Vol.45, No.3, 2021, pp.773-783, doi:10.32604/biocell.2021.014233
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ARTICLE
Overloading of differentiated Caco-2 cells during lipid transcytosis induces glycosylation mistakes in the Golgi complex
  • GALINA N. DENISOVA1, IVAN D. DIMOV1, ANNA V. ZAITSEVA1,2, LINARD J. ARTIUX3, ALEXANDER A. MIRONOV1,4,*, NATALIA R. KARELINA1
1 Department of Anatomy, Saint Petersburg State Paediatric Medical University, Petersburg, 194100, Russia
2 Department of Biochemistry, Saint Petersburg State Paediatric Medical University, Petersburg, 194100, Russia
3 Department of Heart and Vessel Surgery, Saint Petersburg State Paediatric Medical University, Petersburg, 194100, Russia
4 The FIRC Institute of Molecular Oncology, Milan, 20139, Italy
* Corresponding Author: Alexander A. Mironov. Email:
Received 12 September 2020; Accepted 27 December 2020; Issue published 03 March 2021
Abstract
Overloading the intestine enterocytes with lipids induced alteration of the Golgi complex (GC; ) and could cause glycosylation errors. Here, using differentiated Caco-2 cells with the established 0[I] blood group phenotype (no expression of the blood antigens A and B [AgA, AgB] under normal conditions) as a model of human enterocytes we examined whether the overloading of these cells with lipids could cause errors in the Golgi-dependent glycosylation. We demonstrated that under these conditions, there were alterations of the GC and the appearance of lipid droplets in the cytoplasm. Rare cells produced AgA and AgB. This suggested that after overloading of enterocytes with lipids, AgA were mistakenly synthesized in individual enterocytes by the Golgi glycosyltransferases. These mistakes could explain why in the absence of AgA and AgB antibodies against them exist in the blood.
Keywords
Golgi; Blood group antigens; Glycosylation errors; Enterocyte; Lipid transcytosis; Caco-2 cells
Cite This Article
DENISOVA, G. N., DIMOV, I. D., ZAITSEVA, A. V., ARTIUX, L. J., MIRONOV, A. A. et al. (2021). Overloading of differentiated Caco-2 cells during lipid transcytosis induces glycosylation mistakes in the Golgi complex. BIOCELL, 45(3), 773–783.
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