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1

Activity of partially purified UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase with different peptide acceptors

100%

Porowska H., Paszkiewicz-Gadek A., Gindzienski A.

Acta Biochimica Polonica

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1999

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tom 46

|

nr 2

As part of investigations on the role of the UDP-GalNAc-ribosome complex in the initial O-glycosylation of proteins, we have isolated from porcine gastric mucosa GalNAc-transferase, mucin and apomucin, and its three fractions containing carbohydrate in the amounts: I - 1.6%, II - 0.65% and III - 0.00% (wt/wt) of apomucin mass. Amino acid analysis showed that fractions I and II contained slightly higher amounts of serine and threonine as compared to native mucin and apomucin. The short peptide Pro-Thr-Ser-Ser-Pro-Ile-Ser-Thr was the most effectively glycosylated. Our apomucin preparations are also good acceptors of GalNAc and can be used for testing of O-glycosylation in vitro.

2

Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation

86%

Cylwik B., Lipartowska K., Chrostek L., Gruszewska E.

Acta Biochimica Polonica

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2013

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tom 60

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nr 3

Glycosylation is a form of post-translational modification of proteins and occurs in every living cell. The carbohydrate chains attached to the proteins serve various functions. There are two main types of protein glycosylation: N-glycosylation and O-glycosylation. In this paper, we describe the O-glycosylation process and currently known congenital disorders of glycosylation associated with defects of protein O-glycosylation. This process takes place in the cis Golgi apparatus after N-glycosylation and folding of the proteins. The O-glycosylation is essential in the biosynthesis of mucins, the formation of proteoglycan core proteins and blood group proteins. Most common forms of O-glycans are the mucin-type glycans. There are more than 20 known disorders related to O-glycosylation disturbances. We review 8 of the following diseases linked to defects in the synthesis of O-xylosylglycans, O-N acetylgalactosaminylglycans, O-xylosyl/N-acetylglycans, O-mannosylglycans, and O-fucosylglycans: multiple exostoses, progeroid variant of Ehlers-Danlos syndrome, progeria, familial tumoral calcinosis, Schneckenbecken dysplasia, Walker-Warburg syndrome, spondylocostal dysostosis type 3, and Peter's plus syndrome. Causes of these diseases include gene mutations and deficiency of proteins (enzymes). Their diagnosis includes syndromic presentation, organ-specific expression and laboratory findings.

3

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

86%

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

Acta Biochimica Polonica

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2010

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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.

4

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Role of sulfation in the processing of gastric mucins

86%

Liau Y. H., Murty V. L. N., Slomiany A., Bielanski W., Slomiany B. L.

Journal of Physiology and Pharmacology

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1991

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tom 42

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nr 4

The role of sulfation in the processing of mucus glycoprotein in gastric mucosa was investigated. Rat gastric mucosal segments were incubated in MEM at various medium sulfate concentrations in the presence of [³⁵S]Na₂ SO₄ [³H] glucosamine and [³H]proline, with and without chlorate an inhibitor of PAPS formation. The results revealed that the mucin sulfation attained maximum at 300 µM medium sulfate concentration. Introduction of chlorate into the incubation medium, while having no effect on the protein synthesis as evidenced by [³H]proline incorporation, caused at its optimal concentration of 2 mM a 90% decrease in mucin sulfation and a 40% drop in mucin glycosylation. Evaluation of mucin molecular forms distribution indicated the predominance of the high molecular mucin form in the interacellular fraction and the low molecular mucin from in the extracellular fraction. Increase in medium sulfate caused an increase in the high molecular weight mucin form in both fractions, and this effect was inhibited by chlorate. Also, higher medium sulfate concentrations led to a higher degree of sulfation in the high molecular weight mucin form, the effect of which was inhibited by chlorate. The results suggest that the sulfation process is an early event taking place at the stage of mucin subunit assembly and is required for mucin polymer formation. Hence, the disturbances in mucin sulfation process could be determinal to the maintenance of gastric mucus coat integrity.

5

Age-related profile of beta-N-acetylhexosaminidase glycosylation in rat liver

86%

Litynska A., Przybylo M.

Acta Biochimica Polonica

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1998

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tom 45

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nr 3

β-N-acetylhexosaminidase was prepared from a liver lysosomal fraction obtained from rats between 18 days of gestation (group I) and 72 weeks of age (groups II-VI). A glycan chain analysis was performed after an electrophoresis and blotting, followed by a very sensitive detection system with highly specific digoxigenin-labelled lectins. The presence of high-mannose /hybrid type glycans, as well as their fucosylated forms was shown in all the experimental groups. Complex-type glycans with terminal sialic acid or galactose were present in all the groups except for 1-week-old rats in which only a positive reaction with lectins from Galanthus nivalis and Aleuria aurantia - was observed. Thus it may be assumed that age-related changes in the glycosylation pattern occur on the first days after birth.

