From an increase in the number of tandem repeats through the decrease of sialylation to the downregulation of MUC1 expression level
Syrkina M., Viushkov V., Potashnikova D., Veiko V., Vassetzky Y., Rubtsov M. A.
Journal of Cellular Biochemistry
Vol.120, Issue3, P. 4472-4484
Опубликовано: 2019
Тип ресурса: Статья
Аннотация:
Enhanced glucose uptake by cancer cells was demonstrated in many studies in vitro and in vivo. Glycolysis is one of the main ways of obtaining energy in hypoxia conditions. However, in addition to energy exchange, carbohydrates are also necessary for the posttranslational modification of the protein molecules. Cancer cells are often characterized by an enhanced expression of different glycoproteides. Correct glycosylation defines the structure and activity of such molecules. We demonstrated that under the same cultivation conditions, the intensity of glycosylation does not depend on the total number of potential O-glycosylation sites in one molecule. As a model for the investigation, the tandem repeat region (region with variable number of tandem repeats) of the human mucin MUC1, in which each of the repeats carries four potential O-glycosylation sites, was used. An increase of the tandem repeat number in the recombinant protein did not lead to a proportional increase in the level of s
Ключевые слова:
cancer; cell metabolism; glycosylation; MUC1; sLe a; tandem repeat
agarose; carbohydrate; messenger RNA; mucin 1; nucleotide; recombinant protein; signal peptide; MUC1 protein, human; mucin 1; amino acid sequence; amino terminal sequence; Article; carbohydrate analysis; carboxy terminal sequence; cell membrane; controlled study; down regulation; fluorescence; fusion gene; gene number; human; molecular weight; mRNA expression level; nucleotide sequence; polymerase chain reaction; priority journal; protein processing; reduction (chemistry); sialylation; tandem repeat; amino acid repeat; biosynthesis; cell line; genetics; glycosylation; Cell Line; Down-Regulation; Glycosylation; Humans; Mucin-1; Repetitive Sequences, Amino Acid
Язык текста: Английский
ISSN: 1097-4644
Syrkina M.
Viushkov V.
Potashnikova D.
Veiko V.
Vassetzky Y.
Rubtsov M. A. Mikhail Aleksandrovich 1983-
Сyркина М.
Виушков В.
Поташникова Д.
Веико В.
Вассетзкy Y.
Рубцов М. А. Михаил Александрович 1983-
From an increase in the number of tandem repeats through the decrease of sialylation to the downregulation of MUC1 expression level
Текст визуальный непосредственный
Journal of Cellular Biochemistry
John Wiley & Sons
Vol.120, Issue3 P. 4472-4484
2019
Статья
cancer cell metabolism glycosylation MUC1 sLe a tandem repeat
agarose carbohydrate messenger RNA mucin 1 nucleotide recombinant protein signal peptide MUC1 protein, human mucin 1 amino acid sequence amino terminal sequence Article carbohydrate analysis carboxy terminal sequence cell membrane controlled study down regulation fluorescence fusion gene gene number human molecular weight mRNA expression level nucleotide sequence polymerase chain reaction priority journal protein processing reduction (chemistry) sialylation tandem repeat amino acid repeat biosynthesis cell line genetics glycosylation Cell Line Down-Regulation Glycosylation Humans Mucin-1 Repetitive Sequences, Amino Acid
Enhanced glucose uptake by cancer cells was demonstrated in many studies in vitro and in vivo. Glycolysis is one of the main ways of obtaining energy in hypoxia conditions. However, in addition to energy exchange, carbohydrates are also necessary for the posttranslational modification of the protein molecules. Cancer cells are often characterized by an enhanced expression of different glycoproteides. Correct glycosylation defines the structure and activity of such molecules. We demonstrated that under the same cultivation conditions, the intensity of glycosylation does not depend on the total number of potential O-glycosylation sites in one molecule. As a model for the investigation, the tandem repeat region (region with variable number of tandem repeats) of the human mucin MUC1, in which each of the repeats carries four potential O-glycosylation sites, was used. An increase of the tandem repeat number in the recombinant protein did not lead to a proportional increase in the level of s