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Wyświetlanie 1-15 z 25
Tytuł:
Faba bean albumins glycation
Autorzy:
Kostyra, H.
Darewicz, M.
Smyk, B.
Powiązania:
https://bibliotekanauki.pl/articles/1371479.pdf
Data publikacji:
1992
Wydawca:
Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Tematy:
glycotransferase
food biotechnology
albumin
monosaccharide
protein
pepsin
trypsin
physiological condition
faba bean
enzymatic glycosylation
glycation
Źródło:
Polish Journal of Food and Nutrition Sciences; 1992, 01, 4; 121-126
1230-0322
2083-6007
Pojawia się w:
Polish Journal of Food and Nutrition Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Comparative biochemical analysis of lectin and nuclease from Chelidonium majus L.
Autorzy:
Fik, Ewa
Dalgalarrondo, Michele
Haertlé, Thomas
Goździcka-Józefiak, Anna
Powiązania:
https://bibliotekanauki.pl/articles/1044368.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycoproteins
glycosylation
plant lectins
Chelidonium majus
Opis:
It has been recently recognized that lectins exhibit other activities besides hemagglutination. Previously we have found that purified lectin from Chelidonium majus showed DNase activity (Fik, Goździcka-Józefiak & Kędzia, 1995, Herba Polon. 41, 84-95). Comparison of lectin and DNase from the sap from leaves and roots of Chelidonium majus proved that both these compounds are composed of 24 kDa monomer subunits which have an identical N-terminal sequence but differ in amino-acid composition and degree of glycosylation. Possible interrelationship between lectin and DNase is discussed.
Źródło:
Acta Biochimica Polonica; 2000, 47, 2; 413-420
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Impact of ethanol on innate protection of gastric mucosal epithelial surfaces and the risk of injury
Autorzy:
Slomiany, A.
Piotrowski, E.
Piotrowski, J.
Slomiany, B.L.
Powiązania:
https://bibliotekanauki.pl/articles/69166.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Fizjologiczne
Tematy:
mucin glycosylation
ethanol
innate protection
in vivo
gastric mucus
gastric mucosa
epithelial surface
in vitro
binding protein
gastric injury
Źródło:
Journal of Physiology and Pharmacology; 2000, 51, 3
0867-5910
Pojawia się w:
Journal of Physiology and Pharmacology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The participation of ribosome-UDP-GalNAc complex in the initiation of protein glycosylation in vitro
Autorzy:
Paszkiewicz-Gadek, Anna
Porowska, Halina
Gindzieński, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1044369.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
UDP-GalNAc-transferase
UDP-GalNAc
apomucin
ribosome
Opis:
The gastric epithelial cells ribosome-UDP-GalNAc complex is a donor of UDP- GalNAc as the substrate for N-acetylgalactosaminyltransferase, which catalyse the transfer of GalNAc residue to the polypeptide, existing on polysomes. It was observed that the deglycosylated porcine mucin and synthetic peptide (PTSSPIST) can be also glycosylated with participation of N-acetylgalactosaminyltransferase and ribosome- UDP-GalNAc complex. The probability of the ribosome-UDP-GalNAc complex as an intermediate in the O-glycosylation is considered.
Źródło:
Acta Biochimica Polonica; 2000, 47, 2; 421-426
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Adhesion properties of human bladder cell lines with extracellular matrix components: the role of integrins and glycosylation.
Autorzy:
Lityńska, Anna
Przybyło, Małgorzata
Pocheć, Ewa
Laidler, Piotr
Powiązania:
https://bibliotekanauki.pl/articles/1043727.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
integrins
bladder cell lines
adhesion
Opis:
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 α2, a5 and β1 integrin subunits 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 α3 integrin increased adhesion of cancer cells to collagen, LN and FN, but also of the HCV29 line with colagen. It seems that α3 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. N-Acetylneuraminic acid inhibited adhesion of all cell lines to LN and FN irrespective of their malignancy.
Źródło:
Acta Biochimica Polonica; 2002, 49, 3; 643-650
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Adhesive properties of carcinoembryonic antigen glycoforms expressed in glycosylation-deficient Chinese hamster ovary cell lines.
