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Chemical Compound Review:

SureCN542627 N-[(2S,3R,4R,5R,6R)-4,5- dihydroxy-6...

Synonyms: ZINC05167371, AR-1L8552, FT-0662639, AC1L3U9J, 3554-93-6, ...

Kojima, N. et al., Nakano, T. et al., Byrd, J.C. et al., Niv, Y. et al., Muto, S. et al., et al.

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Disease relevance of benzyl-alpha-N-acetylgalactosamine

The adhesion of the myelogenous leukemia cell line, HL60, to fibronectin and its fragments, heparin binding fragment (40 kDa) and cell attachment fragment (120 kDa), was enhanced by culturing with benzyl-alpha-GalNAc (BZ alpha GalNAc) [1].
Previous studies from our laboratory have shown that benzyl-alpha-GalNAc inhibits the glycosylation of mucin in colon cancer cells [2].
Inhibition of mucin synthesis by benzyl-alpha-GalNAc in KATO III gastric cancer and Caco-2 colon cancer cells [2].
Benzyl-alpha-GalNAc inhibits sialylation of O-glycosidic sugar chains on CD44 and enhances experimental metastatic capacity in B16BL6 melanoma cells [3].

High impact information on benzyl-alpha-N-acetylgalactosamine

Benzyl-N-acetyl-alpha-D-galactosaminide induces a storage disease-like phenotype by perturbing the endocytic pathway [4].
Inhibition of O-linked glycosylation by benzyl-N-acetyl-alpha-d-galactosaminide affects significantly the sorting behavior of DPPIV in intestinal Caco-2 and HT-29 cells [5].
Inhibition of O-glycosylation by benzyl-N-acetyl-alpha-D-galactosaminide (benzyl-GalNAc) was accompanied by a dramatic shift in the sorting of SI from the apical membrane to both membranes [6].
Virus attachment to both cell lines is CD55 independent and sensitive to benzyl N-acetyl-alpha-D-galactosaminide, an inhibitor of O-linked glycosylation [7].
EV70 binding to all cell lines was sensitive to sialidase treatment and to inhibition of O glycosylation by benzyl N-acetyl-alpha-D-galactosaminide [8].

Biological context of benzyl-alpha-N-acetylgalactosamine

Cell adhesion to fibronectin before and after treatment with BZ alpha GalNAc or TPA was inhibited by anti-VLA4 and anti-VLA5 monoclonal antibodies [1].

Anatomical context of benzyl-alpha-N-acetylgalactosamine

On the other hand, the known functions of CD44, such as adhesion to hyaluronate, fibronectin, collagen, and endothelial cells, as well as homotypic aggregation, were not affected by benzyl-alpha-GalNAc regardless of the enhancement of metastatic ability induced by this glycosylation inhibitor [3].

Associations of benzyl-alpha-N-acetylgalactosamine with other chemical compounds

These effects of MUC1 mucin over-expression in MKN74 cells were abolished by the treatment of transfectants with an inhibitor of O-glycan biosynthesis, benzyl-alpha-GalNAc [9].
The mucinous nature of the labelled high-molecular glycoprotein was verified by enzymatic degradation treatments (heparinase, hyaluronidase, chondroitinase ABC, and N-glycanase), alkaline-borohydride treatment, inhibition of labelling by the glycosylation inhibitor benzyl-alpha-GalNAc, and by CsCl-density-gradient centrifugation [10].
The MBL binding to Colo205 cells was more strongly reduced by the pretreatment of the cells with an O-linked glycosylation inhibitor, benzyl-2-acetamide-2-deoxy-alpha-galactopyranoside (Bz-alpha-GalNAc), rather than an N-linked glycosylation inhibitor, tunicamycin [11].

Gene context of benzyl-alpha-N-acetylgalactosamine

Expression of peptide epitopes associated with MUC1 apomucins was increased by benzyl-alpha-GalNAc [12].
In conclusion, benzyl-N-acetyl-alpha-D-galactosaminide induces abnormal O-glycosylation and altered regulation of MUC5AC secretion [13].
Treatment of the cells with benzyl-alpha-GalNAc also decreased their binding to E-selectin (ELAM-1), which recognizes sialyl Lea and sialyl Lex [14].
The expression of VLA4 and VLA5 did not change during treatment with BZ alpha GalNAc or TPA [1].
In this study, we determined whether benzyl-alpha-GalNAc inhibits mucin glycosylation in KATO III gastric cancer cells [2].

