University Press 2004

References

Baeta, A.M., Figarella-Branger, D., Bille-Turc, F., Lepidi, H. & Pellissier, J.F. (1996) Familial desmin myopathies and cytoplasmic body myopathies. Acta Neuropathologica 92, 499–510.CrossRefGoogle ScholarPubMed
Banwell, B.L. (2001) Intermediate filament-related myopathies. Pediatric Neurology 24, 257–263.CrossRefGoogle ScholarPubMed
Bennington, J.L. (1984) Saunders dictionary and encyclopedia of laboratory medicine and technology. 1674 pp. Philadelphia, W.B. Saunders Co. Press.Google Scholar
Borgers, M., De Nollin, S. & Thone, F. (1975) The development of alkaline phosphatase in trichinous muscle. Histochemistry 43, 257–267.CrossRefGoogle ScholarPubMed
Bowen, I.D., den Hollander, J.E. & Lewis, G.H. (1982) Cell death and acid phosphatase activity in the regenerating planarian Polycelis tenuis Iijima . Differentiation 21, 160–167.CrossRefGoogle ScholarPubMed
Brown, K.E., Brunt, E.M. & Heinecke, J.W. (2001) Immunohistochemical detection of myeloperoxidase and its oxidation products in Kupffer cells of human liver. American Journal of Pathology 159, 2081–2088.CrossRefGoogle ScholarPubMed
Bruce, R.G. (1970) The structure and composition of the capsule of Trichinella spiralis in host muscle. Parasitology 60, 223–227.CrossRefGoogle ScholarPubMed
Burstone, S.M. (1962) Enzyme histochemistry and its application in the study of neoplasms.pp. 449–454. London, Academic Press.Google Scholar
Chung, Y.Y. & Ko, R.C. (1999) A novel cDNA clone encoding a specific excretory/secretory antigen of larval Trichinella pseudospiralis . Parasitology Research 85, 685–691.CrossRefGoogle ScholarPubMed
Despommier, D.D. (1975) Adaptive changes in muscle fibers infected with Trichinella spiralis . American Journal of Pathology 78, 477–496.Google ScholarPubMed
Despommier, D.D., Gold, A.M., Buck, S.W., Capo, V. & Silberstein, D. (1990) Trichinella spiralis: secreted antigen of the infective L1 larva localizes to the cytoplasm and nucleoplasm of infected host cells. Experimental Parasitology 71, 27–38.CrossRefGoogle Scholar
Fidzianska, A., Drac, H. & Kaminska, A.M. (1999) Familial inclusion body myopathy with desmin storage. Acta Neuropathologica 97, 509–514.Google ScholarPubMed
Goudeau, B., Dagvadorj, A., Rodrigues-Lima, F., Nedellec, P., Casteras-Simon, M., Perret, E., Langlois, S., Goldfarb, L. & Vicart, P. (2001) Structural and functional analysis of a new desmin variant causing desmin-related myopathy. Human Mutation 18, 338–396.CrossRefGoogle ScholarPubMed
Hadas, E., Gustowska, L. & Janczewska, D. (1995) Histochemical investigations of the biochemical defence mechanism in experimental trichinellosis: I. peroxidase activity. Tropical Medicine and Parasitology 46, 281–283.Google Scholar
Hulinska, D., Shaikenov, B. & Grim, M. (1984) Histochemical differentiation of four species of the genus Trichinella from days 10–40 of their development in muscles of experimentally infected mice. Folia Parasitologica 31, 19–27.Google ScholarPubMed
Ko, R.C., Fan, L., Lee, D.L. & Compton, H. (1994) Changes in host muscles induced by excretory/secretory products of larval Trichinella spiralis and Trichinella pseudospiralis . Parasitology 108, 195–205.CrossRefGoogle ScholarPubMed
Lee, D.L., Ko, R.C., Yi, X.Y. & Yeung, M.H. (1991) Trichinella spiralis : antigenic epitopes from the stichocytes detected in the hypertrophic nuclei and cytoplasm of the parasitized muscle fibre (nurse cell) of the host. Parasitology 102, 117–123.CrossRefGoogle ScholarPubMed
Li, Z., Mericskay, M., Agbulut, O., Butler-Browne, G., Carlsson, L., Thornell, L.E., Babinet, C. & Paulin, D. (1997) Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. Journal of Cell Biology 139, 129–144.CrossRefGoogle Scholar
Lodish, H., Berk, A., Zipursky, S.L., Matsudaira, P., Baltimore, D. & Darnell, J. (2000) Molecular cell biology. 4th edn. 1084 pp. New York, Von Hoffman Press.Google Scholar
