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    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:
    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:
    Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation
    Autorzy:
    Cylwik, Bogdan
    Lipartowska, Karina
    Chrostek, Lech
    Gruszewska, Ewa
    Powiązania:
    https://bibliotekanauki.pl/articles/1039531.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    O-glycosylation
    genetic defects
    diagnostics
    Opis:
    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.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 3; 361-368
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Congenital disorders of glycosylation. Part I. Defects of protein N-glycosylation
    Autorzy:
    Cylwik, Bogdan
    Naklicki, Marcin
    Chrostek, Lech
    Gruszewska, Ewa
    Powiązania:
    https://bibliotekanauki.pl/articles/1039567.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    N-glycosylation
    genetic defects
    diagnostics
    Opis:
    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.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 2; 151-161
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Effect of α3β1 and αvβ3 integrin glycosylation on interaction of melanoma cells with vitronectin
    Autorzy:
    Janik, Marcelina
    Przybyło, Małgorzata
    Pocheć, Ewa
    Pokrywka, Małgorzata
    Lityńska, Anna
    Powiązania:
    https://bibliotekanauki.pl/articles/1040422.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    adhesion
    integrin
    glycosylation
    migration
    vitronectin
    Opis:
    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.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 1; 55-61
    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:
    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:
    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:
    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:
    Glycosylation of immune system proteins and its role in autoimmune diseases and cancer
    Autorzy:
    Trzyna, Anna
    Tabarkiewicz, Jacek
    Mazur, Artur
    Powiązania:
    https://bibliotekanauki.pl/articles/1597351.pdf
    Data publikacji:
    2020-03-30
    Wydawca:
    Uniwersytet Rzeszowski. Wydawnictwo Uniwersytetu Rzeszowskiego
    Tematy:
    Glycosylation
    Immunity
    Cellular
    Humoral
    Autoimmune Diseases
    Opis:
    Introduction. Structural glycans have great biological significance and are involved in signaling and cell communication of the immune system. They are attached to proteins and lipids in an enzymatic process called glycosylation where glycosyltransferase and glycosidases bind sugar residues and lead to the formation of bioconjugates. Aim. In this paper we describe the importance of glycosylation in the immune system and its changes in diseases. Material and methods. This review was performed according to systematic literature search of major bibliographic databases. Results. Proper glycosylation ensures the functioning of the organism, however, defects in structural glycans of immune system changes their properties and can lead to disorders and further to autoimmune diseases. It has been also proven that glycosylation of autoimmune system is changed during cancer. In this paper we described types of structural glycans, significance of glycosylation of selected components of the immune system and its modifications in disorders. Conclusions. Knowledge about changes in the glycosylation in diseases is the key to understanding the processes of autoimmune diseases and may allow the development of new treatments in the future.
    Źródło:
    European Journal of Clinical and Experimental Medicine; 2020, 1; 32-37
    2544-2406
    2544-1361
    Pojawia się w:
    European Journal of Clinical and Experimental Medicine
    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:
    Changes of the expression of Lewis blood group antigens in glycoproteins of renal cancer tissues
    Autorzy:
    Borzym-Kluczyk, Małgorzata
    Radziejewska, Iwona
    Powiązania:
    https://bibliotekanauki.pl/articles/1039579.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    ELISA
    sialyl Lewisa/x
    glycosylation
    renal cancer
    Opis:
    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.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 2; 223-226
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Inhibitors of N-glycosylation as a potential tool for analysis of the mechanism of action and cellular localisation of glycoprotein P
    Autorzy:
    Wojtowicz, Karolina
    Szaflarski, Witold
    Januchowski, Radosław
    Zawierucha, Piotr
    Nowicki, Michał
    Zabel, Maciej
    Powiązania:
    https://bibliotekanauki.pl/articles/1039626.pdf
    Data publikacji:
    2012
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    N-glycosylation
    glycoprotein P
    multidrug resistance
    inhibitors
    Opis:
    Multidrug resistance has for many years attracted attention of numerous investigators. Attempts have also been made to increase efficiency of anti-neoplastic therapy. For this reason, most of efforts have been devoted to analysing proteins engaged in the mechanism of multidrug resistance such as the N-glycosylated membrane protein glycoprotein P. Interestingly, glycosylation probably plays a significant role in the intracellular location and activity of modified proteins. Inhibitors of glycosylation have been demonstrated to alter the activity of glycoprotein P in various ways, depending on the cell line examined. These inhibitors markedly reduce multidrug resistance of cancer cells, thus promoting success of anti-neoplastic therapy. Here, we review the basic knowledge on N-glycosylation inhibitors, their effect on glycoprotein P and their therapeutic potential.
