Wyniki wyszukiwania

1

Glikoproteiny układu odpornościowego: struktura i funkcja części cukrowej wybranych receptorów błonowych limfocytów T. Cz. I

100%

Polak K., Pochec E.

Postępy Biologii Komórki

|

2017

|

tom 44

|

nr 2

2

Glikoproteiny układu odpornościowego: rola glikanów antygenów zgodności tkankowej (MHC) oraz znaczenie galektyn w aktywacji i apoptozie limfocytów T. Cz. II

100%

Polak K., Pochec E.

Postępy Biologii Komórki

|

2017

|

tom 44

|

nr 3

3

HMGB1 inhibition during zymosan-induced inflammation: the potential therapeutic action of riboflavin

100%

Mazur-Bialy A. I., Pochec E.

Archivum Immunologiae et Therapiae Experimentalis

|

2016

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tom 64

|

nr 2

4

Rola glikozylacji w aktywacji receptora nabłonkowego czynnika wzrostu

81%

Zabczynska M., Opiola K., Pochec E.

Postępy Biologii Komórki

|

2016

|

tom 43

|

nr 2

5

Diverse expression of N-acetylglucosaminyltransferase V and complex-type Beta1,6-branched N-glycans in uveal and cutaneous melanoma cells

81%

Pochec E., Rydlewska M., Przybylo M., Litynska A.

Acta Biochimica Polonica

|

2015

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tom 62

|

nr 2

6

Integrin alpha3 beta1 from human melanoma; characterisation of its N-linked oligosaccharides

81%

Kremser E., Litynska A., Pochec E.

Acta Biochimica Polonica

|

2003

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tom 50

|

nr Supplement 1

7

New insight into the direct anti-inflammatory activity of a myokine irisin against proinflammatory activation of adipocytes. Implication for exercise in obesity

81%

Mazur-Bialy A. I., Bilski J., Pochec E., Brzozowski T.

Journal of Physiology and Pharmacology

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2017

|

tom 68

|

nr 2

8

N-glycoproteins bearing beta1-6 branching oligosaccharides from A375 human melanoma cell line analysed by HPLC/MS

81%

Ochwat D., Hoja-Lukowicz D., Pochec E., Litynska A.

Acta Biochimica Polonica

|

2003

|

tom 50

|

nr Supplement 1

9

Immunomodulatory effect of riboflavin deficiency and enrichment - reversible pathological response versus silencing of inflammatory activation

81%

Mazur-Bialy A. I., Pochec E., Plytycz B.

Journal of Physiology and Pharmacology

|

2015

|

tom 66

|

nr 6

10

Adhesion properties of human bladder cell lines with extracellular matrix components: the role of integrins and glycosylation

80%

Litynska A., Przybylo M., Pochec E., Laidler P.

Acta Biochimica Polonica

|

2002

|

tom 49

|

nr 3

Integrin subunits present on human bladder cells displayed heterogeneous functional specificity in adhesion to extracellular matrix proteins (ECM). The non-malignant cell line (HCV29) showed significantly higher adhesion efficiency to collagen IV, laminin (LN) and fibronectin (FN) than cancer (T24, Hu456) and v-raf transfected (BC3726) cell lines. Specific antibodies to the a2, a5 and β1 integrin sub- units inhibited adhesion of the non-malignant cells, indicating these integrin participation in the adhesion to ECM proteins. In contrast, adhesion of cancer cells was not inhibited by specific antibodies to the β1 integrin subunit. Antibodies to a3 integrin increased adhesion of cancer cells to collagen, LN and FN, but also of the HCV29 line with colagen. It seems that a3 subunit plays a major role in modulation of other integrin receptors especially in cancer cells. Differences in adhesion to ECM proteins between the non-malignant and cancer cell lines in response to Gal and Fuc were not evident, except for the v-raf transfected cell line which showed a distinct about 6-fold increased adhesion to LN on addition of both saccharides. .-Acetylneuraminic acid inhibited adhesion of all cell lines to LN and FN irrespective of their malignancy.

11

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

71%

Janik M. E., Przybylo M., Pochec E., Pokrywka M., Litynska A.

