Presence of Sialic Acid and Hexosamine in Proteins of the Aqueous Humour

Takki-Luukkainen, I.-T.; Miettinen, T. A.

doi:10.1111/j.1755-3768.1959.tb03415.x

Cited by 6 publications

(3 citation statements)

References 10 publications

(1 reference statement)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…HPTLC analyses were performed using the solvent system chloroform/methanol/0.2% CaCl 2 , 60:35:8 by vol. Bound sialic acid was determined by the resorcinol-HCl method (Svennerholm 1957;Takki-Luukkainen and Miettinen 1959), pure Neu5Ac being used as the reference standard.…”

Section: Methodsmentioning

confidence: 99%

GM1 promotes TrkA‐mediated neuroblastoma cell differentiation by occupying a plasma membrane domain different from TrkA

Chiricozzi

Biase

Maggioni

et al. 2019

Journal of Neurochemistry

View full text Add to dashboard Cite

Recently, we highlighted that the ganglioside GM1 promotes neuroblastoma cells differentiation by activating the TrkA receptor through the formation of a TrkA–GM1 oligosaccharide complex at the cell surface. To study the TrkA–GM1 interaction, we synthesized two radioactive GM1 derivatives presenting a photoactivable nitrophenylazide group at the end of lipid moiety, 1 or at position 6 of external galactose, 2; and a radioactive oligosaccharide portion of GM1 carrying the nitrophenylazide group at position 1 of glucose, 3. The three compounds were singly administered to cultured neuroblastoma Neuro2a cells under established conditions that allow cell surface interactions. After UV activation of photoactivable compounds, the proteins were analyzed by PAGE separation. The formation of cross‐linked TrkA–GM1 derivatives complexes was identified by both radioimaging and immunoblotting. Results indicated that the administration of compounds 2 and 3, carrying the photoactivable group on the oligosaccharide, led to the formation of a radioactive TrkA complex, while the administration of compound 1 did not. This underlines that the TrkA–GM1 interaction directly involves the GM1 oligosaccharide, but not the ceramide. To better understand how GM1 relates to the TrkA, we isolated plasma membrane lipid rafts. As expected, GM1 was found in the rigid detergent‐resistant fractions, while TrkA was found as a detergent soluble fraction component. These results suggest that TrkA and GM1 belong to separate membrane domains: probably TrkA interacts by ‘flopping’ down its extracellular portion onto the membrane, approaching its interplay site to the oligosaccharide portion of GM1.

show abstract

Section: Methodsmentioning

confidence: 99%

GM1 promotes TrkA‐mediated neuroblastoma cell differentiation by occupying a plasma membrane domain different from TrkA

Chiricozzi

Biase

Maggioni

et al. 2019

Journal of Neurochemistry

View full text Add to dashboard Cite

show abstract

“…HPTLC analyses were performed using the solvent system chloroform/methanol/0.2% CaCl 2 , 60 : 35 : 8 by vol. Bound sialic acid was determined by the resorcinol‐HCl method (Svennerholm ; Takki‐Luukkainen and Miettinen ), pure Neu5Ac being used as the reference standard.…”

Section: Methodsmentioning

confidence: 99%

Role of theGM1 ganglioside oligosaccharide portion in the TrkA‐dependent neurite sprouting in neuroblastoma cells

Chiricozzi

Pomè

Maggioni

et al. 2017

Journal of Neurochemistry

115

View full text Add to dashboard Cite

GM1 ganglioside (II NeuAc-Gg Cer) is known to promote neurite formation in neuroblastoma cells by activating TrkA-MAPK pathway. The molecular mechanism by which GM1 is involved in the neurodifferentiation process is still unknown, however, in vitro and in vivo evidences have suggested that the oligosaccharide portion of this ganglioside could be involved. Here, we report that, similarly to the entire GM1 molecule, its oligosaccharide II NeuAc-Gg rather than its ceramide (Cer) portion is responsible for the neurodifferentiation process by augmenting neurite elongation and increasing the neurofilament protein expression in murine neuroblastoma cells, Neuro2a. Conversely, asialo-GM1, GM2 and GM3 oligosaccharides are not effective in neurite elongation on Neuro2a cells, whereas the effect exerted by the Fuc-GM1 oligosaccharide (IV αFucII Neu5Ac-Gg ) is similar to that exerted by GM1 oligosaccharide. The neurotrophic properties of GM1 oligosaccharide are exerted by activating the TrkA receptor and the following phosphorylation cascade. By photolabeling experiments performed with a nitrophenylazide containing GM1 oligosaccharide, labeled with tritium, we showed a direct interaction between the GM1 oligosaccharide and the extracellular domain of TrkA receptor. Moreover, molecular docking analyses confirmed that GM1 oligosaccharide binds the TrkA-nerve growth factor complex leading to a binding free energy of approx. -11.5 kcal/mol, acting as a bridge able to increase and stabilize the TrkA-nerve growth factor molecular interactions.

show abstract

“…This has indeed turned out to be the case in various animal species as demonstrated by Balazs et al (1959), Takki-Luukkainen & Miettinen (1959), Balazs & Sundblad (1960) and Schmidt (1960).…”

mentioning

confidence: 84%

Sialic Acid in the Aqueous Humor and the Vitreous of Normal Human Eyes and of Eyes With Malignant Melanoma of the Choroid

Falbe-Hansen

Degn

1969

Acta Ophthalmologica

View full text Add to dashboard Cite

Presence of Sialic Acid and Hexosamine in Proteins of the Aqueous Humour

Cited by 6 publications

References 10 publications

GM1 promotes TrkA‐mediated neuroblastoma cell differentiation by occupying a plasma membrane domain different from TrkA

GM1 promotes TrkA‐mediated neuroblastoma cell differentiation by occupying a plasma membrane domain different from TrkA

Role of theGM1 ganglioside oligosaccharide portion in the TrkA‐dependent neurite sprouting in neuroblastoma cells

Sialic Acid in the Aqueous Humor and the Vitreous of Normal Human Eyes and of Eyes With Malignant Melanoma of the Choroid

Contact Info

Product

Resources

About