Galectin Fingerprinting in Tumor Diagnosis: Differential Expression of Galectin-3 and Galectin-3 Binding Sites, But Not Galectin-1, in BenignvsMalignant Uterine Smooth Muscle Tumors

Abstract

Cell-matrix interactions are governed by a distinct set of proteins, with 2 nonintegrin laminin-binding proteins, galectin-1 and galectin-3, providing 1 aspect. The expression patterns of laminin and the 2 galectins and galectin binding sites were quantitatively determined by means of computer-assisted microscopy with the aim of differentiating between 16 leiomyomas and 10 leiomyosarcomas of the uterus. Three quantitative variables were computed for each of the 5 histochemical markers: labeling index, which describes the percentage of tissue area specifically stained by a given marker; mean optical density which reflects the concentration of the marker; and concentrational heterogeneity, which characterizes the degree of heterogeneity of the marker distribution in the tumor tissue areas. The results reveal evident differences in the galectin-3-related parameters in the 2 tumors groups. Whereas the concentration of galectin-3 binding sites was significantly (P = .01) weaker in the leiomyosarcomas than in the leiomyomas, the percentages of tumor tissue expressing galectin-3 (P = .02) and its binding sites (P = .002) were significantly higher in the leiomyosarcomas than in the leiomyomas. Although significantly (P = .02) higher, the concentration of laminin was more heterogeneously distributed (P = .01) in the leiomyosarcomas than in the leiomyomas. In contrast, the levels of expression of galectin-1 and its accessible binding sites remained similar for both the leiomyomas and the leiomyosarcomas. Finally we document how the levels of expression of galectin-3 and its binding sites can be of assistance in reliably differentiating leiomyomas from leiomyosarcomas.

Galectin-1 and galectin-3 in fetal development of bovine respiratory and digestive tracts

“…The potential for cross-reactivities had been noticed in initial studies (Cerra et al 1984;Carding et al 1985a, b;Hinek et al 1988;Wasano and Yamamoto 1989). Rigorous controls to exclude side reactions with homologous proteins on cells and in tissues are thus necessary, as done for galectin-1 and -3 (Cornillot et al 1998;Kopitz et al 1998;Schwarz et al 1999). Having made suitable tools available, we herein extend our study of galectins in bovine development.…”

Comprehensive galectin fingerprinting in a panel of 61 human tumor cell lines by RT-PCR and its implications for diagnostic and therapeutic procedures

“…Engineered ligand derivatives are instrumental in delineating such alterations in the architecture of the combining sites (Solõ s et al 1996;RuÈ diger et al 2000). Histochemically, these dierences have begun to be exploited in tumor diagnosis by the introduction of labeled galectins as tools in pathology (Andre et al 1999;FrancË ois et al 1999;Schwarz et al 1999;Delorge et al 2000;Plza k et al 2000).…”

Benign metastasizing leiomyoma of the uterus: documentation of clinical, immunohistochemical and lectin-histochemical data of ten cases

“…They can furnish diagnostic information such as is obtained by immunohistochemical means for breast cancer [18,19]. In addition, the presence of galectin-reactive binding sites monitored by labeled galectins is of promising relevance [2], as also recently underscored by the reliable capacity for distinguishing leiomyomas from leiomyosarcomas [35]. The measured intensity of the presence of galectins 1 and 3 in tumor cells was similar in BML, and about 70% of the cells exhibited moderate staining intensity of binding capacities and galectins (Tables 6, 7).…”