Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 55 (1977), S. 359-373 
    ISSN: 1432-1440
    Keywords: Lectins ; Phytohaemagglutinins ; Glycoproteins ; Enzyme differentiation ; Affinity chromatography ; Lectine ; Phytohämagglutinine ; Glykoproteine ; Enzym-Differenzierung ; Affinitätschromatographie
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Lectine sind Proteine, die ursprünglich in Pflanzensamen nachgewiesen wurden. Sie zeichnen sich durch die Fähigkeit aus, Polysaccharide beziehungsweise Glykoproteine und Glykolipide auf Grund ihres Zuckeranteils zu binden. In der vorliegenden Übersicht werden neben dem molekularem Aufbau und der Spezifität der Lectine die in vivo und in vitro Funktionen, wie Glykoprotein-Präzipitation, Agglutination von Zellen, Transformation von Lymphozyten und Toxinwirkung dargestellt. Die wachsende Bedeutung der Lectine wird am Beispiel der kürzlich aus Kaninchenleber gewonnenen Lectin-analogen Proteine aufgezeigt, die für die Reabsorption zirkulierender Glykoproteine verantwortlich sind. Am Beispiel der N-Acetylneuraminsäure (NANA) wird die wesentliche Rolle entständiger Zuckerreste von Glykoproteinen im Rahmen der Fetalentwicklung und onkogenen Transformation sowie der Immunologie und Homöostaseologie demonstriert. Entsprechend den differenten Kohlenhydratresten ist durch affinitätschromatographische Trennung eine Differenzierung adulter, fetaler und transformierter Proteine sowie mehr oder minder immunogener Zellen möglich. Zusätzlich können Lectine zur Reinigung von Proteinen und Zellen herangezogen werden. Die Möglichkeiten des diagnostischen Einsatzes von Lectinen, ihre Bedeutung für das Studium des Glykoprotein-Turnovers sowie ihre Anwendung in der präparativen und analytischen Biochemie werden diskutiert.
    Notes: Summary Lectins are proteins or glycoproteins, originally isolated from plant seeds. Characteristics are their ability to bind glycoproteins or glycolipids depending on the carbohydrate residues. The present review describes the structure of the lectins, their binding specificity and their functions with respect to precipitation of glycoproteins, agglutination of cells, transformation of lymphocytes and toxic action. Recently, lectin-analogs have been described in rabbit liver, which are responsible for the hepatic uptake of circulating glycoproteins. The regulation of this process is intimately linked to the terminal N-Acetylneuraminic acid (NA-NA). Moreover, its significance is shown during fetal development, oncogenic transformation, immunologic recognition as well as homostasis. Due to the different terminal carbohydrate residues, glycoproteins of adult, fetal or transformed cells can be separated using affinity chromatography. Besides the purification of glycoproteins, lectins are also used for the separation of intact cells. Therefore the use of lectins is recommended for preparative and analytical methods, for the measurement of glycoprotein — turnover and for clinical diagnostics.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 57 (1979), S. 151-159 
    ISSN: 1432-1440
    Keywords: Glycoproteins ; Glycosyltransferases ; Lectins ; Oncology ; Immunology ; Glycoproteine ; Glycosyltransferassen ; Lectine ; Onkologie ; Immunologie
