Have a personal or library account? Click to login
The synthesis of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE), α-dystroglycan, and β-galactoside α-2,3-sialyltransferase 6 (ST3Gal6) by skeletal muscle cell as a response to infection with Trichinella spiralis Cover

The synthesis of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE), α-dystroglycan, and β-galactoside α-2,3-sialyltransferase 6 (ST3Gal6) by skeletal muscle cell as a response to infection with Trichinella spiralis

Open Access
|Dec 2022

References

  1. Barresi, R., Campbell, K.P. (2006): Dystroglycan: from biosynthesis to pathogenesis of human disease. J Cell Sci, 119(2): 199–207. DOI: 10.1242/jcs.02814
  2. Broccolini, A., Gidaro, T., De Cristofaro, R., Morosetti, R., Gliubizzi, C., Ricci, E., Tonali, P.A., Mirabella, M. (2008): Hyposialylation of neprilysin possibly affects its expression and enzymatic activity in hereditary inclusion-body myopathy muscle. J Neurochem, 105(3): 971–981. DOI: 10.1111/j.1471-4159.2007.05208.x Broccolini, A., Gidaro, T., Morosetti, R., Mirabella, M. (2009): Hereditary inclusion-body myopathy: clues on pathogenesis and possible therapy. Muscle Nerve, 40(3): 340–349. DOI: 10.1002/mus.21385
  3. Cohn, R.D. (2005): Dystroglycan: important player in skeletal muscle and beyond. Neuromusc Dis, 15(3): 207–217. DOI: 10.1016/j.nmd.2004.11.005
  4. Combs, A.C., Ervasti, J.M. (2005): Enhanced laminin binding by alpha-dystroglycan after enzymatic deglycosylation. Biochem J, 390(1): 303–309. DOI: 10.1042/BJ20050375
  5. Cox, M.L., Schary, C.L., Luster, C.W., Stewart, Z.S., Korytko, P.J., Khan, K.N.M., Paulauskis, J.D., Dunston, R.W. 2006: Assestment of fixatives, fixation, and tissue processing on morphology and RNA integrity. Exp Mol Pathol, 80(2): 183–191. DOI: 10.1016/j.yexmp.2005.10.002
  6. Dalangood, S., Zhu, Zh., Ma, Zh., Li, J., Zeng, Q., Yan, Y., Shen, B., Yan, J., Huang, R. (2020): Identification of glycogene-type and validation of ST3Gal6 as a biomarker predicts clinical outcome and cancer cell invasion in urinary bladder cancer. Theranostics, 10(22): 10078–10091. DOI: 10.7150/thno.48711
  7. Despommier, D.D. (1998): How does Trichinella spiralis make itself at home? Parasitol Today, 14(8): 318–23. DOI: 10.1016/s0169-4758(98)01287-3
  8. Glavey, S.V., Cunningham, S., Murillo, L.S., Loughrey, C., Wu, P., Cairns, M., Gill, S.K., Kruger, A., Gerlach, J.Q., Kane, M., Morgan, G.J., Joshi, L., O`Dwyer, M.E. (2012): Glycosylation-related gene expression is dysregulated in multiple myeloma and overexpression of the sialyltransferase ST3Gal6 is associated with inferior survival. In Abstracts of Myeloma – Biology and Pathophysiology, Excluding Therapy: Poster II. November 16, 2012. Blood, 120 (21): 2931. DOI: 10.1182/blood.V120.21.2931.2931
  9. Hanisch, F., Weidemann, W., Grossmann, M., Joshi, P.R., Holzhausen, H.J., Stoltenburg, G., Weis, J., Zierz, S., Horstkorte, R. (2013): Sialylation and muscle performance: Sialic acid is a marker of muscle ageing. PLOS One, 8(12): e80520. DOI: 10.1371/journal.pone.0080520
