Peanut (Arachis hypogaea) lectin recognizes α-linked galactose, but not N-acetyl lactosamine in N-linked oligosaccharide terminals

被引:40
作者
Chacko, BK [1 ]
Appukuttan, PS [1 ]
机构
[1] Sree Chitra Tirunal Inst Med Sci & Technol, Div Biochem, Trivandrum 695011, Kerala, India
关键词
peanut (Arachis hypogaea) lectin; alpha-linked galactose; N-acetyl lactosamine;
D O I
10.1016/S0141-8130(01)00139-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Peanut (Arachis hypogaea) agglutinin (PNA) is extensively used as tumour marker as it strongly recognises the cancer specific T antigen (Ga1 beta --> 3GalNAc-), but not its sialylated version. However, an additional specificity towards Gal beta1 --> 4GlcNAc (LacNAc), which is not tumour specific, had been attributed to PNA. For correct interpretation of lectin histochemical results we examined PNA sugar specificity using naturally occurring or semi-synthetic glycoproteins, matrix-immobilised galactosides and lectin-binding tissue glycoproteins, rather than mono- or disaccharides as ligands. Dot-blots, transfer blots or polystyrene plate coatings of the soluble glycoconjugates were probed with horse-radish peroxidase (HRP) conjugates of PNA and other lectins of known specificity. Modifications of PNA-binding glycoproteins, including selective removal of O-linked oligosaccharides and treatment with glycosidases revealed that Gal beta1 --> 4GlcNAc (LacNAc) was ineffective while terminal alpha -linked galactose (TAG) as well as exposed T antigen (Gal beta1 --> 3 GalNAc-) was excellent as sugar moiety in glycoproteins for their recognition by PNA. When immobilised, melibiose was superior to lactose in PNA binding. Results were confirmed using TAG-specific human serum anti-a-galactoside antibody. (C) 2001 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:365 / 371
页数:7
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