ZIB

Treffer pro Seite

Treffer 1 - 2 | 2 Treffer

Sortierung

Digitale Medien

Wheat germ agglutinin-binding protein changes in highly malignant Friend leukemia cells metastasizing to the liver (1988)

Elia, Giuliano ; Ferrantini, Maria ; Belardelli, Filippo ; [weitere]

Springer

Clinical & experimental metastasis 6 (1988), S. 347-362

zur Merkliste hinzufügen auf der Merkliste

Details

ISSN: 1573-7276

Quelle: Springer Online Journal Archives 1860-2000

Thema: Medizin

Notizen: Abstract We have used binding of radioactive lectins (i.e. Concanavalin A (ConA), Wheat Germ Agglutinin (WGA) andRicinus communis agglutinin I (RCAI)) to membrane glycoproteins separated in SDS gel electrophoresis, to detect specific carbohydrate changes in plasma membrane proteins ofin vivo passaged Friend erythroleukemia cells (FLC). These cells are highly metastatic to the liver, whereas the originalin vitro passaged tumor cells do not metastasize. Marked qualitative differences in the high molecular weight region of the gels (100–200 kD) were observed between the WGA binding glycoproteins of metastaticin vivo passaged FLC and nonmetastaticin vitro passaged FLC. Furthermore, the binding of WGA to plasma membrane proteins ofin vivo passaged FLC was much greater than the binding of WGA to plasma membrane proteins ofin vitro passaged FLC. Lectin binding experiments after sialic acid removal byin situ mild acid hydrolysis of FLC glycoproteins indicated that an increased sialylation of the 120 and 145 kD glycoproteins was responsible for the increased WGA reactivity ofin vivo passaged FLC plasma membranes. Besides the increased sialylation, other changes in glycosylation of the 100–200 kD glycoproteins ofin vivo passaged FLC were observed: (1) qualitative differences between the WGA binding patterns of the two cell types were restored after treatment of the gels with mild acid and subsequent Smith degradation; (2) after chemical removal of sialic acid residues from the gels, qualitative differences in the RCA binding patterns to the glycoproteins of the two cell types were apparent.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01760571

Permalink

Bibliothek	Standort	Signatur	Band/Heft/Jahr	Verfügbarkeit

Andere fanden auch interessant ...

Artikel (Nationallizenzen)

Volltext

Digitale Medien

Cholera toxin B-subunit protects mammalian cells from ricin and abrin toxicity (1982)

Delfini, Carlo ; Sargiacomo, Massimo ; Amici, Carla ; [weitere]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 20 (1982), S. 359-367

zur Merkliste hinzufügen auf der Merkliste

Details

ISSN: 0730-2312

Schlagwort(e): cholera toxin ; abrin ; ricin ; inhibition of protein synthesis ; protection effect ; receptor redistribution ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie , Chemie und Pharmazie , Medizin

Notizen: The glycoproteins ricin and abrin intoxicate cells by inhibiting protein synthesis. Pretreatment of HeLa cells with cholera toxin partially protects them from ricin and abrin activity. The involvement in this phenomenon of the various effects of cholera toxin, namely, redistribution of membrane receptors elicited from protomer B and increasing cyclic AMP concentrations induced by protomer A, were studied. Substances able to enhance cyclic AMP concentrations do not affect ricin and abrin activity, while protomer B alone protects cells. In addition, the effects of several lectins on ricin or abrin toxicity were examined. Almost complete prevention of ricin or abrin activity was obtained using concanavalin A (Con A) and wheat germ agglutinin (WGA). Conversely, neither succinyl Con A nor Ulexeuropeus agglutinin (UEA) affected the cellular response. Both protomer B of cholera toxin and Con A did not alter the binding of ricin or abrin; they seem to protect cells by altering membrane structure.

Zusätzliches Material: 4 Ill.