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Zunehmende chemische und biochemische Kenntnisse über Struktur, Biosynthese und Katabolismus der Glycopteine haben auch neue Einblicke in die Pathobiochemie und klinische Bedeutung der Glycoproteine ermöglicht. Diese werden in der vorliegenden Übersicht zusammenfassend dargestellt. 1. Während der Fetalperiode besitzen die endständigen Kohlenhydratreste der Glycoproteine wichtige Funktionen bei der Zell-Adhäsion, -Fusion und gerichteten Migration. Daneben wird die Rolle der endständigen N-Acetylneuraminsäure (NANA) von Glycoproteinen für die immunologische Toleranz zwischen Mutter und Kind diskutiert. 2. Unter onkologischen Gesichtspunkten wird der Einfluß des Glycoproteinmusters der Plasmamembran für das Tumorwachstum und die Metastasierung beschrieben. Veränderte Glycosyltransferase-Aktivitäten im Serum von Tumorpatienten gewinnen zunehmend an diagnostischer Bedeutung. 3. Durch endständige Kohlenhydratreste von Glycoproteinen wird nicht nur die Immunogenität von Makromolekülen, sondern auch die Immunkompetenz des Organismus beeinflußt. Hierdurch erlangen diese Strukturen sowohl bei der immunologischen Tumorabwehr als auch bei Autoimmunerkrankungen klinische Relevanz. Über Ergebnisse ausgewählter Fachgebiete wird in einer nachfolgenden Übersicht berichtet (Klin. Wochenschr.57, 199 (1979)
    Notes: Summary Increasing knowledge on structure, biosynthesis and catabolism of glycoproteins have given new insights on the patho-biochemical and clinical significance of these macromolecules. The most important results and conclusions are summarized in this review. 1. The terminal sugars of glycoproteins—N-acetylneuraminic acid (NANA) and L-fucose—as well as the penultimate galactose molecule have important functions in cell interaction, adhesion and recognition. Moreover, these carbohydrates mediate the migration and distribution of cells and it is believed that they are essential part of the feto-maternal “immunological barrier”. 2. Evidence indicating that the composition and pattern of plasma membrane glycoproteins is associated with tumour growth and metastatic formation is accumulating. Moreover, the determination of serum glycosyltransferase activity is gaining increasing interest, because the level of theses enzymes is substantially elevated in patients with neoplastic disease. 3. Diseases of the autoimmunosystem are likely linked to a disturbed glycoprotein metabolism. The clinical importance is underlined by studies on immunotherapy of tumours.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1432-1440
    Keywords: Ascites ; Liver cirrhosis ; Plasminogen ; Antiproteases ; Fibrinolysis ; Dexamethasone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Fibrinolysis induced by the infusion of plasminogen activators into the circulation has been shown to cause coagulation disorders in ascites retransfusion. Dexamethasone is known to inhibit the synthesis of plasminogen activators by peritoneal macrophages. We therefore assessed its potential in preventing the occurrence of fibrinolysis by injecting 16 mg dexamethasone intraperitoneally in 10 patients 24 h before ascites retransfusion was performed. In addition, the effect of dexamethasone upon the activity or concentration of several proteases and antiproteases related to coagulation in plasma and ascites was analyzed on 15 occasions. An increase of the activity of plasminogen, α2-antiplasmin, and antithrombin III, and in the concentration of α1-protease inhibitor in ascites was induced by the dexamethasone injection. However, the reaction was not identical in all patients. Those patients having an increase of plasminogen activities of 0.6 CTA U/ml or more did not show signs of fibrinolysis during retransfusion. The results obtained indicate that intraperitoneal injection of dexamethasone decreases the concentration of plasminogen activators in ascites and thereby reduces the risk of coagulation disorders during retransfusion procedures. Since the effect is variable and not sustained, assessment of preoperative plasminogen concentrations is mandatory in order to prevent complications.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 61 (1983), S. 111-112 
