GM1 structural requirements to mediate neuronal functions

被引:2
|
作者
Fazzari, Maria [1 ]
Lunghi, Giulia [1 ]
Di Biase, Erika [1 ]
Maggioni, Margherita [1 ]
Carsana, Emma Veronica [1 ]
Cioccarelli, Laura [1 ]
Vigani, Laura [1 ]
Loberto, Nicoletta [1 ]
Aureli, Massimo [1 ]
Mauri, Laura [1 ]
Ciampa, Maria Grazia [1 ]
Valsecchi, Manuela [1 ]
Takato, Koichi [2 ]
Imamura, Akihiro [3 ,4 ]
Ishida, Hideharu [3 ,4 ]
Ben Mariem, Omar [5 ]
Saporiti, Simona [6 ]
Palazzolo, Luca [5 ]
Chiricozzi, Elena [1 ]
Eberini, Ivano [5 ,7 ]
Sonnino, Sandro [1 ]
机构
[1] Univ Milan, Dept Med Biotechnol & Translat Med, Milan, Italy
[2] Gifu Univ, Fac Appl Biol Sci, 1-1 Yanagido, Gifu 5011193, Japan
[3] Gifu Univ, Dept Appl Bioorgan Chem, 1-1 Yanagido, Gifu 5011193, Japan
[4] Gifu Univ, Inst Glyco Core Res iGCORE, 1-1 Yanagido, Gifu 5011193, Japan
[5] Univ Milan, Dipartimento Sci Farmacol & Biomol Rodolfo Paolett, Milan, Italy
[6] Merck Serono SpA, Analyt Excellence & Program Management, Rome, Italy
[7] Univ Milan, Data Sci Res Ctr, Milan, Italy
关键词
GM1; ganglioside; oligosaccharide; Plasma membrane signaling; TrkA receptor; Neurodifferentiation; Molecular docking; NERVE GROWTH-FACTOR; CEREBELLAR GRANULE CELLS; GANGLIOSIDE GM1; PLASMA-MEMBRANE; OLIGOSACCHARIDE PORTION; EXOGENOUS GANGLIOSIDES; NEUROBLASTOMA-CELLS; MICELLAR PROPERTIES; NEURITE OUTGROWTH; G(M1) GANGLIOSIDE;
D O I
10.1007/s10719-023-10141-8
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
Since the 1980s, it has been known that the administration of ganglioside GM1 to cultured cells induced or enhanced neuronal differentiation. GM1 mechanism of action relies on its direct interaction and subsequent activation of the membrane tyrosine kinase receptor, TrkA, which naturally serves as NGF receptor. This process is mediated by the sole oligosaccharide portion of GM1, the pentasaccharide beta-Gal-(1-3)-beta-GalNAc-(1-4)-[alpha-Neu5Ac-(2-3)]-beta-Gal-(1-4)-beta-Glc. Here we detailed the minimum structural requirements of the oligosaccharide portion of GM1 for mediating the TrkA dependent neuritogenic processing. By in vitro and in silico biochemical approaches, we demonstrated that the minimal portion of GM1 required for the TrkA activation is the inner core of the ganglioside's oligosaccharide beta-Gal-(1-3)-beta-GalNAc-(1-4)-[alpha-Neu5Ac-(2-3)]-beta-Gal. The addition of a sialic acid residue at position 3 of the outer galactose of the GM1 oligosaccharide, which forms the oligosaccharide of GD1a, prevented the interaction with TrkA and the resulting neuritogenesis. On the contrary, the addition of a fucose residue at position 2 of the outer galactose, forming the Fucosyl-GM1 oligosaccharide, did not prevent the TrkA-mediated neuritogenesis.
引用
收藏
页码:655 / 668
页数:14
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