6

Binding properties and expression of the Fc gamma receptors on guinea pig peritoneal macrophages treated with inhibitors of glycosylation

86%

Gorczyca W., Halas E., Wieczorek Z., Lisowski J.

Archivum Immunologiae et Therapiae Experimentalis

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1992

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tom 40

|

nr 5-6

7

Subtle differences in glycosylation of blood group M and N type glycophorin A detected with anti-Tn lectins and confirmed by chemical analysis

86%

Krotkiewski H., Duk M., Lisowska E.

Acta Biochimica Polonica

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1995

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tom 42

|

nr 1

A higher content of Tn and sialyl-Tn receptors in glycophorin A of blood group N than in that of blood group M was suggested by reactions with anti-Tn lectins. Analysis of [^-elimination products of two blood group M and two blood group N preparations by gas liquid chromatography-mass spectrometry showed that GalNAc- -ol was detectable in minor amounts in all analyzed samples and its content was higher in the products obtained from desialylated antigens. Moreover, the content of Gal N Ac- -ol detected in blood group N samples was almost twice as high as in respective blood group M samples. Since blood group M and N antigens differ in two amino-acid residues, our results support the existence of sequence-dependent differences in efficiency of substitution of glycophorin GalNAc-Ser/Thr residues with galactose.

8

Immunological functions of steryl glycosides

72%

Shimamura M.

Archivum Immunologiae et Therapiae Experimentalis

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2012

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tom 60

|

nr 5

9

Effect of N-glycosylation inhibition on the synthesis and processing of classical swine fever virus glycoproteins

72%

Tyborowska J., Zdunek E., Szewczyk B.

Acta Biochimica Polonica

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2007

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tom 54

|

nr 4

813-819

Classical swine fever virus (CSFV) is often used as a surrogate model in molecular studies of the closely related hepatitis C virus. In this report we have examined the effect of the inhibition of glycosylation on the survival and maturation of CSFV. Viral glycoproteins (Erns, E1, E2) form biologically active complexes — homo- and heterodimers, which are indispensable for viral life cycle. Those complexes are highly N-glycosylated. We studied the influence of N-glycosylation on dimer formation using Erns and E2 glycoproteins produced in insect cells after infection with recombinant baculoviruses. The glycoproteins were efficiently synthesized in insect cells, had similar molecular masses and formed dimers like their natural counterparts. Surprisingly, the addition of tunicamycin (an antibiotic which blocks early steps of glycosylation) to insect cell culture blocked not only dimer formation but it also led to an almost complete disappearance of E2 even in monomeric form. Tunicamycin did not exert a similar effect on the synthesis and formation of Erns dimers; the dimers were still formed, which suggests that Erns glycan chains are not necessary for dimer formation. We have also found that very low doses of tunicamycin (much lower than those used for blocking N-glycosylation) drastically reduced CSFV spread in SK6 (swine kidney) cell culture and the virus yield. These facts indicate that N-glycosylation inhibitors structurally similar to tunicamycin may be potential therapeutics for the inhibition of the spread of CSFV and related viruses

10

Glycosylation of proteins in healthy and pathological human renal tissues

72%

Borzym-Kluczyk M., Radziejewska I., Darewicz B.

Folia Histochemica et Cytobiologica

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2012

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tom 50

|

nr 4

11

Changes of the expression of Lewis blood group antigens in glycoproteins of renal cancer tissues

72%

Borzym-Kluczyk M., Radziejewska I.

Acta Biochimica Polonica

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2013

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tom 60

|

nr 2

Sialic acid and sialyl Lewisa/x are found on N- and O-glycans of many human malignant cells. Carbohydrate antigens can be used as tumor markers, and an increase of their levels in cancer cells is associated with tumor progression. The aim of this study was to assess the level of some Lewis blood group antigens on glycoproteins in tumor (cancer tissue), intermediate zone (adjacent to tumor tissue), and normal renal cortex/medulla (uninvolved by tumor). The study was performed on tissues taken from 30 patients. Relative amounts of sugar structures of proteins with molecular masses above 30 kDa were determined by ELISA-like test with biotinylated lectins: MAA (Maackia amurensis), SNA (Sambucus nigra), and monoclonal antibodies anti-sialyl Lewisa/x. Higher expression of all examined structures was revealed in cancer tissues. Significant increases were observed for sialic acid linked α 2-3 in cancer tissues when compared to healthy ones and also among intermediate and healthy tissues. The sialic acid linked α 2-6 and sialyl Lewisx structures were significantly increased in cancerous cells when compared to normal and intermediate renal tissue. In case of sialyl Lewisa antigen, a significant difference was discovered between normal and intermediate tissue. Our results confirm that the examined Lewis antigens can be involved in tumor development. Their increase in cancer tissues can suggest their specific role in the process.