    ISSN: 1432-1440
    Keywords: Lectin ; Gluten-sensitive enteropathy ; High-mannose type glycoproteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The pathogenesis of gluten-sensitive enteropathy is as yet unknown. According to one theory gluten may act as a lectin with toxic properties for the intestinal cells. We can now confirm this theory by laser nephelometric measurements and demonstrate the oligomannosyl specificity of this lectin-like protein gluten. Furthermore, we demonstrate the highly more intensive binding capacity of gluten for the glycoproteins of the immature crypt cells of the intestinal brush border compared to those from the mature villous zone. It is discussed that gluten-sensitive enteropathy is caused by a genetically determined defect-glycosylation of intestinal glycoproteins with the synthesis of more mannosylated glycoproteins.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 61 (1983), S. 669-679 
    ISSN: 1432-1440
    Keywords: Gluten Gluten-sensitive enteropathy ; HLA ; Lectin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The corn protein gluten causes the gluten-sensitive enteropathy in susceptible persons (HLA-antigens). The diagnosis is made on the basis of the morphological criteria of villous atrophy of the jejunal mucosa and the clinical observation that the malabsorption can be healed by a gluten-free diet. The disease, which occurs in children and adults, is a distinct entity. Life-long adherence to a gluten-free diet is difficult. Intentional or unintentional reintroduction of gluten often causes masked disease states. These are best classified on the basis of electron-microscopy study of the jejunal biopsy. We propose a new classification of the phases of remission. A group of diseases exist which are closely related to gluten-sensitive enteropathy. Frequently villous atrophy is detectable. However, the disease does not respond to a gluten-free diet. The pathophysiology of these diseases is at present unclear. Diseases involving autoimmune processes also appear to be associated with gluten-sensitive enteropathy. The common factor is probably an immuno-genetic defect. This is supported by the existence of common HLA-antigen constellations. Gluten has been characterised in vitro as a lectin with oligomannose specifity. This provides a new pathomechanism for the gluten induced enterocytic destruction.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 54 (1976), S. 439-444 
    ISSN: 1432-1440
    Keywords: Gamma-glutamyl isoenzymes ; Phytohaemagglutinins ; Affinity chromatography ; Liver diseases ; Kidney diseases ; Gamma-Glutamyltransferase ; Isoenzyme ; Phytohämagglutinine ; Affinitätschromatographie ; Lebererkrankungen ; Nierenerkrankungen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung In der vorliegenden Untersuchung wird eine neue Möglichkeit der Isoenzymdifferenzierung der Gamma-Glutamyltransferase (GGT) (EC Nr.2.3.2.2.) mit Hilfe von Concanavalin A und Con A-Sepharose aufgezeigt. Auf Grund des unterschiedlichen Zuckeranteils des Glykoproteins kann eine Unterscheidung zwischen Leber- und Nieren-GGT erreicht werden. Weiterhin konnte erstmals ein verändertes Anlagerungsverhalten eines Glykoproteins an Concanavalin A bei bestimmten Erkrankungen nachgewiesen werden. So verliert die Gamma-Glutamyltransferase bei alkoholtoxischer Hepatitis durch vermehrte Neuraminsäurekonzentration am Molekül ihre Con A-Affinität. Mögliche Ursachen der differenten Con A-GGT-Bindungsfähigkeit, sowie der weitere Einsatz affinitätschromatographischer Isoenzymdifferenzierung mit Hilfe von Con A-Sepharose werden diskutiert.
