Expression of beta-N-acetylgalactosaminylated N-linked sugar chains is associated with functional differentiation of bovine mammary gland

Journal of Biochemistry
T SatoK Furukawa

Abstract

During lactation the mammary gland synthesizes a large amount of glycoproteins including those composing milk fat globule membrane (MFGM). Our previous study showed that N-linked sugar chains with GalNAc beta1-->4GlcNAc structure appears to increase in bovine MFGM glycoproteins during early lactation [Ujita et al. (1993) FEBS Lett. 332, 119-122]. Western blot analysis of membrane glycoproteins from lactating and post-lactating bovine mammary glands using Wistaria floribunda agglutinin (WFA), which binds oligosaccharides terminating with beta-N-acetylgalactosamine, and Ricinus communis agglutinin-I (RCA-I), which binds oligosaccharides preferentially terminating with beta-1,4-galactose, showed that the number and reactivity of protein bands to WFA but not to RCA-I decrease drastically in the post-lactating mammary sample. Establishment of primary cultured epithelial cells from lactating bovine mammary gland and their culture on collagen-coated dishes in the presence of a mixture of lactogenic hormones revealed that N-linked sugar chains with GalNAc beta1-->4GlcNAc structure are expressed in the functionally differentiated cells without altering the apparent beta-galactosylation of the oligosaccharides. These results strongly sug...Continue Reading

Citations

Feb 9, 2010·Bioscience, Biotechnology, and Biochemistry·Mizuho InagakiTohru Suzuki
Jul 9, 2014·BioMed Research International·Kiyoko HiranoKiyoshi Furukawa
Apr 25, 2003·International Journal of Cancer. Journal International Du Cancer·Noriaki KitamuraKiyoshi Furukawa
Nov 4, 2020·Proceedings of the National Academy of Sciences of the United States of America·Jua LeeHyun Joo An
Dec 13, 2019·Journal of Agricultural and Food Chemistry·Rivca L Valk-WeeberSander S van Leeuwen

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