12

New insight into organic anion transporters from the perspective of potentially important interactions and drugs toxicity

72%

Mor A. L., Kaminski T. W., Karbowska M., Pawlak D.

Journal of Physiology and Pharmacology

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2018

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tom 69

|

nr 3

13

Congenital disorders of glycosylation. Part I. Defects of protein N-glycosylation

72%

Cylwik B., Naklicki M., Chrostek L., Gruszewska E.

Acta Biochimica Polonica

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2013

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tom 60

|

nr 2

Glycosylation is the most common chemical process of protein modification and occurs in every living cell. Disturbances of this process may be either congenital or acquired. Congenital disorders of glycosylation (CDG) are a rapidly growing disease family, with about 50 disorders reported since its first clinical description in 1980. Most of the human diseases have been discovered recently. CDG result from defects in the synthesis of the N- and O-glycans moiety of glycoproteins, and in the attachment to the polypeptide chain of proteins. These defects have been found in the activation, presentation, and transport of sugar precursors, in the enzymes responsible for glycosylation, and in proteins that control the traffic of component. There are two main types of protein glycosylation: N-glycosylation and O-glycosylation. Most diseases are due to defects in the N-glycosylation pathway. For the sake of convenience, CDG were divided into 2 types, type I and II. CDG can affect nearly all organs and systems. The considerable variability of clinical features makes it difficult to recognize patients with CDG. Diagnosis can be made on the basis of abnormal glycosylation display. In this paper, an overview of CDG with a new nomenclature limited to the group of protein N-glycosylation disorders, clinical phenotype and diagnostic approach, have been presented. The location, reasons for defects, and the number of cases have been also described. This publication aims to draw attention to the possibility of occurrence of CDG in each multisystem disorder with an unknown origin.

14

Alterations in protein secretion caused by metabolic engineering of glycosylation pathways in fungi

72%

Kruszewska J. S., Perlinska-Lenart U., Gorka-Niec W., Orlowski J., Zembek P., Palamarczyk G.

Acta Biochimica Polonica

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2008

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tom 55

|

nr 3

447-456

Due to its natural properties, Trichoderma reesei is commonly used in industry-scale production of secretory proteins. Since almost all secreted proteins are O-glycosylated, modulation of the activity of enzymes of the O-glycosylation pathway are likely to affect protein production and secretion or change the glycosylation pattern of the secreted proteins, altering their stability and biological activity. Understanding how the activation of different components of the O-glycosylation pathway influences the glycosylation pattern of proteins and their production and secretion could help in elucidating the mechanism of the regulation of these processes and should facilitate creation of engineered microorganisms producing high amounts of useful proteins. In this review we focus on data concerning Trichoderma, but also present some background information allowing comparison with other fungal species.

15

Glycophenotype of prostatic carcinomas

72%

Khabaz M., McClure J., McClure S., Stoddart R. W.

Folia Histochemica et Cytobiologica

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2010

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tom 48

|

nr 4

16

Applying plant lectins to assay the effect of environmental pollution on the glycosylation of human placenta

72%

Konska G., Pituch-Noworolska A., Kaczmarczyk G., Tyrkalska K., Zamorska L., Guillot J.

Polish Journal of Environmental Studies

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2005

|

tom 14

|

nr 3

Our study was designed to establish whether air pollution in urbanized industrial centers of southern Poland affects the process of glycosylation in a full-term human placenta. This process of glycosylation was analyzed by the quantitative determination of the binding of WGA and LCA lectins to placental villi. The study was performed on human placentas collected in 1990-91 and 2000-01 in regions of southern Poland differing in their degree of environmental pollution: the highly polluted areas of Upper Silesia and Cracow agglomeration. The Bieszczady area with low pollution was considered the control. The concentrations of nitrogen and sulfur oxides and the concentration of aerosols were used as markers of the degree of air pollution. The direct immunofluorescence reaction of the placenta tissues with fluorescein-labeled (FITC) lectins was used. The staining of the placenta tissues was examined under a fluorescence microscope linked to an analysis system. A microdensytometric method was used to assay the amount of tissue-bound lectins. The results showed no significant effect of the three main air pollutants in the study areas in southern Poland, i.e. nitrogen and sulfur oxides and high level of aerosols, on the structure of WGAand LCA-specific glycoconjugates in human placenta. However, the marked quantitative changes in the degree of lectin binding to placental cellular structures were noted within the last 10-year period in all studied regions.

17

Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation

72%

Perlinska-Lenart U., Kurzatkowski W., Janas P., Kopinska A., Palamarczyk G., Kruszewska J. S.