    Notes: Summary In this investigation a new possibility of isoenzyme-differentiation of the gamma-glutamyltransferase (GGT) (EC Nr.2.3.2.2.) was demonstrated by Concanavalin A and Con A-Sepharose. Because of the different sugar content of the glycoproteins distinction between liver- and kidney-GGT is possible. Furthermore it was possible for the first time to show a different precipitation behaviour of one glycoprotein to Concanavalin A in certain diseases. In case of alcoholic hepatitis GGT looses its Concanavalin A-affinity because of increased neuraminic acid concentration. The possible reasons of the different behaviour of the binding affinity of Concanavalin A and Con A-Sepharose and GGT as well as additional use for enzyme-differentiation by Con A-Sepharose affinity chromatography are discussed.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 57 (1979), S. 199-214 
    ISSN: 1432-1440
    Keywords: Glycoproteins ; Glycosyltransferases ; Lectin-like proteins ; Oncology ; Immunology ; Gastroenterology ; Hematology and Hemostaseology ; Pulmology ; Neurology ; Glycoproteine ; Glycosyltransferasen ; Lectin-analoge Proteine ; Onkologie ; Immunologie ; Gastroenterologie ; Pulmologie ; Endokrinologie ; Hämatologie u. Blutgerinnung ; Neurologie
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Zunehmende chemische und biochemische Kenntnisse über Struktur, Biosynthese und Katabolismus der Glycoproteine haben auch neue Einblicke in die Pathobiochemie und klinische Bedeutung der Glycoproteine ermöglicht, die in Teil II dieser Übersicht unter Berücksichtigung ausgewählter klinischer Fachgebiete dargestellt werden: 1. Die Glycoproteine der Plasmamembran des Erytrozyten beeinflussen entscheidend sowohl die Antigenität als auch die in-vivo Halbwertszeit dieser Zellen. Pathologische Glycoproteinmuster der Erythrozyten-Membran sind bei verschiedenen Anämie-Formen beschrieben. Auch bestimmte Störungen der Blutgerinnung können als Ergebnis eines veränderten Glycoproteinmusters sowohl der Thrombozyten-Membran als auch einiger Gerinnungsfaktoren gedeutet werden. 2. Die terminalen Kohlenhydratreste zirkulierender Glycoproteine bestimmen deren in-vivo-Halbwertszeit. Da bei Lebererkrankungen eine gestörte Glycosylierung dieser Proteine möglich ist, sind hiermit neue Ansätze zur Interpretation veränderter Glycoproteinkonzentrationen und Enzymaktivitäten im Plasma bei diesen Erkrankungen gegeben. Lectin-analoge Proteine der Plasmamembran von Hepatozyten sind wahrscheinlich an der Genese von Lebererkrankungen beteiligt. 3. Ebenso sind die Glycoproteine des Tracheobronchialsekrets bei verschiedenen Erkrankungen strukturellen Änderungen unterworfen, die auch für das pathobiochemische Verständnis von Bedeutung sein können. 4. Über die strukturabhängige Funktion der Glycoproteine des Genitaltrakts und deren endokrinologische Steuerung liegen neue Erkenntnisse vor. Daneben wird durch die terminalen Kohlenhydratreste verschiedener Hypophysen-Hormone deren Akzeptor-Rezeptor-Spezifität mitbestimmt. 5. Über die Rolle terminaler Zuckerreste von Glycokonjugaten bei der Kontaktfindung von Nervenzellen sowie bei der Erregungsausbreitung liegen, teilweise noch hypothetische, Denkmodelle vor. Sowohl bei genetisch determinierten als auch erworbenen malignen und benignen Erkrankungen des Zentralnervensystems sind pathologische Glycoproteinmuster oder Glycosyltransferase- und Glycosidase-Aktivitäten nachgewiesen. Insgesamt verspricht das Studium des Glycoprotein-Stoffwechsels damit für viele klinische Bereiche neue Ansätze für pathobiochemische, diagnostische und therapeutische Fragestellungen.
