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1998 | 45 | 3 |

Tytuł artykułu

Age-related profile of beta-N-acetylhexosaminidase glycosylation in rat liver

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
β-N-acetylhexosaminidase was prepared from a liver lysosomal fraction obtained from rats between 18 days of gestation (group I) and 72 weeks of age (groups II-VI). A glycan chain analysis was performed after an electrophoresis and blotting, followed by a very sensitive detection system with highly specific digoxigenin-labelled lectins. The presence of high-mannose /hybrid type glycans, as well as their fucosylated forms was shown in all the experimental groups. Complex-type glycans with terminal sialic acid or galactose were present in all the groups except for 1-week-old rats in which only a positive reaction with lectins from Galanthus nivalis and Aleuria aurantia - was observed. Thus it may be assumed that age-related changes in the glycosylation pattern occur on the first days after birth.

Wydawca

-

Rocznik

Tom

45

Numer

3

Opis fizyczny

p.791-797,fig.

Twórcy

autor
  • Jagiellonian University, R.Ingardena 6, 30-060 Krakow, Poland
autor

Bibliografia

  • 1. Sagherian, C.f Poroszlay, P., Vavougios, G. & Mahuran, D. (1993) Proteolytic processing of the pro/? chain of /^-hexosaminidase occurs at basic residues contain within an exposed disul­fide loop structure. Biochem. Cell. Biol. 71, 340-347.
  • 2. Church, W.B., Swensen, L.f James, M.N.G. & Mahuran, D. (1992) Crystallization of human /^-hexosaminidase B. J. Mol. Biol 227, 577-580.
  • 3. Mahuran, D J. (1990) Characterization of hu­man placental /^-hexosaminidase I2. J. Biol. Chem. 265, 6794-6799.
  • 4. Sonderfeld-Fresko, S. & Proia, R.L. (1989) Analysis of the glycosylation and phosphoryla­tion of the lysosomal enzyme /3-hexosamini- dase B, by site-directed mutagenesis. J. Biol. Chem. 264, 7692-7697.
  • 5. Wietz, G. & Proia, R.L. (1992) Analysis of the glycosylation and phosphorylation of the a- subunit of the lysosomal enzyme, ^-hexo­saminidase A, by site-directed mutagenesis. J. Biol Chem. 267, 10039-10044.
  • 6. Quon, D.V.K., Proia, R.L., Fowler, A.V., Blei- baum, J. & Neufeld, E.F. (1989) Proteolytic processing of the /?-subunit of the lysosomal enzyme, /^-hexosaminidase, in normal human fibroblasts. J. Biol Chem. 264, 3380-3384.
  • 7. Mahuran, D.J., Noete, K., Klavins, M.H., Le­ung, A. & Grave, R.A. (1988) Proteolytic proc­essing of pro-« and proprecursors from hu­man /^-hexosaminidase. J. Biol Chem. 263, 4612-4618.
  • 8. Mahuran, D. & Lowden, J.A. (1980) The subunit and polypeptide structure of hexo­saminidase from human placenta. Can. J. Bio- chem. 58, 287-294.
  • 9. Kornfeld, S. (1990) Lysosomal enzyme target­ing. Biochem. Soc. Trans. 18, 357-374.
  • 10. Kobata, A. (1992) Structures and functions of the sugar chains of glycoproteins. Eur. J. Bio­chem. 209, 483-501.
  • 11. Kato, S., Oda-Tamai, S. & Akamatsu, N. (1988) Postnatal changes in N-linked oligosaccha­rides of glycoproteins in rat liver. Biochem. J. 253, 59-66.
  • 12. Olea, M.T. & Nagata, T. (1991) Quantitative assessment of lysosomal size, number and en­zyme activity in mouse kidney during matu ra­tional development. Cell Mol Biol 37, 679-685.
  • 13. Dc Duve, C., Pressman, B.B., Gianetto, R., Wattiaux, R. & Appelmans, F. (1955) Intracel­lular distribution patterns of enzymes in rat liver tissue. Biochem. J. 60, 604-617.
  • 14. Wójczyk, B., Hoja, D. & Lityńska, A. (1991) Pu­rification of /^-glucuronidase and structural as­sessment of the carbohydrate chains by lectin affinity immunoelectrophoresis. Glycoconju- gate J. 8, 340-349.
  • 15. Chenais, F., Virella, G. & Patrick, C.C. (1977) Isolation of soluble immuno complex by affin­ity chromatography using staphylococcal pro­tein A-Scpharose as substrate. J. Immunol Methods 18, 183-192.
  • 16. Affinity Chromatography: Principles and Meth­ods (1979) p. 15, Pharmacia Fine Chemicals Uppsala.
  • 17. Haselbcck, A., Schickaneder, E., von der Eltz, H. & Hosel, W. (1990) Structural characteriza­tion of glycoprotein carbohydrate chains by using digoxigenin-labeled lectins on blot. Anal. Biochem. 191, 25-30.
  • 18. Towbin, H., SUtekelm, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from poly- acrylamide gels to nitrocellulose sheets: Proce­dure and some applications. Proc. Natl Acad. Sci. U.S.A. 76, 4350-4354.
  • 19. Laemmli, U.K. (1970) Maturation of the head of bacteriophage T4. Nature 227, 690-685.
  • 20. Kaplan, H.A. & Jamieson, J.C. (1977) The ef­fect of inflammation on the rat liver /?-galacto- sidase and /3-JV-acetylglucosaminidase. Life Sciences 21, 1311-1316.
  • 21. Bradford, M M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem, 72, 248-254.
  • 22.0'Dowd, B.F. & Mahuran, D. (1984) Charac­terization by nuclear magnetic resonance of the concanavalin A binding oligosaccharides on the j3\y chain of placental /^-hexosaminidase B: Lectin binding to the separated polypeptide chains of hexosaminidases A and B. Can. J. Biochem. Cell. Biol 63, 723-729.
  • 23.0'Dowd, B.F., Cummings, D.A., Gravel. R.A. & Mahuran, D. (1988) Oligosaccharide structure and amino acid sequence of the major glyco- peptides of mature human /^-hexosaminidase. Biochemistry 27, 5216-5226.
  • 24. Hasilik, A. & Neufeld. E.F. (1980) Biosynthe­sis of lysosomal enzymes in fibroblasts. J. Biol Chem. 255, 4937-4935.
  • 25. Hasilik, A. & von Figura, K. (1981) Oligosac­charides in lysosomal enzymes. Eur. J. Bio­chem. 121, 125-129.
  • 26. Bianchi, R.A., Fogal, T., Bertini, F. & Sosa, M.A. (1995) Lysosomal enzyme activity in rat adrenal gland related to the postnatal develop­ment. Mechanisms Aging Dev. 84, 151-156.
  • 27. Oda-Tamai, S., Kato, S. & Akamatsu, N. (1991) Postnatal changes in sialylation of glycopro­teins in rat liver. Biochem. J. 280, 179-185.
  • 28. Sosa, M.A., Bclmonte, S. & Bertini, F. (1996) Changes in iV-acetyl-^-D-glucosaminidase bind­29. ing system in rat liver during growth. Mecha­nisms Aging Dev. 86, 75-81.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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