References

Role of cell surface O-linked oligosaccharides in adhesion of HL60 cells to fibronectin: regulation of integrin-dependent cell adhesion by O-linked oligosaccharide elongation. Kojima, N., Saito, M., Tsuji, S. Exp. Cell Res. (1994) [Pubmed]
Inhibition of mucin synthesis by benzyl-alpha-GalNAc in KATO III gastric cancer and Caco-2 colon cancer cells. Byrd, J.C., Dahiya, R., Huang, J., Kim, Y.S. Eur. J. Cancer (1995) [Pubmed]
Benzyl-alpha-GalNAc inhibits sialylation of O-glycosidic sugar chains on CD44 and enhances experimental metastatic capacity in B16BL6 melanoma cells. Nakano, T., Matsui, T., Ota, T. Anticancer Res. (1996) [Pubmed]
Benzyl-N-acetyl-alpha-D-galactosaminide induces a storage disease-like phenotype by perturbing the endocytic pathway. Ulloa, F., Real, F.X. J. Biol. Chem. (2003) [Pubmed]
Intestinal dipeptidyl peptidase IV is efficiently sorted to the apical membrane through the concerted action of N- and O-glycans as well as association with lipid microdomains. Alfalah, M., Jacob, R., Naim, H.Y. J. Biol. Chem. (2002) [Pubmed]
O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts. Alfalah, M., Jacob, R., Preuss, U., Zimmer, K.P., Naim, H., Naim, H.Y. Curr. Biol. (1999) [Pubmed]
Enterovirus 70 binds to different glycoconjugates containing alpha2,3-linked sialic acid on different cell lines. Nokhbeh, M.R., Hazra, S., Alexander, D.A., Khan, A., McAllister, M., Suuronen, E.J., Griffith, M., Dimock, K. J. Virol. (2005) [Pubmed]
Binding to decay-accelerating factor is not required for infection of human leukocyte cell lines by enterovirus 70. Haddad, A., Nokhbeh, M.R., Alexander, D.A., Dawe, S.J., Grisé, C., Gulzar, N., Dimock, K. J. Virol. (2004) [Pubmed]
Increased invasiveness of MUC1 and cDNA-transfected human gastric cancer MKN74 cells. Suwa, T., Hinoda, Y., Makiguchi, Y., Takahashi, T., Itoh, F., Adachi, M., Hareyama, M., Imai, K. Int. J. Cancer (1998) [Pubmed]
Mucin synthesis and secretion in relation to spontaneous differentiation of colon cancer cells in vitro. Niv, Y., Byrd, J.C., Ho, S.B., Dahiya, R., Kim, Y.S. Int. J. Cancer (1992) [Pubmed]
Human mannose-binding lectin preferentially binds to human colon adenocarcinoma cell lines expressing high amount of Lewis A and Lewis B antigens. Muto, S., Sakuma, K., Taniguchi, A., Matsumoto, K. Biol. Pharm. Bull. (1999) [Pubmed]
E-selectin binding by pancreatic tumor cells is inhibited by cancer sera. Sawada, T., Ho, J.J., Chung, Y.S., Sowa, M., Kim, Y.S. Int. J. Cancer (1994) [Pubmed]
Permanent exposure of mucin-secreting HT-29 cells to benzyl-N-acetyl-alpha-D-galactosaminide induces abnormal O-glycosylation of mucins and inhibits constitutive and stimulated MUC5AC secretion. Hennebicq-Reig, S., Lesuffleur, T., Capon, C., De Bolos, C., Kim, I., Moreau, O., Richet, C., Hémon, B., Recchi, M.A., Maës, E., Aubert, J.P., Real, F.X., Zweibaum, A., Delannoy, P., Degand, P., Huet, G. Biochem. J. (1998) [Pubmed]
Effect of benzyl-alpha-GalNAc, an inhibitor of mucin glycosylation, on cancer-associated antigens in human colon cancer cells. Huang, J., Byrd, J.C., Yoon, W.H., Kim, Y.S. Oncol. Res. (1992) [Pubmed]

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