concanavalin-a and Cystadenoma

The lectin histochemistry of ovarian mucinous cystadenoma was studied using a panel of lectins comprising Triticum vulgaris, Lotus tetragonolobus, Arachis hypogaea, Griffonia simplicifolia I, concanavalin A, and Dolichus biflorus. All 23 cases examined in this study stained extensively with T. vulgaris. Of all the lectins, D. biflorus was the least reactive. Concanavalin A stained mainly the perinuclear zone, whereas the other lectins frequently stained the cytoplasm, glycocalyx, and extracellular luminal mucin. This pattern of lectin reactivity resembles endocervical more than intestinal epithelium and suggests that ovarian mucinous cystadenomas are of müllerian nature. The lack of difference in lectin reactivity between cystadenomas with and without goblet/Paneth cells supports a common histogenetic origin of both groups.

Topics: Concanavalin A; Cystadenoma; Female; Histocytochemistry; Humans; Lectins; Mucins; Ovarian Neoplasms; Peanut Agglutinin; Plant Lectins; Staining and Labeling; Wheat Germ Agglutinins

The placental alkaline phosphatase was purified by immunoaffinity chromatography from ovarian epithelial tumours to homogeneity. Up to 40% of the catalytical phosphatase activity in these tumours was derived from this placental type alkaline phosphatase (PLAP). The purified enzyme were similar to those of PLAP, whereas the PLAP-like isozyme was more heat-stable and resistant to 8 M urea than PLAP. The amino terminal sequence of the PLAP-like enzyme demonstrated heterogeneity at position three in the N-terminal end compared with PLAP. Phenyl-Sepharose affinity chromatography and different lectin chromatographies demonstrated the tumour-derived enzyme to be microheterogeneous, both with regard to concanavalin A binding and hydrophobicity properties.

Topics: Alkaline Phosphatase; Biomarkers, Tumor; Chromatography, Affinity; Concanavalin A; Cystadenoma; Electrophoresis; Female; GPI-Linked Proteins; Humans; Isoenzymes; Ovarian Neoplasms