Preferencje help
Polish version English version Język
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 17

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych:  mucin
help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
1
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Synthesis and macromolecular organization of gastrointestinal mucin

100%
Slomiany A., Slomiany B. L.
Journal of Physiology and Pharmacology
|
1992
|
tom 43
|
nr 2
Mucus glycoproteins (mucins), the principal determinants of mucus protective qualities and mucosal defense, are studied extensively to define pathological aberrations in the relation to gastrointestinal disease and to develop the mucous barrier strengthening agents. Recent work from our laboratory provided evidence as to the initial stages of the gastrointestinal mucin synthesis, molecular size of the apomucin, its macromolecular organization and interaction with other elements of gastrointestinal mucus. Using monoclonal antibodies against apomucin (clone 1H7), O- glycosylated with N-acetylgalactosamine apomucin (clone 2B4), and that against carboxyl terminal of the apomucin (clone 3G12), the mucin synthesizing polysomes were isolated and glycosylated peptides ranging in size from 6-60kDa identified. The in vitro synthesis in the cell-free system also afforded 60-64kDa products recognized by 1H7 and 3G12 antimucin MAbs. The obtained results provided evidence that the mucin core consists of 60kDa peptide which at cotranslational stage is O-glycosylated with N-acetylgalactosamine. Studies on mucin polymer assembly revealed that mucin preparations prepared by equilibrium density gradient centrifugation and Sepharose 2B chromatography (Mantle, M., Mantle, D., and Allen, A. (1981) Biochem. J. 195, 277-285) are not completely purified and contain DNA and extraneous proteins. The evidence was obtained that so called mucin “link protein”, 118kDa glycopeptide, is a N-glycosylated fragment of fibronectin, whereas the supposedly native undegraded mucin isolated by Carlstedt et al. (Biochem. J. (1983) 211, 13-22) was found to contain mucin-fibronectin-DNA complexes. The general picture that emerged from the studies is that the pure mucin consists of 60kDa glycosylated peptides only. The carboxyl terminal (8-12kDa fragment) of these peptides is not glycosylated (naked) and is responsible for mucin interaction with fibronectin and other fibronectin-like extracellular matrix proteins. While the formation of the mucosal coat depends on many other factors and extracellular components, our findings on mucin structure and interaction with the extracellular matrix proteins provide explanation as to the possible mechanism of mucin adherence to the epithelial surfaces.
2

Quantification of the CD8plus T cell response against a mucin epitope in patients with breast cancer

86%
Kokowski K., Harnack U., Dorn D. C., Pecher G.
Archivum Immunologiae et Therapiae Experimentalis
|
2008
|
tom 56
|
nr 2
3

Lactococcus lactis IBB477 presenting adhesive and mucoadhesive properties as a candidate carrier strain for oral vaccination against influenza virus

72%
Radziwill-Bienkowska J. M., Zochowska D., Bardowski J., Mercier-Bonin M., Kowalczyk M.
Acta Biochimica Polonica
|
2014
|
tom 61
|
nr 3
4
Content available remote

The role of mucus and its components in protection and repair within the alimentary tract mucosa: Polish experience

72%
Gindzienski A., Zwierz K., Sarosiek J.
Journal of Physiology and Pharmacology. Supplement
|
2003
|
tom 54
|
nr 3
127-144
The Gastroenterology Research Laboratory at New York Medical College, New York City, NY, directed by Prof. Dr. George B. Jerzy Glass and after his retirement by Prof. Dr. Bronislaw L. Slomiany and Prof. Dr. Amalia Slomiany served as a lunching pad for successful careers in exploration of mucus for Dr. Andrzej Gindzienski and Dr. Krzysztof Zwierz and Janusz Badurski at the Medical School in Bialystok, Poland as well as Dr. Jerzy Sarosiek at Gastroenterology Research Laboratory, University of Virginia Health Sciences Center, Charlottesville, VA and currently, Gastroenterology Research Laboratory, Kansas University Medical Center, Kansas City, KS, USA. The dynamic and insightful research endeavors implemented at the Medical School of Bialystok revealed new information regarding enzymatic pathways of mucin synthesis especially its carbohydrate components such as hexosamines. These discoveries become instrumental in our understanding of the alimentary tract mucin synthesis and function in health and disease. Similarly innovative mucus research conducted across the Atlantic Ocean uncovered the novelty of mucin elaborated within the esophageal submucosal mucous glands in humans by demonstration that its chemical characteristics are different both from human salivary and gastric mucins. In addition, a novel method for the measurement of the thickness of the gastric mucus layer ex vivo in humans has also been developed. These pioneering works are continued at both mucus exploration centers attracting younger generation of investigators enticed by the mystery of the structure and function of the mucus barrier and its leading role in mucosal protection against injury as well as immediate and unequivocal contribution to mucosal repair and reconstitution process.
5
Content available remote

