Differences in the sialylation patterns of membrane stress proteins in chemical carcinogen-induced tumors developed in BALB/c and IL-1alpha deficient mice.
We evaluated the patterns of sialylation on fibrosarcoma cell lines arising following 3-methylcholanthrene treatments of wild-type and IL-1alpha-deficient mice; the former induced progressive tumors, whereas the latter cell lines induced regressing tumors or failed to develop into tumors in mice due to immune rejection. In regressing tumors, terminating alpha2-6-Neu5Ac residues were present at lower levels than in progressively growing tumors. In both tumor cells, the amount of alpha2-6-Neu5Ac residues was higher by an order of magnitude relative to the amount expressed in primary fibroblasts harvested from IL-1alpha-deficient and wild-type mice. We focused on membrane proteins, which may interact with the immune system. Interestingly, HSP65, grp75, and gp96 were found on the surfaces of malignant cells and were shown to possess sialylated N-glycans. The amount of trisialylated glycans on gp96 and HSP65 and monosialylated glycans on grp75 of regressing cells was significantly lower than in progressively growing cells, suggesting a dependency of these specific glycoforms on anti-tumor immunity.
Department of Biotechnology Engineering, Faculty of Engineering and the Israeli Center for Glycobiology, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel.
Avi
A
Avidan
Michal
M
Perlmutter
Smadar
S
Tal
Omer
O
Oraki
Tsachi
T
Kapp
Yacov
Y
Krelin
Moshe
M
Elkabets
Shahar
S
Dotan
Ron N
RN
Apte
Rachel G
RG
Lichtenstein
D000818:Animals; D002240:Carbohydrate Sequence; D002273:Carcinogens; D045744:Cell Line, Tumor; D002851:Chromatography, High Pressure Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D000939:Epitopes / Q000737:chemistry; D005354:Fibrosarcoma / Q000139:chemically induced / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D005434:Flow Cytometry; D015972:Gene Expression Regulation, Neoplastic; D006360:Heat-Shock Proteins / Q000378:metabolism*; D053582:Interleukin-1alpha / Q000172:deficiency* / Q000378:metabolism; D013058:Mass Spectrometry; D008565:Membrane Proteins / Q000378:metabolism*; D008748:Methylcholanthrene; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D011230:Precancerous Conditions / Q000378:metabolism*; D021381:Protein Transport; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D012799:Sialyltransferases / Q000235:genetics / Q000378:metabolism; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D002273:Carcinogens; D000939:Epitopes; D006360:Heat-Shock Proteins; D053582:Interleukin-1alpha; D008565:Membrane Proteins; D011134:Polysaccharides; D012333:RNA, Messenger; D008748:Methylcholanthrene; D012799:Sialyltransferases; D019158:N-Acetylneuraminic Acid; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase