1988 Fiscal Year Final Research Report Summary
Studies on carbohydrate structures of plasma membrane blycoproteins in relation to the loss of cell adhesion.
| Project/Area Number |
62580108
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | University of Tokyo |
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Principal Investigator |
FURUKAWA Kiyoshi Research Associate, Department of Biochemistry, Institute of Medical Science, University of Tokyo., 医科学研究所, 助手 (10190133)
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| Co-Investigator(Kenkyū-buntansha) |
AMANO Junko Research Assistance, Department of Biochem., Inst. of Medical Science, Universit, 医科学研究所, 教務職員 (10159460)
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| Project Period (FY) |
1987 – 1988
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| Keywords | Cell adhesion / Glycoproteins / Hybrid-type sugar chains |
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| Research Abstract |
The carbohydrate structures of plasma membrane glycoproteins prepared from tissue forming cells and from non-tissue forming cells have been determined. The results showed that various tissues of rat contain mainly biantennary complex-type and high-mannose type sugar chains with different amounts of tri- and tetraantennary complex-type ones, of sialic acid, of fucose, of -galactose, of bisecting N-acetylglucosamine and of lactosaminoglycan in a tissue specific manner. When two rat ascites hepatoma cells were analyzed in comparison to normal livers, they were primarily tri- and tetraantennary complex-type sugar chains and those with a repeating structure which are different from that of livers. However, one ascites hepatoma cells, AH414, which lose cell adhesion and are present as single cells, expressed fucosyl hybrid-type sugar chains in much larger amount than livers and the other ascites hepatoma cells, AH7974, which maintain partial intercellular adhesion.
When mucin-type glycoprotei
… More
ns associated with plasma membranes of liver and two ascites hepatoma of rat were analyzed by using a low density WGA-Sepharose column to which sialyl mucin-type glycoproteins preferentially bind, AH414 cells showed the presence of highly sialylated glycoprotein(s) with clusted mucin-type sugar chains, which were detected but in much lesser amount in liver and AH7974 cells. The carbohydrate structures of them were turned out to be GalNAc, Gal 1-GalNAc and Gal 1-(GlcNAc 1-)GalNAc.
The above results indicated that the appearance of hybrid-type sugar chains as well as highly sialylated mucin-type sugar chains in plasma membrane glycoproteins may be related to the loss of cell adhesion of originally tissue forming cells. The activities of galactosyltransferases that are involved in the synthesis of Asn-linked and mucin-type sugar chains in the transformed cells were high, which probably may reflect the increased synthesis of branched Asn-linked sugar chains and of highly sialylated clustered mucin-type glycoproteins. Less
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Research Products
(2 results)