    Źródło:
    Acta Biochimica Polonica; 2012, 59, 4; 445-450
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Effect of tunicamycin on the biogenesis of hepatitis C virus glycoproteins
    Autorzy:
    Reszka, Natalia
    Krol, Ewelina
    Patel, Arvind
    Szewczyk, Boguslaw
    Powiązania:
    https://bibliotekanauki.pl/articles/1040320.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycoproteins
    glycosylation inhibition
    hepatitis C virus
    tunicamycin
    Opis:
    Hepatitis C virus (HCV) infects humans, with a prevalence around 3% of population, causing acute and chronic hepatitis and hepatocellular carcinoma. We studied the effect of inhibition of glycosylation on the assembly of the HCV particle. HCV possesses two envelope glycoproteins E1 and E2 that are highly modified by N-glycans. These glycan residues are crucial for viral entry and maturation of the progeny. Here, we examined the influence of inhibition of N-glycosylation on expression of E1 and E2. Since the propagation of HCV in cell culture is limited, we used a recombinant baculovirus producing viral-like particles in insect cells. Our data showed that blocking of N-glycan transfer to the nascent polypeptide chain with the antibiotic tunicamycin resulted in the loss of E1 and E2. We also found that a dose of tunicamycin that did not influence the cell viability significantly reduced the E2 level in infected cells. The results indicate that blocking of glycosylation at an early step efficiently reduces the assembly of HCV virions. Thus, we suggest that derivatives of tunicamycin that preferentially block glycosylation of viral proteins may become potential therapeutic agents against HCV.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 4; 541-546
    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
    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:
    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:
    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:
    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:
    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:
    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:
    Distinct expression, localization and function of two Rab7 proteins encoded by paralogous genes in a free-living model eukaryote
    Autorzy:
    Osińska, Magdalena
    Wiejak, Jolanta
    Wypych, Emilia
    Bilski, Henryk
    Bartosiewicz, Rafał
    Wyroba, Elżbieta
    Powiązania:
    https://bibliotekanauki.pl/articles/1039860.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycosylation
    antipeptide antibodies
    Real-Time PCR
    Rab7 isotypes
    RNAi
    2D electrophoresis
    Paramecium octaurelia
    STED
    Opis:
    Rab7 GTPases are involved in membrane trafficking in the late endosomal/lysosomal pathway. In Paramecium octaurelia Rab7a and Rab7b are encoded by paralogous genes. Antipeptide antibodies generated against divergent C-termini recognize Rab7a of 22.5 kDa and Rab7b of 25 kDa, respectively. In 2D gel electrophoresis two immunoreactive spots were identified for Rab7b at pI about 6.34 and about 6.18 and only one spot for Rab7a of pI about 6.34 suggesting post-translational modification of Rab7b. Mass spectrometry revealed eight identical phosphorylated residues in the both proteins. ProQ Emerald staining and ConA overlay of immunoprecipitated Rab7b indicated its putative glycosylation that was further supported by a faster electrophoretic mobility of this protein upon deglycosylation. Such a post-translational modification and substitution of Ala140 in Rab7a for Ser140 in Rab7b may result in distinct targeting to the oral apparatus where Rab7b associates with the microtubular structures as revealed by STED confocal and electron microscopy. Rab7a was mapped to phagosomal compartment. Absolute qReal-Time PCR analysis revealed that expression of Rab7a was 2.6-fold higher than that of Rab7b. Upon latex internalization it was further 2-fold increased for Rab7a and only slightly for Rab7b. Post-transcriptional gene silencing of rab7a suppressed phagosome formation by 70 % and impaired their acidification. Ultrastructural analysis with double immunogold labeling revealed that this effect was due to the lack of V-ATPase recruitment to phagolysosomes. No significant phenotype changes were noticed in cells upon rab7b silencing. In conclusion, Rab7b acquired a new function, whereas Rab7a can be assigned to the phagolysosomal pathway.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 4; 597-607
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    New insight into organic anion transporters from the perspective of potentially important interactions and drugs toxicity
    Autorzy:
    Mor, A.L.
    Kaminski, T.W.
    Karbowska, M.
    Pawlak, D.
