ascites/sambucus

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Differences in cell surface carbohydrates, and in laminin and fibronectin synthesis, between adherent and non-adherent Ehrlich ascites tumor cells.

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Differences in cell surface carbohydrates and in laminin and fibronectin synthesis between 2 Ehrlich ascites tumor (EAT) cell lines, the adherent and non-adherent EAT cells, have been studied. The adherent EAT (a-EAT) cells grow in monolayer in vitro in the presence of fetal bovine serum. The

Wild-type and cultured Ehrlich ascites tumour cells differ in tumorigenicity, lectin binding patterns and binding to basement membranes.

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Three different variants of the Ehrlich ascites tumour (EAT) cell were derived and the lectin surface reactivities, as well as the malignant characteristics of each variant, were studied. Wild-type cells (EAT-wt) were selected for growth on basement membranes and tissue culture plastic to give EAT-c

Reactivity of mucin-specific lectin from Sambucus sieboldiana with simple sugars, normal mucins and tumor-associated mucins. Comparison with other lectins.

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Mucin-specific lectin from Sambucus sieboldiana (SSA-M) reacts in Western blotting and ELISA with mucins from porcine stomach, bovine and ovine submaxillary glands, the human milk fat globule membrane, in vitro human ovarian, breast and colonic tumor cell lines, and mucins produced in vivo in the

Glycoproteomic identification of potential glycoprotein biomarkers in ovarian cancer proximal fluids.

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BACKGROUND Ovarian cancer is the leading cause of death among all gynecological disorders. Aberrant glycosylation, or more specifically, increased sialylation of proteins has been observed in ovarian cancer. Several sialyltransferase genes have been shown to be up-regulated at both the mRNA and

Differential expression of cell surface sialoglycoconjugates on wild-type and cultured Ehrlich tumor cells as revealed by quantitative lectin-gold ultrastructural cytochemistry.

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Three variants of the classical Ehrlich ascites tumor (EAT) cell have been studied by quantitative, sialic acid-specific, lectin-gold ultrastructural cytochemistry. Electron microscopic examination revealed pronounced differences in the surface morphology of the three cell variants. The wild-type

Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.

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Ovarian cancer causes more deaths than any other gynecological disorder. Perturbed glycosylation is one of the hallmarks of this malignancy. Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer. The majority of ovarian carcinomas express high levels of

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