Regulatory effect of dexamethasone on tracheal calcium processing proteins and mucosal secretion

72%
Lee B., Ahn C., Jeon B.-H., Jung E.-M., Yoo Y.-M., Jeung E.-B.
Journal of Physiology and Pharmacology
|
2019
|
tom 70
|
nr 1
6

Polysaccharides and mucin 5AC (MUC5AC) expression in gallbladder mucosa of young patients with gallstones as evaluated by spatial visualization and quantification

72%
Kasprzak A., Malkowski W., Helak-Lapaj C., Seraszek A., Kaczmarek E., Adamek A., Zabel M.
Folia Histochemica et Cytobiologica
|
2010
|
tom 48
|
nr 4
7

Low molecular mass products of depolymerization of purified mucin - attempts at isolation and characterization

72%
Minkiewicz I., Gindzienski A.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 4
Samples of crude mucin were incubated at room temperature for 48 and 96 h in a sodium azide containing buffer, pH 7.0. Then each sample was purified, reduced and alkylated with iodo[14C]acetamide. Electrophoretic analysis demonstrated that radioactivity was incorporated into the mucin subunits and proteins of 100 and 140 kDa. The results of our experiments suggest that the released proteins can be a part of mucin molecule, cleaved by proteolysis and reduction of disulfide bridges.
8
Content available remote

Screening and modulation of extracellular signals by mucous barrier. Serum glycosylphosphatidylinositol phospholipase D (GPI-PLD) releases protective mucous barrier from oral mucosa

72%
Slomiany A., Nishikawa H., Slomiany B. L.
Journal of Physiology and Pharmacology
|
2002
|
tom 53
|
nr 1
Performance of mucosal epithelial barrier is modified by numerous agents that exert effects on mucin-Mucin Binding Protein (MBP)complex.The aim of the studies described was to determine the nature of the damage or modification of oral mucous barrier by the short-term exposure to ethanol.Methods:Culture of rat buccal mucosa in the presence of ethanol and [3H]-labeled proline and palmitate revealed substantial decrease in MBP synthesis and the release of MBP to the medium.The radioscanning of the samples prepared from the culture medium and the apical epithelial membranes subjected to SDS- PAGE and western blotting disclosed that the released,water soluble 97kDa MBP glycopeptide was labeled with proline and palmitate.When the experiments were conducted in the presence of 5mM EDTA,the GPI-PLD inhibitor,the majority of radiolabeled MBP remained in the membrane-bound form and was extractable with Triton X-114.The results on the purified GPI-linked MBP degradation by serum enzyme,by the saliva containing serum transudate,and the suppression of the process by inclusion of GPI-PLD-specific inhibitor support our contention that membrane MBP is released to medium by GPI-PLD- like activity.Results:The release of MBP from apical epithelial surfaces was induced by depletion of mucin and the presence of serum-derived GPI-PLD in the tissue homogenate. Strong likelihood exists that under in situ conditions ethanol-induced transudation of serum to saliva provides the vehicle for the transfer of GPI-PLD activity to salivary contents. Defacement of the oral surfaces from mucous barrier signals prospect of lumenal agent influence on the unprotected epithelial exterior,and allows ingression of microbes and untoward acting substances into the organism.
9

