Temat: Glycosylation - Katalog OPAC zbiorów

Skocz do pozycji: 1.

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

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Skocz do pozycji: 2.

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

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Skocz do pozycji: 3.

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

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Skocz do pozycji: 4.

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

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Skocz do pozycji: 5.

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

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Skocz do pozycji: 6.

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

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Skocz do pozycji: 7.

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

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Skocz do pozycji: 8.

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

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Skocz do pozycji: 9.

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

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Skocz do pozycji: 10.

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

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