Expression of Caveolin-1 in Human Cutaneous and Uveal Melanoma Cells

Belkot, Klaudyna; Bubka, Monika; Lityń́ska, Anna

doi:10.3409/fb64_3.145

Cited by 5 publications

(3 citation statements)

References 23 publications

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“…Interestingly, it was proved, that caveolin-1 by forming complexes with GnT-III can act as a regulator of its distribution within the Golgi [ 48 ]. The expression of caveolin-1 in melanoma cells has been studied by Bełkot et al, and their work showed that in case of WM266–4 melanoma cells its expression is relatively low and the distribution within the cells do not show localization of the protein in ER and Golgi apparatus [ 49 ]. It is possible, that in WM266–4-GnT-III melanoma cells studied here, the level of caveolin-1 is thus too low to localize GnT-III in the early compartments of the secretory pathway.…”

Section: Discussionmentioning

confidence: 99%

The glycomic effect of N-acetylglucosaminyltransferase III overexpression in metastatic melanoma cells. GnT-III modifies highly branched N-glycans

et al. 2018

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N-acetylglucosaminyltransferase III (GnT-III) is known to catalyze N-glycan “bisection” and thereby modulate the formation of highly branched complex structures within the Golgi apparatus. While active, it inhibits the action of other GlcNAc transferases such as GnT-IV and GnT-V. Moreover, GnT-III is considered as an inhibitor of the metastatic potential of cancer cells both in vitro and in vivo. However, the effects of GnT-III may be more diverse and depend on the cellular context. We describe the detailed glycomic analysis of the effect of GnT-III overexpression in WM266–4-GnT-III metastatic melanoma cells. We used MALDI-TOF and ESI-ion-trap-MS/MS together with HILIC-HPLC of 2-AA labeled N-glycans to study the N-glycome of membrane-attached and secreted proteins. We found that the overexpression of GnT-III in melanoma leads to the modification of a broad range of N-glycan types by the introduction of the “bisecting” GlcNAc residue with highly branched complex structures among them. The presence of these unusual complex N-glycans resulted in stronger interactions of cellular glycoproteins with the PHA-L. Based on the data presented here we conclude that elevated activity of GnT-III in cancer cells does not necessarily lead to a total abrogation of the formation of highly branched glycans. In addition, the modification of pre-existing N-glycans by the introduction of “bisecting” GlcNAc can modulate their capacity to interact with carbohydrate-binding proteins such as plant lectins. Our results suggest further studies on the biological function of “bisected” oligosaccharides in cancer cell biology and their interactions with carbohydrate-binding proteins.Electronic supplementary materialThe online version of this article (10.1007/s10719-018-9814-y) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

The glycomic effect of N-acetylglucosaminyltransferase III overexpression in metastatic melanoma cells. GnT-III modifies highly branched N-glycans

et al. 2018

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“…The hypothesis that PRL3 exerts a different role depending on the existence of caveolar structures is further strengthened by the observation that in primary uveal melanoma cells PRL3 affects integrin clustering predominantly at the focal adhesion sites of the membrane [ 44 ]. Uveal melanoma cells, however, express a considerably lower, or no amounts of Caveolin 1 compared to melanoma cells of cutaneous origins [ 45 ], such as B16F0 cells.…”

Section: Discussionmentioning

confidence: 99%

Chemotherapy induced PRL3 expression promotes cancer growth via plasma membrane remodeling and specific alterations of caveolae-associated signaling

et al. 2018

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BackgroundThe outcome of cancer therapy is greatly defined by the ability of a tumor cell to evade treatment and re-establish its bulk mass after medical interventions. Consequently, there is an urgent need for the characterization of molecules affecting tumor reoccurrence. The phosphatase of regenerating liver 3 (PRL3) protein was recently emerged among the targets that could affect such a phenomenon.MethodsThe expression induction of PRL3 in melanoma cells treated with chemotherapeutic agents was assessed by western blotting. The effect of PRL3 expression on cancer growth was investigated both in vitro and in vivo. The association of PRL3 with the caveolae structures of the plasma membrane was analyzed by detergent free raft purification. The effect of PRL3 expression on the membrane organization was assayed by electron microscopy and by membrane biophysical measurements. Purification of the plasma membrane fraction and co-immunoprecipitation were used to evaluate the altered protein composition of the plasma membrane upon PRL3 expression.ResultsHere, we identified PRL3 as a genotoxic stress-induced oncogene whose expression is significantly increased by the presence of classical antitumor therapeutics. Furthermore, we successfully connected the presence of this oncogene with increased tumor growth, which implies that tumor cells can utilize PRL3 effects as a survival strategy. We further demonstrated the molecular mechanism that is connected with the pro-growth action of PRL3, which is closely associated with its localization to the caveolae-type lipid raft compartment of the plasma membrane. In our study, PRL3 was associated with distinct changes in the plasma membrane structure and in the caveolar proteome, such as the dephosphorylation of integrin β1 at Thr788/Thr789 and the increased partitioning of Rac1 to the plasma membrane. These alterations at the plasma membrane were further associated with the elevation of cyclin D1 in the nucleus.ConclusionsThis study identifies PRL3 as an oncogene upregulated in cancer cells upon exposure to anticancer therapeutics. Furthermore, this work contributes to the existing knowledge on PRL3 function by characterizing its association with the caveolae-like domains of the plasma membrane and their resident proteins.Electronic supplementary materialThe online version of this article (10.1186/s12964-018-0264-8) contains supplementary material, which is available to authorized users.

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“…The hypothesis that PRL3 exerts a different role depending on the existence of caveolar structures is further strengthened by the observation that in primary uveal melanoma cells PRL3 affects integrin clustering predominantly at the focal adhesion sites of the membrane 151 . Uveal melanoma cells, however, express a considerably lower, or no amounts of Caveolin 1 compared to melanoma cells of cutaneous origins 248 , such as B16F0 cells.…”

Section: 2mentioning

confidence: 87%

Regulatory role of plasma membrane microdomains in cellular stress sensing and growth signaling

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Expression of Caveolin-1 in Human Cutaneous and Uveal Melanoma Cells

Cited by 5 publications

References 23 publications

The glycomic effect of N-acetylglucosaminyltransferase III overexpression in metastatic melanoma cells. GnT-III modifies highly branched N-glycans

The glycomic effect of N-acetylglucosaminyltransferase III overexpression in metastatic melanoma cells. GnT-III modifies highly branched N-glycans

Chemotherapy induced PRL3 expression promotes cancer growth via plasma membrane remodeling and specific alterations of caveolae-associated signaling

Regulatory role of plasma membrane microdomains in cellular stress sensing and growth signaling

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