Acta Biochimica Polonica

|

2010

|

tom 57

|

nr 1

55-61

The metastatic transformation of melanocytes is associated with altered expression of adhesion molecules, including αvβ3 and α3β1 integrins. Integrin αvβ3 is a primary vitronectin (VN) receptor, while both integrin types take part in adhesion to VN when they are in complex with uPAR. Although their role in melanoma cell interaction with VN is of great interest, the influence of N-oligosaccharides attached to these glycoproteins is still unappreciated. The present study assesses the role of αvβ3 and α3β1 integrins and the influence of their glycosylation status on WM9 and WM239 metastatic melanoma cell interactions with VN. Cell adhesion to and migration on VN were selected as the studied cell behaviour parameters. Functionblocking antibodies and swainsonine (SW) treatment were used in these tests. Both cell lines interacted with VN in an integrin-mediated but cell-line-specific manner. In WM9 cells, migration was not completely inhibited by antibodies against α3β1 or αvβ3 integrins, suggesting the participation of other VN receptors. In both cell lines in coprecipitation test the formation of an integrins/uPAR complex was shown. In the presence of SW formation of the complex did not occur, suggesting the participation of glycosylation in this proccess. Additionally, the adhesion properties of WM9 cells were changed after SW treatment. Our results suggest that in these two metastatic cell lines integrin-linked N-oligosaccharides influence the VN adhesion receptor activity and function.

12

Flow cytometry analysis of integrin expression in uveal and cutaneous melanoma cells

71%

Pochec E., Przybylo M., Plesniak R., Litynska A., Laidler P.

Acta Biochimica Polonica

|

2006

|

tom 53

|

nr Supplement 1

13

Myokine irisin-induced protection against oxidative stress in vitro. Involvement of heme oxygenase-1 and antioxidazing enzymes superoxide dismutase-2 and glutathione peroxidase

71%

Mazur-Bialy A. I., Kozlowska K., Pochec E., Bilski J., Brzozowski T.

Journal of Physiology and Pharmacology

|

2018

|

tom 69

|

nr 1

14

Identification of PNA-positive proteins in the primary uveal melanoma cell line by mass spectrometry

61%

Hoja-Lukowicz D., Litynska A., Pochec E., Przybylo M., Kremser E., Ciolczyk-Wierzbicka D., Laidler P.

Acta Biologica Cracoviensia. Series Zoologia

|

2006

|

tom 48

39-47

15

The structure of the oligosaccharides of alpha3beta1 integrin from human ureter epithelium [HCV29] cell line

61%

Litynska A., Pochec E., Hoja-Lukowicz D., Kremser E., Laidler P., Amoresano A., Monti C.

Acta Biochimica Polonica

|

2002

|

tom 49

|

nr 2

There is a growing line of evidence that glycosylation of a and β subunits is important for the function of integrins. Integrin a3β1, from human ureter epithelium cell — line HCV29, was isolated by affinity chromatography on laminin GD6 peptide. Characterization of its carbohydrate moieties was carried out using sodium dodecyl sul- fate/polyacrylamide gel electrophoresis followed by Western blotting on Immobilon P and on-blot deglycosylation with peptide .-glycosidase-F. Profiles of N-glycans for each subunit were obtained by matrix-assisted laser desorption/ionization mass spec- trometry. Our findings demonstrated, in both subunits of integrin a3β1, the presence of complex type oligosaccharides with a wide heterogeneity. Bi- tri- and tetra- antennary structures were the most common, while high-mannose type structures were minor. Also the presence of short poly-. -acetyllactosamine entities was shown. These results show that while the predominant oligosaccharides of both subunits are identical, some slight differences between them do exist.

Ograniczanie wyników

Glikoproteiny układu odpornościowego: struktura i funkcja części cukrowej wybranych receptorów błonowych limfocytów T. Cz. I

Glikoproteiny układu odpornościowego: rola glikanów antygenów zgodności tkankowej (MHC) oraz znaczenie galektyn w aktywacji i apoptozie limfocytów T. Cz. II

HMGB1 inhibition during zymosan-induced inflammation: the potential therapeutic action of riboflavin

Rola glikozylacji w aktywacji receptora nabłonkowego czynnika wzrostu

Diverse expression of N-acetylglucosaminyltransferase V and complex-type Beta1,6-branched N-glycans in uveal and cutaneous melanoma cells

Integrin alpha3 beta1 from human melanoma; characterisation of its N-linked oligosaccharides

New insight into the direct anti-inflammatory activity of a myokine irisin against proinflammatory activation of adipocytes. Implication for exercise in obesity

N-glycoproteins bearing beta1-6 branching oligosaccharides from A375 human melanoma cell line analysed by HPLC/MS

Immunomodulatory effect of riboflavin deficiency and enrichment - reversible pathological response versus silencing of inflammatory activation

Adhesion properties of human bladder cell lines with extracellular matrix components: the role of integrins and glycosylation

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

Flow cytometry analysis of integrin expression in uveal and cutaneous melanoma cells

Myokine irisin-induced protection against oxidative stress in vitro. Involvement of heme oxygenase-1 and antioxidazing enzymes superoxide dismutase-2 and glutathione peroxidase

Identification of PNA-positive proteins in the primary uveal melanoma cell line by mass spectrometry

The structure of the oligosaccharides of alpha3beta1 integrin from human ureter epithelium [HCV29] cell line