    Notes: Summary Increasing knowledge on structure, biosynthesis and catabolism of glycoproteins have given new insights on the pathobiochemical and clinical significance of these macromolecules. The most important results and conclusions are summarized here. For part I of this review see Klin. Wochenschr. 1. Glycoconjugates of the erythrocyte membrane are mainly responsible for the antigenic behaviour and the half-life of these cells. Pathological alterations of the glycoprotein pattern have been found in cases of anemia. Several findings suggest that certain types of hemostatic impairment can be ascribed to changes of the glycoprotein composition of both the platelets and the clotting factors. 2. Terminal sugars determine the half-life of circulating glycoproteins. The observed changes of the glycoprotein concentration and enzyme activity in the serum of patients with liver diseases can be partly attributed to a disturbed glycosylation within the liver cell. Lectin-like proteins of the plasma membrane are probably involved in the development of hepatic diseases. 3. Bronchopulmonary diseases are quite often accompanied by changes in the amount and composition of glycoproteins secreted, a finding which might be important when elucidating the pathobiochemical mechanism. 4. Recently, substantial interest has been generated by findings of a structure-dependent function of glycoproteins within the genital tract. It is known that terminal sugars influence the acceptor-receptor specificity of several hormones released by the hypophysis. 5. The function of terminal sugar residues during the process of contact finding and the excitation transmission between neurons is well-established. Congenital or acquired diseases of the central nervous system, either benignant or malignant, often exhibit pathologic alterations of the glycoprotein pattern and the activity of glycosyltransferases or glycosidases. Taken together studies on glycoprotein metabolism may shed new light on pathogenesis, diagnosis and treatment of many diseases.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 8
    ISSN: 1432-1440
    Keywords: Plasminogen ; Fibronectin ; Antiproteases ; Ascites ; Liver cirrhosis ; Tumors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The concentrations of several proteases and antiproteases known to be present in ascites were tested in plasma and ascitic fluid with regard to their ability to separate ascites according to malignant or nonmalignant disease. Seventeen patients with proven malignant ascites and 37 with ascites due to liver cirrhosis were included. Activities of plasminogen,α 2-antiplasmin, antithrombin-III, and factor V, and the concentration ofα 1-protease inhibitor were significantly higher in the plasma of patients with malignant ascites than in cirrhotic patients. Fibronectin, plasminogen,α 2-macroglobulin,α 1-protease inhibitor, antithrombin-III, and albumin revealed higher concentrations or activities in malignant ascites than in cirrhotic ascites. Due to a wide variation of most parameters, only fibronectin, antithrombin III, andα 1-protease inhibitor in ascites had a sensitivity and specificity higher than 90% for malignant ascites. When the specific protein/albumin ratio was used, only the accuracy of fibronectin was increased reaching a sensitivity and specificity of 100%. The plasma/ascites gradients of the proteins assessed differed significantly, that of fibronectin being much higher (22±7) than that of all other proteins. In malignant ascites fibronectin concentration was only correlated withα 1-protease inhibitor concentration but not with the concentration or activity of all other proteins, while in cirrhotic ascites most proteins revealed a positive correlation. The determination of the fibronectin concentration or the fibronectin/albumin ratio in ascites can differentiate malignant and nonmalignant ascites. All other proteases and antiproteases assessed are of lesser value for this purpose, although most are significantly increased in ascites and plasma of patients with malignant disorders.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 632 (1991), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Journal of periodontal research 37 (2002), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The local salivary immunoglobulin A (IgA) response in patients with aggressive periodontitis to oral microorganisms and its role for the pathogenesis has not been determined. This study investigated the hypothesis that aggressive periodontitis patients have impaired oral secretory immunity. Our test group was made-up of 19 aggressive periodontitis patients and 19 age- and gender-matched periodontally healthy controls. Total IgA, IgA subclass 1, IgA subclass 2 and IgA reactive to Actinobacillus actinomycetemcomitans Y4, Treponema denticola ATCC 35404 and Candida albicans DSM 3454 were determined by enzyme-linked immunosorbent assay in whole unstimulated and stimulated saliva. A statistically significantly lower concentration and secretion rate of total salivary IgA (P 〈 0.01) and IgA1 (P 〈 0.001) was found in the aggressive periodontitis group in resting and stimulated saliva. A decrease of IgA2 (P 〈 0.05) was seen in resting saliva. Although only minor differences were detected in the concentration and secretion of bacteria-reactive IgA in both groups, the proportion of bacteria-reactive IgA from the total IgA was significantly higher (P 〈 0.01) in the aggressive periodontitis group in all three microorganisms tested. Our results indicate an inhibition of total secretory IgA. In particular an IgA subclass 1-specific decrease in aggressive periodontitis was noted, while the bacteria-reactive humoral immune system in saliva was activated. The role of the decrease of IgA1 immunoglobulins in aggressive periodontitis with respect to susceptibility for periodontal diseases has to be elucidated.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...