Effect of alpha3beta1 and alphavbeta3 integrin glycosylation on interaction of melanoma cells with vitronectin.

Janik, Marcelina; Przybyło, Małgorzata; Pocheć, Ewa; Pokrywka, Małgorzata; Lityń́ska, Anna

doi:10.18388/abp.2010_2372

Cited by 21 publications

(13 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our group has investigated the glycosylation profiles of melanoma cells for over fifteen years. We have clearly demonstrated that the glycosylation profile of adhesion proteins (mainly integrins) depends on the stage of tumor development (Pocheć et al, 2003, Przybyło et al, 2007Pocheć et al, 2013) and the location of metastasis (Kremser et al, 2008;Janik et al, 2010). Here we searched for the reasons of a different behavior of UM and CM cells in the surface glycosylation.…”

Section: Introductionmentioning

confidence: 99%

Diverse expression of N-acetylglucosaminyltransferase V and complex-type β1,6-branched N-glycans in uveal and cutaneous melanoma cells

et al. 2015

Self Cite

View full text Add to dashboard Cite

Although both uveal (UM) and cutaneous (CM) melanoma cells derive from the transformed melanocytes, their biology varies significantly in several aspects. Malignant transformation is frequently associated with alternations in cell glycosylation, in particular those concerning branched complex-type N-glycans. These changes occur principally in β1,4-N-acetylglucosaminyltransferase III (GnT-III) that catalyzes the synthesis of glycans with bisected N-acetylglucosamine (GlcNAc) and β1,6-N-acetylglucosaminyltransferase V (GnT-V) that is involved in forming β1,6-branched antenna in complex-type glycans. We searched for the reasons of a different behavior of CM and UM cells in the expression of GnT-III and GnT-V and their oligosaccharide products. Our study showed that UM cells have more β1,6-branched glycans than CM cells, what results from a higher expression of MGAT5 gene encoding GnT-V. The higher β1,6-branching of glycans in UM may contribute to their higher potential to migrate on fibronectin and weaker binding to main extracellular matrix proteins, observed in our previous studies.

show abstract

Section: Introductionmentioning

confidence: 99%

Diverse expression of N-acetylglucosaminyltransferase V and complex-type β1,6-branched N-glycans in uveal and cutaneous melanoma cells

et al. 2015

Self Cite

View full text Add to dashboard Cite

show abstract

“…Our work demonstrated that β1,6-branched oligosaccharides on αvβ3 and α3β1 integrins are essential for the association of the uPAR with integrins in human melanoma cell lines WM9 and WM239, seen in the failure of co-precipitation of the two integrins with the uPAR in SW-treated cells. Adhesion of the two melanoma cells to VN was dependant on β1,6 branching of αvβ3 and α3β1 integrins in a cell-line-specific manner [76].…”

Section: Different Techniques Have Been Employed To Analyze α3β1mentioning

confidence: 92%

“…It has been demonstrated that the glycosylation profile of integrins depends on the stage of melanoma development [37,58,59,74] and the location of the metastasis [75,76] and that glycosylation is essential to the interaction between integrin and ECM proteins during adhesion and migration processes [58,75,76]. These studies have produced ample evidence for the presence of glycoforms associated with melanoma carcinogenesis on α3β1, α5β1, and αvβ3 integrins.…”

Section: Alterations Of Integrin Glycosylation In Melanoma Carcinogenmentioning

confidence: 99%

Glycosylation of Integrins in Melanoma Progression

Pocheć¹,

Lityń́ska²

2016

Human Skin Cancer, Potential Biomarkers and Therapeutic Targets

View full text Add to dashboard Cite

Each stage of melanoma development from transformed melanocytes to metastatic lesions requires the involvement of cell adhesion receptors, among which integrins are of particular importance. Strong N-glycosylation of αβ integrin heterodimers influences their processing, activation, and functions related to the modulation of cell adhesion to extracellular matrix proteins (ECM) and the basement membrane. A lack of N-glycans on integrin chains significantly reduces their interactions with the ECM. Melanoma progression is accompanied by changes in the composition of N-glycans on integrin subunits. The glycosylation profile of integrins depends on the stage of melanoma development and on the location of the metastasis. Enhanced expression of β1,6-branched complex-type oligosaccharides and altered sialylation are wellcharacterized changes in the N-glycosylation of integrins observed in melanoma progression. This chapter summarizes the current state of knowledge about α3β1, α5β1, and αvβ3 integrin glycosylation in melanoma and the functional consequences of changed glycosylation for the development of this cancer.

show abstract

“…We demonstrated that not only gain or loss of adhesion molecule expression and increased level of β1,6-branched N-oligosaccharides, but also changes in the number of proteins being a substrate for GnT-V appear to be a consequence of disease progression from a tumourigenic to the metastatic phenotype. The involvement of these glycoproteins in adhesion and migration of cutaneous melanoma cells has been clearly demonstrated [60,62,63,[66][67][68][69][70][71]. In general, overexpression of β1,6-branched N-glycans on cell adhesion molecules contributed to the significant decrease in these cell adhesion level to extracellular matrix components, loss of contact inhibition as well as increased motility in vitro and enhanced metastasis in vivo.…”

Section: Glycosylation and Melanomamentioning

confidence: 97%

Bitter Sweetness of Malignant Melanoma: Deciphering the Role of Cell Surface Glycosylation in Tumour Progression and Metastasis

Przybyło¹,

Janik²,

Hoja-Łukowicz³

2016

Human Skin Cancer, Potential Biomarkers and Therapeutic Targets

View full text Add to dashboard Cite

Malignant melanoma is the sixth most commonly diagnosed cancer in developed countries. Like in many cancers, survival rates are closely associated with the time of melanoma detection. Regrettably, most cases of melanoma are caught at diffuse state and methods used in clinical practice and experimental trials are not effective. Thus, there is a great interest in discovering biomarkers that could be used for screening those with melanoma, as prognostic and prediction factors as well as new potential targets for melanoma treatment. For this purpose, many groups have examined alteration in the structure and expression of carbohydrate part of glycoconjugates to identify changes that occur with melanoma. The observed changes include increased β1,6 branching correlating with higher abundance of polylactosamine extension, increased sialylation accompanied by differences in the position of sialic acid residues, increased fucosylation, higher levels of T and Tn antigens as well as changes in the expression of ganglioside structures. As a consequence of glycan modification, the loosened matrix adhesion, increased motility, higher invasive potential and metastasis formation have been observed. Growth and migration of melanoma cells have been also found to be stimulated by advanced glycation end products. Biomarker discovery is a multi-step process and the recent glycomic data on melanoma are mostly related to the discovery phase, as the first one leading to validation and standardisation steps.

show abstract

Effect of alpha3beta1 and alphavbeta3 integrin glycosylation on interaction of melanoma cells with vitronectin.

Cited by 21 publications

References 56 publications

Diverse expression of N-acetylglucosaminyltransferase V and complex-type β1,6-branched N-glycans in uveal and cutaneous melanoma cells

Diverse expression of N-acetylglucosaminyltransferase V and complex-type β1,6-branched N-glycans in uveal and cutaneous melanoma cells

Glycosylation of Integrins in Melanoma Progression

Bitter Sweetness of Malignant Melanoma: Deciphering the Role of Cell Surface Glycosylation in Tumour Progression and Metastasis

Contact Info

Product

Resources

About