Identification of proteins bearing β1–6 branched N-glycans in human melanoma cell lines from different progression stages by tandem mass spectrometry analysis

Przybyło, Małgorzata; Martuszewska, Danuta; Pocheć, Ewa; Hoja-Łukowicz, Dorota; Lityń́ska, Anna

doi:10.1016/j.bbagen.2007.05.006

Cited by 56 publications

(65 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, only a few proteins have been identified to carry this type of glycans. Comparative analysis of primary and metastatic human melanoma cell lines showed that metastatic cells possessed greater number of protein reacting with PHA-L than the primary WM35 cells [32,45,46]. Among the identified proteins were mainly integrin subunits ( 2 , 3 , 5 , v , 1 ), N-cadherin and LAMP1 protein.…”

Section: Melanoma and Glycosylationmentioning

confidence: 98%

Protein Glycosylation as Marker of Melanoma Progression

Lityń́ska¹,

Przybyło²,

Hoja-Łukowicz³

et al. 2008

CCTR

View full text Add to dashboard Cite

A lot of experimental data has been produced which suggests that there is a crucial role for glycans during the different stages of melanoma progression. Malignant transformation is associated with various alterations in the glycosylation pattern of the protein glycans. The most common changes are associated with the presence of more branched and hypersialylated N-linked oligosaccharides, re-expression of fetal-type antigens and premature terminated glycans. Some of these changes may provide the tumor cells with an advantage in influencing their social behavior and facilitating metastasis formation so, glycan-target therapy in combination with existing protocols may have an important impact in the treatment of melanoma.

show abstract

Section: Melanoma and Glycosylationmentioning

confidence: 98%

Protein Glycosylation as Marker of Melanoma Progression

Lityń́ska¹,

Przybyło²,

Hoja-Łukowicz³

et al. 2008

CCTR

View full text Add to dashboard Cite

show abstract

“…[6][7][8][9][10][11][12] It transfers a GlcNAc residue to the 6-position of a Man residue, resulting in increased branching of the N-glycan (Figure 1). GnT-V requires a trisaccharide as an acceptor in the reaction with UDP-GlcNAc as a donor.…”

Section: Introductionmentioning

confidence: 99%

Conformational Flexibility and Dynamics of Two (1→6)‐Linked Disaccharides Related to an Oligosaccharide Epitope Expressed on Malignant Tumour Cells

Olsson

Säwén

Stenutz

et al. 2009

Chemistry A European J

View full text Add to dashboard Cite

The conformational flexibility and dynamics of two (1-->6)-linked disaccharides that are related to the action of the glycosyl transferase GnT-V have been investigated. NMR NOE and T-ROE spectroscopy experiments, conformation-dependent coupling constants and molecular dynamics (MD) simulations were used in the analyses. To facilitate these studies, the compounds were synthesised as alpha-d-[6-(13)C]-Manp-OMe derivatives, which reduced the (1)H NMR spectral overlap and facilitated the determination of two- and three-bond (1)H,(1)H, (1)H,(13)C and (13)C,(13)C-coupling constants. The population distribution for the glycosidic omega torsion angle in alpha-d-Manp-(1-->6)-alpha-d-Manp-OMe for gt/gg/tg was equal to 45:50:5, whereas in alpha-d-Manp-OMe it was determined to be 56:36:8. The dynamic model that was generated for beta-d-GlcpNAc-(1-->6)-alpha-d-Manp-OMe by MD simulations employing the PARM22/SU01 CHARMM-based force field was in very good agreement with experimental observations. beta-d-GlcpNAc-(1-->6)-alpha-d-Manp-OMe is described by an equilibrium of populated states in which the phi torsion angle has the exo-anomeric conformation, the psi torsion angle an extended antiperiplanar conformation and the omega torsion angle a distribution of populations predominantly between the gauche-trans and the gauche-gauche conformational states (i.e., gt/gg/tg) is equal to 60:35:5, respectively. The use of site-specific (13)C labelling in these disaccharides leads to increased spectral dispersion, thereby making NMR spectroscopy based conformational analysis possible that otherwise might be difficult to attain.

show abstract

“…Firstly, larger substitutions on these oligosaccharides may alter structural and functional characteristics of proteins that carry them [21]. The small subset of proteins that carry these oligosaccharides include, integrins, cadherins, CD-44 , EGF-R and Lysosome associated membrane proteins (LAMPs) [9,[21][22][23][24]. It is possible that some of these modifications aid organ specific metastasis.…”

Section: Introductionmentioning

confidence: 99%

Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen–Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3

et al. 2008

View full text Add to dashboard Cite

Galectin-3 on vascular endothelium has been shown to facilitate lung specific metastasis. Metastatic variants of B16 melanoma were chosen to identify specific ligands that mediate lung colonization via galectin-3. Flow cytometry showed that, galectin-3 binding to cells correlates with surface expression of poly N-acetyllactosamine (polylacNAc) but not with other reported ligands, e.g. Thomsen-Friedenreich (T/Tn) antigen. Immobilized galectin-3 promoted adhesion of melanoma cells in a metastasis dependent manner. Moreover, adhesion and galectin-3 binding to cells were specifically inhibited with lactose. These properties together with lung metastasis were inhibited with N-glycosylation inhibitor Swainsonine (SW), whereas, O-glycosylation inhibitor Benzyl-alpha-N-acetylgalactosamine (BG) had no effect. BG treatment significantly increased expression of T/Tn antigen on low metastatic cells; however, had no effect on their metastatic potential. The studies very comprehensively demonstrate the importance of polylacNAc substitutions on N-oligosaccharides in galectin-3 mediated lung metastasis.

show abstract

Identification of proteins bearing β1–6 branched N-glycans in human melanoma cell lines from different progression stages by tandem mass spectrometry analysis

Cited by 56 publications

References 46 publications

Protein Glycosylation as Marker of Melanoma Progression

Protein Glycosylation as Marker of Melanoma Progression

Conformational Flexibility and Dynamics of Two (1→6)‐Linked Disaccharides Related to an Oligosaccharide Epitope Expressed on Malignant Tumour Cells

Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen–Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3

Contact Info

Product

Resources

About