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|Vicia faba : Fava bean, broad bean|
Molecular structure of
Fava bean, broad bean:VFA, Favin
|Lecster ID:644|| Edit Entry |
|Source Organism:||Fava bean, broad bean|
| Common Nomenclature:||VFA, Favin|
|Characterization Notes:||The lectin behaves as a 'cold agglutinin' displaying stronger agglutination than the naturally occurring ABO agglutinin in the cold. For discussion of characteristics of Favin, see: J Biol Chem 1979 Jul 25;254(14):6803-10|
|Biological Activity:||Agglutinates human group A erythrocytes at a titer of 1:4; group B erythrocytes at a titer of 1:1; by crude lectin preparation (16mg/ml). See: Int J Cancer 1970;6:283|
Dietary lectins can alter the proliferation of colonic cells.
A normal healthy cell is said to be well differentiated, meaning that its characteristic features and structures are intact. Differentiation is regulated by adhesion molecules which, being glycosylated, are targets for lectin binding.
Researchers from Hammersmith Hospital, London, assessed the effects of dietary lectins on the behavior of cancer cells in the colon.
VFA (broad bean lectin) stimulated an undifferentiated colon cancer cell line to differentiate into gland like structures. The adhesion molecule epCAM is involved in this. See: Gut 1999 May;44(5):709-14
|Specificity:|| The purified lectin shows a high affinity for N-acetyl-D-glucosamine (GlcNAc); D-mannose|
|References:||Prep Biochem 1984;14(4):373-87|
2014-11-28: Current Date 22:10:2 GMT: Current Time
By Peter D'Adamo. Copyright 2001-2011.