Determination of carbohydrate-binding preferences of human galectins with carbohydrate microarrays.
Galectins are a class of carbohydrate-binding proteins named for their galactose-binding preference and are involved in a host of processes ranging from homeostasis of organisms to immune responses. As a first step towards correlating the carbohydrate-binding preferences of the different galectins with their biological functions, we determined carbohydrate recognition fine-specificities of galectins with the aid of carbohydrate microarrays. A focused set of oligosaccharides considered relevant to galectins was prepared by chemical synthesis. Structure-activity relationships for galectin-sugar interactions were determined, and these helped in the establishment of redundant and specific galectin actions by comparison of binding preferences. Distinct glycosylations on the basic lactosyl motifs proved to be key to galectin binding regulation--and therefore galectin action--as either high-affinity ligands are produced or binding is blocked. High-affinity ligands such as the blood group antigens that presumably mediate particular functions were identified.
Horlacher
Tim
T
Federal Institute of Technology (ETH) Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland.
Oberli
Matthias A
MA
Werz
Daniel B
DB
Kröck
Lenz
L
Bufali
Simone
S
Mishra
Rashmi
R
Sobek
Jens
J
Simons
Kai
K
Hirashima
Mitsuomi
M
Niki
Toshiro
T
Seeberger
Peter H
PH
D001789:Blood Group Antigens / Q000378:metabolism; D002241:Carbohydrates / Q000737:chemistry*; D037161:Galectins / Q000378:metabolism*; D006801:Humans; D046228:Microarray Analysis; D009844:Oligosaccharides / Q000138:chemical synthesis / Q000378:metabolism*; D011485:Protein Binding; D013329:Structure-Activity Relationship
D001789:Blood Group Antigens; D002241:Carbohydrates; D037161:Galectins; D009844:Oligosaccharides