Structure and biosynthesis of human salivary mucins

72%
Zalewska A., Zwierz K., Zolkowski K., Gindzienski A.
Acta Biochimica Polonica
|
2000
|
tom 47
|
nr 4
Human salivary glands secrete two types of mucins: oligomeric mucin (MG1) with molecular mass above 1 MDa and monomeric mucin (MG2) with molecular mass of 200-250 kDa. Monomers of MG1 and MG2 contain havily O-glycosylated tandem repeats located at the central domain of the molecules. MG1 monomers are linked by disulfide bonds located at sparsely glycosylated N- and C-end. MG1 are synthesized by mucous cells and MG2 by the serous cells of human salivary glands.
10

The levels of sMUC-1 in patients with multiple myeloma

58%
Lemancewicz D., Bolkun L., Porowska H., Galar M., Semeniuk J., Kloczko J., Dzieciol J.
Folia Histochemica et Cytobiologica
|
2011
|
tom 49
|
nr 4
11

Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin

58%
Solorzano C., Mayoral M. A., Carlos M. A., Berumen J., Guevara J., Chavez F. R., Mendoza-Hernandez G., Agundis C., Zenteno E.
Folia Histochemica et Cytobiologica
|
2012
|
tom 50
|
nr 3
12

Wchlanianie zelaza pokarmowego w swietle jego chemicznych wlasciwosci

58%
Baranowski W. J.
Bromatologia i Chemia Toksykologiczna
|
2007
|
tom 40
|
nr 2
211-215
13

CA-125 of fetal origin can act as a ligand for dendritic cell-specific ICAM-3-grabbing non-integrin

58%
Mitic N., Milutinovic B., Jankovic M.
Cellular and Molecular Biology Letters
|
2014
|
tom 19
|
nr 2
CA-125 (coelomic epithelium-related antigen) forms the extracellular portion of transmembrane mucin 16 (MUC16). It is shed after proteolytic degradation. Due to structural heterogeneity, CA-125 ligand capacity and biological roles are not yet understood. In this study, we assessed CA-125 as a ligand for dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN), which is a C-type lectin showing specificity for mannosylated and fucosylated structures. It plays a role as a pattern recognition molecule for viral and bacterial glycans or as an adhesion receptor. We probed a human DC-SIGN-Fc chimera with CA-125 of fetal or cancer origin using solid- or fluid-phase binding and inhibition assays. The results showed that DC-SIGN binds to CA-125 of fetal origin and that this interaction is carbohydrate-dependent. By contrast, cancerderived CA-125 displayed negligible binding. Inhibition assays indicated differences in the potency of CA-125 to interfere with DC-SIGN binding to pathogen-related glycoconjugates, such as mannan and Helicobacter pylori antigens. The differences in ligand properties between CA-125 of fetal and cancer origin may be due to specificities of glycosylation. This might influence various functions of dendritic cells based on their subset diversity and maturation-related functional capacity.
14

Dietary influences on the secretion into and degradation of mucin in the digestive tract of monogastric animals and humans

58%
Lien K. A., Sauer W. C., He J. M.
Journal of Animal and Feed Sciences
|
2001
|
tom 10
|
nr 2
15
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Lipopolysaccharide a virulence factor of Helicobacter pylori: effect of antiulcer agents

58%
Piotrowski J.
Journal of Physiology and Pharmacology
|
1998
|
tom 49
|
nr 1
16

Expression of MUC1 mucin in human umbilical vein endothelial cells (HUVEC)

51%
Porowska H., Paszkiewicz-Gadek A., Wosek J., Wnuczko K., Rusak M., Szczepanski M.
Folia Histochemica et Cytobiologica
|
2010
|
tom 48
|
nr 3
17

Chemiczne podstawy wchlaniania zelaza z pokarmow

37%
Baranowski W. J.
Bromatologia i Chemia Toksykologiczna
|
2004
|
tom 37
|
nr 3
237-241
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.