    Powiązania:
    https://bibliotekanauki.pl/articles/70038.pdf
    Data publikacji:
    2018
    Wydawca:
    Polskie Towarzystwo Fizjologiczne
    Tematy:
    organic anion transporter
    transmembrane transporter
    drug-drug interaction
    central nervous system
    glycosylation
    herbal preparation
    dietary supplement
    pharmacokinetic interaction
    Źródło:
    Journal of Physiology and Pharmacology; 2018, 69, 3
    0867-5910
    Pojawia się w:
    Journal of Physiology and Pharmacology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Study of concentration of advanced protein glycation products in pregnant women with physiological pregnancy and pregnancy complicated with pre-eclampsia
    Czy AGEs mogą być markerami stanu przedrzucawkowego? Badanie stężenia zaawansowanych produktów glikacji białek u kobiet ciężarnych z ciążą fizjologiczną i ciążą powikłaną stanem przedrzucawkowym
    Autorzy:
    Bodzek, Piotr
    Janosz, Iwona
    Damasiewicz-Bodzek, Aleksandra
    Witek, Łukasz
    Olejek, Anita
    Powiązania:
    https://bibliotekanauki.pl/articles/2130135.pdf
    Data publikacji:
    2022-10-12
    Wydawca:
    Śląski Uniwersytet Medyczny w Katowicach
    Tematy:
    AGEs
    pregnancy
    pre-eclampsia
    non-enzymatic glycosylation
    advanced glycation end products
    ciąża
    stan przedrzucawkowy
    nieenzymatyczna glikozylacja
    zaawansowane produkty glikacji białek
    Opis:
    INTRODUCTION: The role of advanced glycation end products (AGEs) in the pathomechanism of arterial hypertension has been demonstrated, but little information is available on the influence of AGEs on the course of pre-eclampsia (PE). The aim of the study was to assess the concentration profile of advanced protein glycation products in pregnant women diagnosed with PE. MATERIAL AND METHODS: The concentrations of AGEs, carboxymethyllysine (CML), carboxyethyllysine (CEL) and methylglyoxal (MG) in the sera of female respondents were determined using the enzyme immunoassay method. RESULTS: The levels of AGE and CML were lower in the group of women with PE compared to the group of non- -pregnant women (p = 0.0411 and p = 0.0072). A lower CML concentration was found in healthy pregnant women as compared to healthy non-pregnant women (p = 0.00068). Positive correlations were found between AGE and CML levels in women with PE (R = 0.339, p = 0.032) and between CML and CEL in healthy non-pregnant women (R = 0.447, p = 0.012). CONCLUSIONS:We suggest that there is a decrease in the intensity of non-enzymatic protein glycation during pregnancy. Moreover, our study indicates that isolated PE may be associated with a different pathomechanism than chronic hypertension, and therefore AGEs cannot be at present considered a marker of PE.
    WSTĘP: Rola końcowych produktów zaawansowanejglikacji (advanced glycation end products – AGEs) w patomechanizmie nadciśnienia tętniczego została udowodniona, jednak niewiele jest informacji na temat wpływu AGEs na prze-bieg stanu przedrzucawkowego (pre-eclampsia – PE). Celem pracy była ocena profilu stężeń zaawansowanych produktów glikacji białek u kobiet ciężarnych z rozpoznaniem PE. MATERIAŁ I METODY: Oznaczenia stężeń AGEs, karboksymetylolizyny (carboxymethyllysine – CML), karboksyetylolizyny (carboxyethyllysine – CEL) i metyloglioksalu (methylglyoxal – MG) w surowicy badanych kobiet wykonano metodą immunoenzymatyczną. WYNIKI: Stężenia AGE i CML były niższe w grupie kobiet z PE w porównaniu z grupą kobiet nieciężarnych (p = 0,0411 i p = 0,0072). Stwierdzono niższe stężenie CML u zdrowych ciężarnych w porównaniu ze zdrowymi nieciężarnymi (p = 0,00068). Stwierdzono dodatnie korelacje pomiędzy stężeniem AGE i CML u kobiet z PE (R = 0,339, p = 0,032) oraz pomiędzy CML i CEL u zdrowych kobiet nieciężarnych (R = 0,447, p = 0,012). WNIOSKI: Sugerujemy, że w czasie ciąży dochodzi do zmniejszenia intensywności nieenzymatycznej glikacji białek. Ponadto nasze badanie wskazuje, że izolowane PE może być związane z innym patomechanizmem niż przewlekłe nadciśnienie tętnicze i dlatego AGEs nie mogą być obecnie uważane za marker PE.
    Źródło:
    Annales Academiae Medicae Silesiensis; 2022, 76; 106-111
    1734-025X
    Pojawia się w:
    Annales Academiae Medicae Silesiensis
    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
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