TY - JOUR
T1 - Recognition roles of the carbohydrate glycotopes of human and bovine lactoferrins in lectin-N-glycan interactions
AU - Yen, Meng Hsiu
AU - Wu, Albert M.
AU - Yang, Zhangung
AU - Gong, Yu Ping
AU - Chang, En Tzu
PY - 2011/2
Y1 - 2011/2
N2 - Background: Lactoferrin is an iron-binding protein belonging to the transferrin family. In addition to iron homeostasis, lactoferrin is also thought to have anti-microbial, anti-inflammatory, and anticancer activities. Previous studies showed that all lactoferrins are glycosylated in the human body, but the recognition roles of their carbohydrate glycotopes have not been well addressed. Methods: The roles of human and bovine lactoferrins involved in lectin-N-glycan recognition processes were analyzed by enzyme-linked lectinosorbent assay with a panel of applied and microbial lectins. Results and conclusions: Both native and asialo human/bovine lactoferrins reacted strongly with four Man-specific lectins - Concanavalia ensiformis agglutinin, Morniga M, Pisum sativum agglutinin, and Lens culinaris lectin. They also reacted well with PA-IIL, a LFuc>Man-specific lectin isolated from Pseudomonas aeruginosa. Both human and bovine lactoferrins also recognized a sialic acid specific lectin-Sambucus nigra agglutinin, but not their asialo products. Both native and asialo bovine lactoferrins, but not the human ones, exhibited strong binding with a GalNAc>Gal-specific lectin-Wisteria floribunda agglutinin. Human native lactoferrins and its asialo products bound well with four Gal>GalNAc-specific type-2 ribosome inactivating protein family lectins-ricin, abrin-a, Ricinus communis agglutinin 1, and Abrus precatorius agglutinin (APA), while the bovine ones reacted only with APA. General significance: This study provides essential knowledge regarding the different roles of bioactive sites of lactoferrins in lectin-N-glycan recognition processes.
AB - Background: Lactoferrin is an iron-binding protein belonging to the transferrin family. In addition to iron homeostasis, lactoferrin is also thought to have anti-microbial, anti-inflammatory, and anticancer activities. Previous studies showed that all lactoferrins are glycosylated in the human body, but the recognition roles of their carbohydrate glycotopes have not been well addressed. Methods: The roles of human and bovine lactoferrins involved in lectin-N-glycan recognition processes were analyzed by enzyme-linked lectinosorbent assay with a panel of applied and microbial lectins. Results and conclusions: Both native and asialo human/bovine lactoferrins reacted strongly with four Man-specific lectins - Concanavalia ensiformis agglutinin, Morniga M, Pisum sativum agglutinin, and Lens culinaris lectin. They also reacted well with PA-IIL, a LFuc>Man-specific lectin isolated from Pseudomonas aeruginosa. Both human and bovine lactoferrins also recognized a sialic acid specific lectin-Sambucus nigra agglutinin, but not their asialo products. Both native and asialo bovine lactoferrins, but not the human ones, exhibited strong binding with a GalNAc>Gal-specific lectin-Wisteria floribunda agglutinin. Human native lactoferrins and its asialo products bound well with four Gal>GalNAc-specific type-2 ribosome inactivating protein family lectins-ricin, abrin-a, Ricinus communis agglutinin 1, and Abrus precatorius agglutinin (APA), while the bovine ones reacted only with APA. General significance: This study provides essential knowledge regarding the different roles of bioactive sites of lactoferrins in lectin-N-glycan recognition processes.
KW - Carbohydrate glycotope
KW - Iron-binding glycoprotein
KW - Lactoferrin
KW - Lectin binding
KW - N-glycans
UR - http://www.scopus.com/inward/record.url?scp=78649522403&partnerID=8YFLogxK
U2 - 10.1016/j.bbagen.2010.10.007
DO - 10.1016/j.bbagen.2010.10.007
M3 - 文章
C2 - 21055448
AN - SCOPUS:78649522403
SN - 0304-4165
VL - 1810
SP - 139
EP - 149
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 2
ER -