Autorzy:
Krop-Watorek, Anna
Klopocki, Arkadiusz
Czerwinski, Marcin
Lisowska, Elwira
Powiązania:
https://bibliotekanauki.pl/articles/1043841.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
solid-phase cell adhesion assay
N-glycoforms
carcinoembryonic antigen
glycosylation defective mutants
Opis:
Carcinoembryonic antigen (CEA) is an oncofoetal cell surface glycoprotein that serves as an important tumour marker for colorectal and some other carcinomas. Its immunoglobulin-like structure places CEA within the immunoglobulin superfamily. CEA functions in several biological roles including homotypic and heterotypic (with other CEA family members) cell adhesion. Cell-cell interaction can be modulated by different factors, e.g., post-translational modifications such as glycosylation. The purpose of this study was to examine whether changes in carbohydrate composition of CEA oligosaccharides can influence homotypic (CEA-CEA) interactions. In order to modulate glycosylation of CEA we used two different glycosylation mutants of Chinese hamster ovary (CHO) cells, Lec2 and Lec8. Lec2 cells should produce CEA with nonsialylated N-glycans, while Lec8 cells should yield more truncated sugar structures than Lec2. Parental CHO (Pro5) cells and the glycosylation deficient mutants were stably transfected with CEA cDNA. All three CEA glycoforms, tested in a solid-phase cell adhesion assay, showed an ability to mediate CEA-dependent cell adhesion, and no qualitative differences in the adhesion between the glycoforms were observed. Thus, it may be assumed that carbohydrates do not play a role in homotypic adhesion, and the interactions between CEA molecules depend solely on the polypeptide structure.
Źródło:
Acta Biochimica Polonica; 2002, 49, 1; 273-283
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The structure of the oligosaccharides of α3β1 integrin from human ureter epithelium (HCV29) cell line.
Autorzy:
Lityńska, Anna
Pocheć, Ewa
Hoja-Łukowicz, Dorota
Kremser, Elżbieta
Laidler, Piotr
Amoresano, Angela
Monti, Chiara
Powiązania:
https://bibliotekanauki.pl/articles/1043787.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
α3β1 integrin
cell line
MALDI MS
Opis:
There is a growing line of evidence that glycosylation of α and β subunits is important for the function of integrins. Integrin α3β1, 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 sulfate/polyacrylamide gel electrophoresis followed by Western blotting on Immobilon P and on-blot deglycosylation with peptide N-glycosidase-F. Profiles of N-glycans for each subunit were obtained by matrix-assisted laser desorption/ionization mass spectrometry. Our findings demonstrated, in both subunits of integrin α3β1, the presence of complex type oligosaccharides with a wide heterogeneity. Bi- tri- and tetraantennary structures were the most common, while high-mannose type structures were minor. Also the presence of short poly-N-acetyllactosamine entities was shown. These results show that while the predominant oligosaccharides of both subunits are identical, some slight differences between them do exist.
Źródło:
Acta Biochimica Polonica; 2002, 49, 2; 491-500
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation.
Autorzy:
Perlińska-Lenart, Urszula
Kurzątkowski, Wiesław
Janas, Piotr
Kopińska, Agnieszka
Palamarczyk, Grażyna
Kruszewska, Joanna
Powiązania:
https://bibliotekanauki.pl/articles/1041477.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
protein secretion
DPM1 gene
Aspergillus
dolichylphosphate mannose synthase
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2005, 52, 1; 195-205
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity
Autorzy:
Indyk, Katarzyna
Olczak, Teresa
Ciuraszkiewicz, Justyna
Wątorek, Wiesław
Olczak, Mariusz
Powiązania:
https://bibliotekanauki.pl/articles/1041040.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
protein secretion
azurocidin
antimicrobial activity
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2007, 54, 3; 567-573
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Comparison of the localization and post-translational modification of Campylobacter coli CjaC and its homolog from Campylobacter jejuni, Cj0734c/HisJ
Autorzy:
Wyszyńska, Agnieszka
Tomczyk, Karolina
Jagusztyn-Krynicka, Elżbieta
Powiązania:
https://bibliotekanauki.pl/articles/1041127.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
Campylobacter
protein localization
Opis:
Campylobacter is an asaccharolytic microorganism which uses amino acids as a source of carbon and energy. CjaC/HisJ is a ligand-binding protein, a component of the ABC transport system. Campylobacter CjaC/HisJ is post-translationally modified by glycosylation. The number of glycosylation motifs present in the CjaC protein is species-specific. C. coli CjaC has two and C. jejuni one motif (E/DXNYS/T) which serves as a glycan acceptor. Although the two C. coli CjaC motifs have identical amino-acid sequences they are not glycosylated with the same efficiency. The efficacy of CjaC glycosylation in Escherichia coli containing the Campylobacter pgl locus is also rather low compared to that observed in the native host. The CjaC localization is host-dependent. Despite being a lipoprotein, CjaC is recovered in E. coli from the periplasmic space whereas in Campylobacter it is anchored to the inner membrane.