Acta Biochimica Polonica

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2005

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tom 52

|

nr 1

O-glycosylation has been considered a limiting factor in protein secretion in filamentous fungi. Overexpression of the yeast DPM1 gene encoding dolichylphosphate mannose synthase (DPMS) in an Aspergillus nidulans mutant (BWB26A) deficient in O-glycosylation caused an increase in the number of secretory vesicles and changes in protein secretion. However, the secretory proteins, primarily O-mannosylated glucoamylase and N-glycosylated invertase, were mainly trapped in the periplasmic space. Different glycoforms of invertase were found insite the cells, in the periplasmic space and in the cultivation medium. Our data point to the importance of the cell wall as a barrier in protein secretion.

18

Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity

72%

Indyk K., Olczak T., Ciuraszkiewicz J., Watorek W., Olczak M.

Acta Biochimica Polonica

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2007

|

tom 54

|

nr 3

Azurocidin is an inactive serine protease homolog with primary sequence similarity to neutrophil elastase, cathepsin G, and proteinase 3. The aim of this study was to investigate possible consequences of differential glycosylation of azurocidin in regard to its secretion, protein stability as measured by susceptibility to proteolysis, and antibacterial activity. Site-directed mutagenesis was employed to generate mutant azurocidin variants lacking individual N-glycosylation sites. Our results show that N-linked glycans may play a role in proper azurocidin folding and subsequent secretion by insect cells. We also demonstrate that N-linked glycosylation contributes to azurocidin stability by protecting it from proteolysis. The lack of N-glycosylation at individual sites does not significantly influence the azurocidin antibacterial activity.

19

Cytokine, cytokine receptors and glucorticoid network controlling N-glycosylation of acute phase proteins in vitro

72%

Mackiewicz A.

Folia Histochemica et Cytobiologica

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1992

|

tom 30

|

nr 4

20

Differences of alpha3beta1 integrin glycans from different human bladder cell lines

72%

Litynska A., Przybylo M., Ksiazek D., Laidler P.

Acta Biochimica Polonica

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2000

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tom 47

|

nr 2

Expression as well as properties of integrins are altered upon transformation. Cell adhesion regulated by integrins is modulated by glycosylation, one of the most frequent biochemical alteration associated with tumorogenesis. Characterisation of carbohydrate moieties of alpha3beta1 integrin on the cultured human bladder carcinoma (T-24, Hu456, HCV 29T) and human normal ureter and bladder epithelium (HCV 29, Hu609) cell lines was carried out after an electrophoresis and blotting, followed by immunochemical identification of alpha3 and beta1 integrin chains and analysis of their carbohydrates moieties using highly specific digoxigenin-labelled lectins. In all the studied cell lines alpha3beta1 integrin was glycosylated although in general each subunit differently. Basic structures recognized in beta1 subunit were tri- or tetraantennary complex type glycans in some cases sialylated (T-24, HCV 29, HCV 29T) and fucosylated (Hu609, HCV 29T). Positive reaction with Phaseolus vulgaris agglutinin and Datura stramonium agglutinin suggesting the presence of beta1-6 branched N-linked oligosaccharides was found in cancerous cell lines (T-24, Hu456) as well as in normal bladder epithelium cells (Hu609). High mannose type glycan was found only in beta1 subunit from Hu456 transitional cell cancer line. On the other hand alpha3 subunit was much less glycosylated except the invasive cancer cell line T-24 where high mannose as well as sialylated tri- or tetraantennary complex type glycans were detected. This observation suggests that changes in glycosylation profile attributed to invasive phenotype are rather associated with alpha3 not beta1 subunit.

Ograniczanie wyników

Activity of partially purified UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase with different peptide acceptors

Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation

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

Role of sulfation in the processing of gastric mucins

Age-related profile of beta-N-acetylhexosaminidase glycosylation in rat liver

Binding properties and expression of the Fc gamma receptors on guinea pig peritoneal macrophages treated with inhibitors of glycosylation

Subtle differences in glycosylation of blood group M and N type glycophorin A detected with anti-Tn lectins and confirmed by chemical analysis

Immunological functions of steryl glycosides

Effect of N-glycosylation inhibition on the synthesis and processing of classical swine fever virus glycoproteins

Glycosylation of proteins in healthy and pathological human renal tissues

Changes of the expression of Lewis blood group antigens in glycoproteins of renal cancer tissues

New insight into organic anion transporters from the perspective of potentially important interactions and drugs toxicity

Congenital disorders of glycosylation. Part I. Defects of protein N-glycosylation

Alterations in protein secretion caused by metabolic engineering of glycosylation pathways in fungi

Glycophenotype of prostatic carcinomas

Applying plant lectins to assay the effect of environmental pollution on the glycosylation of human placenta

Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation

Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity

Cytokine, cytokine receptors and glucorticoid network controlling N-glycosylation of acute phase proteins in vitro

Differences of alpha3beta1 integrin glycans from different human bladder cell lines