  10. Hinderlich, S., Stäsche, R., Zeitler, R., Reutter, W. (1997): A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. J Biol Chem, 272(39): 24313–24318. DOI: 10.1074/jbc.272.39.24313
  11. Horstkorte, R., Nöhring, S., Wiechens N., Scwarzkopf, M., Danker, K., Reutter, W., Lucka, L. (1999): Tissue expression and amino acid sequence of murine UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase. Eur J Biochem, 260(3): 923–927. DOI: 10.1046/j.1432-1327.1999.00253.x
  12. Johnson, D., Montpetit, M.L., Stocker, P.J., Bennett, E.S. (2004): The sialic acid component of the βsubunit modulates voltage-gat-1 ed sodium channel function. J Biol Chem, 279(43): 44303–44310. DOI: 10.1074/jbc.M408900200
  13. Lapidos, K.A., Kakar, R., McNally, E.M. (2004): The dystrophin glycoprotein complex. Signalling strength and integrity for the sarcolemma. Circ Res, 94(8): 1023–1031. DOI: 10.1161/01.RES.0000126574.61061.25
  14. Marini, M., Ambrosini, S., Sarchielli, E., Thyrion, G.D., Bonacini, L., Vannelli, G.B., Sgambati E. (2014): Expression of sialic acids in human adult skeletal muscle tissue. Acta Histochem, 116(5): 926–935. DOI: 10.1016/j.acthis.2014.03.005
  15. McDearmon, E.L., Combs, A. C., Ervasti, J.M. (2003): Core 1 glycans on α-dystroglycan mediate laminin-induced acetylcholine receptor clustering but not laminin binding. J Biol Chem, 278(45): 44868–44873. DOI: 10.1074/jbc.M307026200
  16. Milcheva, R., Ivanov, D., Iliev, I., Russev, R., Petkova, S., Babál, P. (2015): Increased sialylation as a phenomenon in the accommodation of the parasitic nematode Trichinella spiralis (Owen, 1835) in skeletal muscle fibres. Folia Parasitol, 7(62): 2015.049. DOI: 10 14411/fp.2015.049
  17. Milcheva, R., Janega, P., Celec, P., Petkova, S., Hurniková, Z., Izrael-Vlková B., Todorova, K., Babál, P. (2019): Accumulation of α-2,6-sialoglycoproteins in the muscle sarcoplasm due to Trichinella sp. invasion. Open Life Sci, 14: 470–481. DOI: 10.1515/boil-2019-0053
  18. Milcheva, R.S., Janega, P., Petkova, S.L., Todorova, K.S., Ivanov, D.G., Babál, P. (2020): Absence of ST3Gal2 and ST3Gal4 sialyltransferase expressions in the Nurse cell of Trichinella spiralis Bul J Vet Med, Online First. DOI: 10.15547/bjvm.2020-0006
  19. Nakamura, K., Tsukimoto, Y., Hijiya, N., Niguchi, Y., Yano, S., Yokoyama, S., Kumamoto, T., Moriyama, M. (2010): Induction of GNE in myofibers after muscle injury. Pathobiology, 77(4): 191–199. DOI: 10.1159/000292652
  20. Nonaka, I., Noguchi, S., Nishino I. (2005): Distal myopathy with rimmed vacuoles and hereditary inclusion body myopathy. Curr Neurol Neurosci Rep, 5(1): 61–65. DOI: 10.1007/s11910-005-0025-0
  21. Petrof, B.J., Shrager, J.B., Stedman, H.H., Kelly, A.M., Sweeney, H.L. (1993): Dystrophin protects the sarcolemma from stresses developed during muscle contraction. Proc Natl Acad Sci USA, 90(8): 3710–3714. DOI: 10.1073/pnas.90.8.3710
  22. Sasaki, T., Yamada, H., Matsumura, K., Shimizu, T., Kobata, A., Endo, T. (1998): Detection of O-mannosyl glycans in rabbit skeletal muscle α-dystroglycan. Biochim Biophys Acta, 1425(3): 599–606. DOI: 10.1016/s0304-4165(98)00114-7
  23. Schauer, R. (2009): Sialic acids as regulators of molecular and cellular interactions. Curr Opin Struct Biol, 19(5): 507–514. DOI: 10.1016/j.sbi.2009.06.003
