Blood Group Alterations in Cancer

Kuhns, William J.

doi:10.1007/978-1-4684-3575-7_5

Cited by 5 publications

(1 citation statement)

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“…Tumor-associated carbohydrate antigens found in tissues and body fluids are frequently related to various blood group systems including antigens of the ABH, Lewis, T and Tn blood group systems (19,27). Since many of these tumor-associated antigens are developmentally regulated antigens, also classified as "oncodevelopmental" antigens (9,20,32,41), a systematic knowledge of the expression of carbohydrate antigens during organogenesis is important.…”

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Blood group related carbohydrate antigens in human fetal pancreas

Philipsen

Clausen

Dabelsteen

et al. 1988

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Many tumor‐associated carbohydrate antigens are related to the blood group systems. Since several of these antigens are developmentally regulated, a systematic knowledge of the expression of blood group related carbohydrate antigens during organogenesis is important. By immunohistochemical methods we investigated the expression of carbohydrate structures related to the ABH, Lewis, T and Tn blood group systems in 28 fetal pancreas, from 13th‐40th gestational week using a comprehensive set of well‐defined monoclonal antibodies, reacting with type 1,2,3, and 4 chain carbohydrate structures. The following antigens were found in fetal pancreas: Type 1 chain: Lea, Leb, monosialylated Lea and disialylated Lea, type 2 chain: N‐acetyllactosamine (the immediate precursor to blood group H antigen), branched N‐acetyllactosamine, H‐antigen, Lex and Ley; type 3 chain: H‐antigen. The T‐antigen was well expressed, whereas this was not the case with the Tn‐antigen. As expected the A‐antigen was found in 10 of 24 cases. The A‐related antigens: ALeb, ALed and ALey were only found in a few of these ten specimens whereas type 3 chain A‐repetitive was found in all of them. Since msLea, Lex, Ley and T‐antigen have been described as tumor‐associated antigens, we conclude that several carbohydrate tumorrelated antigens are expressed in fetal pancreas.

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confidence: 99%

Blood group related carbohydrate antigens in human fetal pancreas

Philipsen

Clausen

Dabelsteen

et al. 1988

APMIS

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Synthesis of Sialyl T_N Glycopeptides – Enzymatic Sialylation by α2,6‐Sialyltransferase from Photobacterium damsela

et al. 2005

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The a2,6-sialyltransferase from Photobacterium damsela was applied for the enzymatic sialylation of the T N glycopeptide (APGSTA) with GalNAc a-linked to either the serine or threonine residue in the sequence. The enzyme preparation and reaction conditions were optimized prior to the application. In contrast to the mammalian sialyltransferases which recognize the moiety of GalNAca(1,1)Thr only, this bacterial enzyme can accept GalNAca(1,1)Thr as well as GalNAca(1,1)Ser. Our study also introduced a 4-dimethylaminoazobenzene-4'-sulfonyl (dabsyl) chromophore to the N-terminus of the peptide backbone, which is suitable for glycoconjugate substrates without affecting the binding affinity

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