Enzymatic basis for the structural changes of asparagine-linked sugar chains of membrane glycoproteins of baby hamster kidney cells induced by polyoma transformation - PubMed (original) (raw)

. 1985 Apr 10;260(7):3963-9.

PMID: 2984189

Free article

Enzymatic basis for the structural changes of asparagine-linked sugar chains of membrane glycoproteins of baby hamster kidney cells induced by polyoma transformation

K Yamashita et al. J Biol Chem. 1985.

Free article

Abstract

Previous studies indicated that enrichment of the GlcNAc beta 1----6Man alpha 1---- group with concomitant decrease of the GlcNAc beta 1----4Man alpha 1---- group occurs in the complex-type asparagine-linked sugar chains of the membrane glycoproteins of baby hamster kidney cells transformed by polyoma virus. The enzymatic basis of the chemical change is reported in this paper. By using oligosaccharides isolated from the urine of patients with a variety of exoglycosidase deficiencies, beta-N-acetylglucosaminyltransferases in the cell homogenate were successfully assayed separately. Both baby hamster kidney cells and their polyoma transformants contain beta-N-acetylglucosaminyltransferases I, II, IV, V, and VI, but not beta-N-acetylglucosaminyltransferase III. The beta-N-acetylglucosamine residue added by each beta-N-acetylglucosaminyltransferase (GnT) is shown below. (formula see text) Comparative studies of the specific activities of the five beta-N-acetylglucosaminyltransferases in the two cell lines revealed that the value of beta-N-acetylglucosaminyltransferase V in the polyoma transformant was twice of that in the normal cells, while those of the other four transferases in the two cell lines were not significantly different. Therefore the increase in beta-N-acetylglucosaminyltransferase V may be the direct cause of the changes found in the sugar chains of surface glycoproteins in baby hamster kidney cells transformed by polyoma virus.

PubMed Disclaimer

Cited by

GFPT2/GFAT2 and AMDHD2 act in tandem to control the hexosamine pathway.
Kroef V, Ruegenberg S, Horn M, Allmeroth K, Ebert L, Bozkus S, Miethe S, Elling U, Schermer B, Baumann U, Denzel MS. Kroef V, et al. Elife. 2022 Mar 1;11:e69223. doi: 10.7554/eLife.69223. Elife. 2022. PMID: 35229715 Free PMC article.
Biosynthetic Machinery Involved in Aberrant Glycosylation: Promising Targets for Developing of Drugs Against Cancer.
Vasconcelos-Dos-Santos A, Oliveira IA, Lucena MC, Mantuano NR, Whelan SA, Dias WB, Todeschini AR. Vasconcelos-Dos-Santos A, et al. Front Oncol. 2015 Jun 25;5:138. doi: 10.3389/fonc.2015.00138. eCollection 2015. Front Oncol. 2015. PMID: 26161361 Free PMC article. Review.
Challenge to the suppression of tumor growth by the β4-galactosyltransferase genes.
Furukawa K. Furukawa K. Proc Jpn Acad Ser B Phys Biol Sci. 2015;91(1):1-16. doi: 10.2183/pjab.91.1. Proc Jpn Acad Ser B Phys Biol Sci. 2015. PMID: 25743061 Free PMC article. Review.
Simple sugars to complex disease--mucin-type O-glycans in cancer.
Kudelka MR, Ju T, Heimburg-Molinaro J, Cummings RD. Kudelka MR, et al. Adv Cancer Res. 2015;126:53-135. doi: 10.1016/bs.acr.2014.11.002. Epub 2015 Feb 7. Adv Cancer Res. 2015. PMID: 25727146 Free PMC article. Review.
Enhanced expression of the β4-galactosyltransferase 2 gene impairs mammalian tumor growth.
Tagawa M, Shirane K, Yu L, Sato T, Furukawa S, Mizuguchi H, Kuji R, Kawamura K, Takahashi N, Kato K, Hayakawa S, Sawada S, Furukawa K. Tagawa M, et al. Cancer Gene Ther. 2014 Jun;21(6):219-27. doi: 10.1038/cgt.2014.21. Epub 2014 Jun 6. Cancer Gene Ther. 2014. PMID: 24903013

Enzymatic basis for the structural changes of asparagine-linked sugar chains of membrane glycoproteins of baby hamster kidney cells induced by polyoma transformation - PubMed (original) (raw)