  24. Schwetz, T.A., Norring, N.A., Ednie, A.R., Bennett, E.S. (2011): Sialic Acids Attached to O-Glycans Modulate Voltage-gated Potassium Channel Gating. J Biol Chem, 286(6): 4123–4132. DOI: 10.1074/jbc.M110.171322
  25. Stäsche, R., Hinderlich, S., Weise, C., Effertz, K., Lucka, L., Moormann, R., Reutter, W. (1997): A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. J Biol Chem, 272(39): 24319–24324. DOI: 10.1074/jbc.272.39.24319
  26. Sun, M., Zhao, X., Liang, L., Pan, X., Lv, X., Zhao Y. (2017): Sialyltransferase ST3Gal6 mediates the effect of microRNA-26a on cell growth, migration, and invasion in hepatocellular carcinoma through the protein kinase B/mammalian target of rapamycin pathway. Cancer Sci, 108 (2): 267–276. DOI: 10.1111/cas.13128
  27. Takashima, S. (2008): Characterization of mouse sialyltransferase genes: their evolution and diversity. Biosci Biotechnol Biochem, 72(5): 1155–1167. DOI: 10.1271/bbb.80025
  28. Varki, A. (2007): Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins. Nature, 446: 1023–1029. DOI: 10.1038/nature05816
  29. Varki,, A. (1997): Sialic acids as ligands in recognition phenomena. FASEB J, 11(4): 248–255. DOI: 10.1096/fasebj.11.4.9068613 Weidemann, W., Klukas, C., Klein, A., Simm, A., Schreiber, F., Horstkorte, R. (2010): Lessons from GNE – deficient embryonic stem cells: sialic acid biosynthesis is involved in proliferation and gene expression. Glycobiology, 20(1): 107–117. DOI: 10.1093/glycob/cwp153
  30. Wu, Z., Nagano, I., Takahashi, Y. (2008a): Candidate genes responsible for common and different pathology of infected muscle tissues between Trichinella spiralis and T. pseudospiralis infection. Parasitol Int, 57(3): 368–378. DOI: 10.1016/j.parint.2008.03.005 Wu, Z., Sofronic-Milosavljevic, L., Nagano, I., Takahashi, Y. (2008b): Trichinella spiralis: nurse cell formation with emphasis on analogy to muscle cell repair. Parasit Vectors, 1(1): 27. DOI: 10.1186/1756-3305-1-27
  31. Ye, J., Coulouris, G., Zaretskaya, I., Cutcutache, I., Rozen, S., Madden, T. (2012): Primer-BLAST: A tool to design target-specific primers for polymerase chain reaction. BMC Bioinformatics, 13: 134. DOI: 10.1186/1471-2105-13-134
  32. Zarlenga, D.S., Chute, M.B., Martin, A., Kapel, C.M.O. (2001): A single, multiplex PCR for differentiating all species of Trichinella Parasite, 8(2): S24 – S26. DOI: 10.1051/parasite/200108s2024
  33. Zhang, J.D., Ruschhaupt, M., Biczok, R. (2014): ddCt method for qRT-PCR data analysis. Retrieved October 2021 from http://bioconductor.jp/packages/2.14/bioc/vignettes/ddCt/inst/doc/rtPCR.pdf
DOI: https://doi.org/10.2478/helm-2022-0027 | Journal eISSN: 1336-9083 | Journal ISSN: 0440-6605
Language: English
Page range: 217 - 225
Submitted on: Mar 22, 2022
|
Accepted on: Aug 17, 2022
|
Published on: Dec 17, 2022
In partnership with: Paradigm Publishing Services
Publication frequency: 4 issues per year

© 2022 R. Milcheva, K. Todorova, A. Georgieva, S. Petkova, published by Slovak Academy of Sciences, Institute of Parasitology
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.