Matsuo, A., Wu, Z., Nagano, I. & Takahashi, Y. (2000) Five types of nuclei present in the cyst of Trichinella spiralis . Parasitology 121, 203–210.CrossRefGoogle Scholar
Michejda, J.W. & Boczon, K. (1972) Changes in bioenergetics of skeletal muscle mitochondria during experimental trichinosis in rats. Experimental Parasitology 31, 161–171.CrossRefGoogle ScholarPubMed
Milner, D.J., Weitzer, G., Tran, D., Bradley, A. & Capetanaki, Y. (1996) Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. Journal of Cell Biology 134, 1255–1270.CrossRefGoogle ScholarPubMed
Morimoto, K., Amano, H., Sonoda, F., Baba, M., Senba, M., Yoshimine, H., Yamamoto, H., Ii, T., Oishi, K. & Nagatake, T. (2001) Alveolar macrophages that phagocytose apoptotic neutrophils produce hepatocyte growth factor during bacterial pneumonia in mice. American Journal of Respiratory Cell and Molecular Biology 24, 608–615.CrossRefGoogle ScholarPubMed
Nakano, S., Engel, A.G., Waclawik, A.J., Emslie-Smith, A.M. & Busis, N.A. (1996) Myofibrillar myopathy with abnormal foci of desmin positivity. I. Light and electron microscopy analysis of 10 cases. Journal of Neuropathology and Experimental Neurology 55, 549–562.CrossRefGoogle ScholarPubMed
Pellissier, J.F., Pouget, J., Charpin, C. & Figarella, D. (1989) Myopathy associated with desmin type intermediate filaments. An immunoelectron microscopic study. Journal of the Neurological Sciences 89, 49–61.CrossRefGoogle ScholarPubMed
Posen, S. (1967) Alkaline phosphatase. Annals of Internal Medicine 67, 183–203.Google ScholarPubMed
Stevens, A. & Palmer, J. (1996) Enzyme histochemistry: diagnostic applications. pp. 411–420 in Bancroft, J.D. and Stevens, A. (Eds) Theory and practice of histological techniques. 4th edn. Nottingham, Churchill Livingstone Press.Google Scholar
Telerman-Toppet, N., Bauherz, G. & Nol, S. (1991) Auriculo-ventricular block and distal myopathy with rimmed vacuoles and desmin storage. Clinical Neuropathology 10, 61–64.Google ScholarPubMed
Vajsar, J., Becker, L.E., Freedom, R.M. & Murphy, E.G. (1993) Familial desminopathy: myopathy with accumulation of desmin-type intermediate filaments. Journal of Neurology, Neurosurgery and Psychiatry 56, 644–648.CrossRefGoogle ScholarPubMed
Vassilatis, D.K., Despommier, D., Misek, D.E., Polvere, R.I., Gold, A.M., Van Der Ploeg, L.H. (1992) Analysis of a 43-kDa glycoprotein from the intracellular parasitic nematode Trichinella spiralis . Journal of Biological Chemistry 267, 18459–18465.CrossRefGoogle ScholarPubMed
Visser, J.E., Smith, D.W., Moy, S.S., Breese, G.R., Friedmann, T., Rothstein, J.D. & Jinnah, H.A. (2002) Oxidative stress and dopamine deficiency in a genetic mouse model of Lesch-Nyhan disease. Developmental Brain Research 133, 127–139.CrossRefGoogle Scholar
Wang, X., Osinska, H., Dorn, G.W., Nieman, M., Lorenz, J.N., Gerdes, A.M., Witt, S., Kimball, T., Gulick, J. & Robbins, J. (2001) Mouse model of desmin-related cardiomyopathy. Circulation 103, 2402–2407.CrossRefGoogle ScholarPubMed
Wu, Z., Nagano, I. & Takahashi, Y. (1998) Differences and similarities between Trichinella spiralis and T. pseudospiralis in morphology of stichocyte granules, peptide maps of excretory and secretory (E–S) products and messenger RNA of stichosomal glycoproteins. Parasitology 116, 61–66.CrossRefGoogle Scholar
Wu, Z., Matsuo, A., Nakada, T., Nagano, I. & 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 ScholarPubMed
Xu, D., Wu, Z., Nagano, I. & Takahashi, Y. (1997) A muscle larva of Trichinella pseudospiralis is intracellular, but does not form a typical cyst wall. Parasitology International 46, 1–5.CrossRefGoogle Scholar
Zarlenga, D.S. & Gamble, H.R. (1995) Molecular cloning and expression of an immunodominant 53-kDa excretory-secretory antigen from Trichinella spiralis muscle larvae. Molecular and Biochemical Parasitology 42, 165–174.CrossRefGoogle Scholar