Źródło:
Acta Biochimica Polonica; 2007, 54, 1; 143-150
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effect of N-glycosylation inhibition on the synthesis and processing of classical swine fever virus glycoproteins
Autorzy:
Tyborowska, Jolanta
Zdunek, Ewa
Szewczyk, Bogusław
Powiązania:
https://bibliotekanauki.pl/articles/1040876.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycoproteins
pestivirus
glycosylation
classical swine fever virus
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2007, 54, 4; 813-819
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Studies on oligosaccharyl transferase in yeast
Autorzy:
Lennarz, William
Powiązania:
https://bibliotekanauki.pl/articles/1040850.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
oligosaccharyl transferase
protein glycosylation
yeast
Opis:
In yeast, OT consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. All yeast OT subunits have been cloned and sequenced (Kelleher et al., 1992; 2003; Kelleher & Gilmore, 1997; Kumar et al., 1994; 1995; Breuer & Bause, 1995) and the structure of one of them, Ost4p, has been solved by NMR (Zubkov et al., 2004). Very recently, the preliminary crystal structure of the lumenal domain of an archaeal Stt3p homolog has been reported (Mayumi et al., 2007). Homologs of all OT subunits have been identified in higher eukaryotic organisms (Kelleher et al., 1992; 2003; Kumar et al., 1994; Kelleher & Gilmore, 1997).
Źródło:
Acta Biochimica Polonica; 2007, 54, 4; 673-677
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Alterations in protein secretion caused by metabolic engineering of glycosylation pathways in fungi
Autorzy:
Kruszewska, Joanna
Perlińska-Lenart, Urszula
Górka-Nieć, Wioletta
Orłowski, Jacek
Zembek, Patrycja
Palamarczyk, Grażyna
Powiązania:
https://bibliotekanauki.pl/articles/1040697.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
protein secretion
Trichoderma
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2008, 55, 3; 447-456
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Disruption of Trichoderma reesei gene encoding protein O-mannosyltransferase I results in a decrease of the enzyme activity and alteration of cell wall composition
Autorzy:
Górka-Nieć, Wioletta
Pniewski, Michał
Kania, Anna
Perlińska-Lenart, Urszula
Palamarczyk, Grażyna
Kruszewska, Joanna
Powiązania:
https://bibliotekanauki.pl/articles/1040737.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Trichoderma reesei
pmt1 gene disruption
protein glycosylation
cell wall composition
Opis:
In fungi transfer of the first mannosyl residue to proteins during their O-glycosylation is catalyzed by protein O-mannosyltransferases encoded by pmt genes. Disruption of the pmt1 gene in Trichoderma caused a significant decrease in the total activity of protein O-mannosyltransferases. Moreover, disruption of the pmt1 gene also led to osmotic sensitivity of the strain, indicating an essential role of the PMTI protein activity for cell wall synthesis. At the same time, the strain was defective in septa formation, producing only half the number of septa per unit length of hypha compared with the wild type. Disruption of the pmt1 gene decreased protein secretion but had no effect on glycosylation of secreted proteins, which suggests that PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins.
Źródło:
Acta Biochimica Polonica; 2008, 55, 2; 251-259
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Analysis of recombinant Duffy protein-linked N-glycans using lectins and glycosidases
Autorzy:
Grodecka, Magdalena
Czerwiński, Marcin
Duk, Maria
Lisowska, Elwira
Waśniowska, Kazimiera
Powiązania:
https://bibliotekanauki.pl/articles/1040421.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Duffy antigen
chemokine receptor
chemokines
N-glycosylation
lectins
Opis:
Duffy antigen is a glycosylated blood group protein acting as a malarial and chemokine receptor. Using glycosylation mutants we have previously demonstrated, that all three potential glycosylation sites of the Duffy antigen are occupied by N-linked oligosaccharide chains. In this study, wild-type Duffy glycoprotein and three mutants, each containing a single N-glycan, were used to characterize the oligosaccharide chains by lectin blotting and endoglycosidase digestion. The positive reaction of all the recombinant Duffy forms with Datura stramonium and Sambucus nigra lectins showed that each Duffy N-linked glycan contains Galβ1-4GlcNAc units terminated by (α2-6)-linked sialic acid residues, typical of complex oligosaccharides. The reactivity with Aleuria aurantia and Lens culinaris lectins suggested the presence of (α1-6)-linked fucose at the N-glycan chitobiose core. The failure of the Galanthus nivalis and Canavalia ensiformis lectins to bind to any of the Duffy mutants or to the wild-type antigen indicated that none of the three Duffy N-glycosylation sites carries detectable levels of high-mannose oligosaccharide chains. Digestion of Duffy samples with peptide N-glycosidase F and endoglycosidase H confirmed the presence of N-linked complex oligosaccharides. Our results indicate that Duffy antigen N-glycans are mostly core-fucosylated complex type oligosaccharides rich in N-acetyllactosamine and terminated by (α2-6)-linked sialic acid residues.
Źródło:
Acta Biochimica Polonica; 2010, 57, 1; 49-53
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
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