this page: Lectins
Product Lineup
Lectins
Glyscope/glycan analysis
Other related information
Lectins and Sugar chains
About Lectins
What are lectins?
Hemagglutination activity assay
How to use biotin-labeled lectin
Use as a mitogen
Lectin Agarose
Lectin solubility
About sugar chains
Functions of glycans
Glycans and disease
MGC Products
Other Related Information: Lectins and Sugar chains
Lectin is defined by Goldstein 1) et al. As follows.
- A glyco-binding protein or glycoprotein other than the product of an immune response that aggregates cells or complex carbohydrates.
- It has two or more binding sites and can aggregate animal and plant cells.
- Aggregation is specifically blocked by monosaccharides or oligosaccharides. Generally, lectin is used as a general term for substances having specific binding activity to sugar among proteins or glycoproteins existing in plants, animals, microorganisms, etc.
References
1) Goldstein, IJ, Hughes, RC, Monsigny, M., Osawa, T., and Sharon, N., Nature.285,66 (1980)
Definition of lectins
In 1957, O. Mäkelä classified them into 4 groups according to the coordination of the hydroxyl groups at the C-3 and C-4 positions of the sugar (Table 1). Lectins classified in the 4th county have not been found yet. Recently, the primary structure of lectins has been analyzed, and classification based on that structure (classification by family) has also been performed (Table 2).
Table 1 Classification of lectins based on monosaccharide recognition in Mäkelä
Classification of Mäkelä | origin | Lectin trivial name | Sugar binding specificity | My Togen activity |
Fuc |
Gorse | UEA-I | α-L-Fuc | - |
Gal GalNAc |
Soybean Peanuts Ricinus castor (Ricinus communis) Dorikosumame Mushroom Green beans |
SBA PNA RCA120 DBA ABA PHA-E PHA-L |
α-GalNAc> β-GalNAc β-Gal β-Gal α-GalNAc Gal β1-3GalNAc GalNAc GalNAc |
+ ± - - + |
D-Man D-Glc D-GlcNAc |
Sword bean pea lentil lentil broad bean Pokeweed potato wheat germ gorse |
Con A PSA LCA VFA PWM STA WGA UEA-II |
α-Man > α-Glc α-Man > α-Glc α-Man > α-Glc α-Man > α-Glc GlcNAcβ1-4GlcNAc GlcNAcβ1-4GlcNAc GlcNAcβ1-4GlcNAc GlcNAcβ1-4GlcNAc |
+ + + + + ± - |
L-Glc L-Man |
- | - | - | - |
Table 2 Classification of lectins by family
Family (biological distribution) | Sugar specificity | Main lectins |
Leguminosae Lectin L-type lectin (plant) |
Man Gal Sia Fuc | DSA PHA SBA UEA-I MAM DBA ConA ECA PSA |
Monocot lectin M-type lectin (plant) |
Mab | GNA HHA ASA |
R-type lectin (animals and plants) |
Man Gal Sia Xyl | RCA 120 SSA SNA |
Application of lectins
The table below shows the involvement of diseases and sugar chains. Recently, many glycoproteins and glycolipids that can be used as tumor markers have been found. These are those produced directly by the cancer cells themselves or those produced by surrounding cells due to the influence of the cancer cells, and their quantitative or qualitative fluctuations are applied to diagnosis. For example, α-fetoprotein (AFP) increases significantly with liver cancer, so quantitative changes have been used for diagnosis for some time, but recently, by investigating qualitative changes, "changes in sugar chains". , It is possible to detect canceration at an early stage. In various diseases such as cancer, the discovery of new markers and the development of diagnostic methods using them are eagerly desired and are being actively researched.
Diseases involving sugar chains | Markers and targets | Change | Application |
Liver disease, liver cancer | α-fetoprotein N-type sugar chain 1) | Increased fucosylated sugar chain Increased | Diagnosis by LCA 3) 4) 5) |
LCA binding rate 2) | |||
Transferrin N-type sugar chain | Increase in Lex antigen sugar chain 6) | ||
Increase in AAL binding rate 7) | |||
γGTP N-type sugar chain | Increased branching 8) | Early diagnosis of cancer | |
Increased lactosamine structure | |||
Cholinesterase N-type sugar chain | Fucose α1-3 increase 9) 10) | Diagnosis by AAL | |
Alcoholic liver disease | Transferrin N-type sugar chain | Decrease / disappear 11) 12) | |
Villous cancer | hCG N-type sugar chain | Changes in branching 13) 14) | Differentiation between good and malignant |
Rectal cancer | CEA N-type sugar chain 15) 16) | Type I decreased, type II increased, | Prognosis diagnosis |
high mannose type increased | |||
Lung cancer | Lactic sugar chain antigen | Increased sialyl Lea and Lex 17) | |
ganglioside | GM2 expression 18) | ||
Stomach cancer, large intestine cancer | Glycolipids 19) | ||
Pancreatic cancer | CA19-9 etc. | Increase in sialyl Lea 20) | |
Haptoglobin 21) | Increased fucosylated sugar chains | ||
Kidney cancer, bladder cancer | Glycolipids | Increase in CDH 22) | |
Endometrial cancer | Blood group substance | Expression of H-type sugar chains | Snooping on UEA, PNA23 ) |
Prostate cancer | PSA | ||
Ovarian cancer | CA125 | Diagnosis by WGA 24) | |
Thyroid cancer | Thyroglobulin | Diagnosis by Con A 25) | |
Myeloma | IgG N type sugar chain | Decrease in galactose | |
Osteosarcoma, osteoporosis | Bone Alkaline Phosphatase Sugar Chain 26) 27) | ||
Rheumatoid arthritis | IgG N-type sugar chain 28) 29) | Decrease in galactose 31) | Diagnosis 32) 33) 34) 35) |
α1-acid glycoprotein N-type sugar chain 30) | |||
Pancreatitis | In serum | 2-6 Increase in sialyl Lea 36) | |
Gastritis, enteritis | Glycolipids of mucosal epithelium | ||
leukemia | Ganglioside | Treatment research 37) 38) | |
Neurotic harm | Ganglioside | Therapeutic application | |
Cataract | Glycolipids | Increase in Lex 39) | |
Alzheimer | Glycolipid 40) | Increase / decrease in the amount of glycolipids |
Literature
- Ohno, M., Nishikawa, A., Taniguchi, N., et al., Int. J. Cancer, 51, 315 (1992)
- Yamashita, K., Taketa, K., et al., Cancer Res., 53, 1 (1993)
- Taketa, K., Clinical Laboratory, 39, 1259 (1995)
- Nikkei Sangyo Shimbun, 1997.6.10., P19
- Kuwabara, M., Ariyoshi, Y., Inspection and Technology, 27, 443 (1999)
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