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Query: UNIPROT:P17931 (galectin-3)
 2,860 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Twenty cases of histiocytic sarcoma in 15 female and five male (384 to 722 days of age) hybrid F1 (C57BL/6 x BALB/c) or F2 (F1 x F1) mice were studied for expression of mononuclear phagocyte and other antigens. Histiocytic sarcomas were found most often in liver, uterus, spleen, and lung. Tissues fixed in Bouin's fluid provided preservation of antigen immunoreactivity, using avidin biotin peroxidase complex immunohistochemistry, with monoclonal and polyclonal antibodies. The mononuclear phagocyte antigens, lysozyme and Mac-2 (a galactose-specific lectin that binds IgE), were found in 60-70% of the cases. The receptor for the macrophage colony-stimulating factor (CSF-1), c-fms, was expressed in 2/20 (10%) of the cases. Mouse immunoglobulins were not found in histiocytic sarcoma cells. In uterine histiocytic sarcomas, previously reported as Schwannomas because of their histologic appearance, S-100 protein was not expressed by tumor cells, although they usually expressed Mac-2 and lysozyme. Hyaline droplets were found in the renal tubules of only 2/19 cases. Our studies provide evidence that murine histiocytic sarcoma expresses antigens (Mac-2, lysozyme, c-fms) found in cells of the mononuclear phagocyte series, in contrast to the B-cell origin of many human histiocytic tumors.
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PMID:Expression of mononuclear phagocyte antigens in histiocytic sarcoma of mice. 811 50

Changes in the expression of antigens on mouse uterine or embryonic tissues were examined by enzyme immunocytochemistry. Cryostat sections of uteri from days 1, 8 and 15 of pregnancy were probed with the monoclonal antibodies M3/38 and M3/84, originally defined by their reactivity with macrophage surface antigens (Mac-2 and Mac-3, respectively). In the uterus of pregnant mice, reaction of these antibodies was not limited to leucocytes. M3/38 did not react at detectable levels with cells in the uterus on day 1 but did react with decidual cells immediately surrounding the embryo on day 8. By day 15, the placenta, decidua basalis and metrial gland were intensely positive but the embryo was negative. M3/84 reacted with the luminal side of the endometrium on day 1, the entire decidual mass on day 8, and with all maternal and fetal tissues on day 15. M3/38 was detected in saline-soluble preparations of uterine tissue and had a molecular mass of approximately 32-35 kDa as determined by SDS-PAGE and western blot analysis. The pattern of expression of these molecules suggests a functional relationship to developmental changes that occur at the maternal-fetal interface.
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PMID:Compartmentalized reactivity of M3/38 (anti-Mac-2) and M3/84 (anti-Mac-3) in the uterus of pregnant mice. 850 24

Two beta-galactoside-binding proteins were isolated from uteroplacental complexes of pregnant mice and identified as the S-Lac lectins galectin-1 and galectin-3. The spatiotemporal pattern of appearance of those proteins was determined by immunocytochemistry. Galectin-1 was present in all tissue compartments of the uterus except the luminal and glandular epithelium. It was found in the uteri of animals from all preimplantation stages of pregnancy, as well as in those from nonpregnant, ovariectomized, or sexually immature animals. After implantation of the embryo, cells of the decidua basalis were labeled, as were granular metrial gland cells, all trophoblastic elements of the placenta, the myometrium, and nondecidualized endometrium. By contrast, there was little evidence of galectin-3 in the uteri of nonpregnant animals or during the preimplantation stages of pregnancy. However, immunoreactive material was observed in endometrial cells of the primary decidual zone immediately after implantation and at later stages of pregnancy in the decidua basalis, metrial gland, and all trophoblastic elements of the placenta. There was no evidence of galectin-3 in the myometrium or nondecidualized endometrium. After parturition, amounts of galectin-3 in the endometrium and metrial triangle appeared to decrease as the implantation sites were resorbed. These data suggested that the function of galectin-1 is one of tissue maintenance, whereas the function of galectin-3 is related specifically to pregnancy.
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PMID:Differential expression of two beta-galactoside-binding lectins in the reproductive tracts of pregnant mice. 886 71

In mice, immunoreactive galectin-3 protein has previously been localized in uterine epithelial cells adjacent to implanting blastocysts as well as in the decidualized endometrium of implantation sites, uterine natural killer cells, and several types of placental trophoblast cells. Because galectin-3 is a soluble extracellular molecule, protein localization by immunohistochemical methods does not demonstrate its cellular origin. Therefore, the present study was undertaken to determine precisely which cell types in the utero-placental complex express galectin-3 mRNA. In situ hybridization results demonstrated that galectin-3 mRNA was expressed throughout the utero-placental complex in all cell types previously shown to contain immunoreactive protein, including uterine epithelium, decidualized endometrium, uterine natural killer cells, and placental trophoblasts. These results indicate that galectin-3 protein is not synthesized in a restricted cell type and translocated through the extracellular spaces to other tissue compartments. Furthermore, Northern blot analysis of total RNA prepared from separated fetal and maternal components of utero-placental complexes demonstrated different patterns of expression for galectin-3 mRNA in the uterus and placenta. Relative levels of galectin-3 mRNA peak at midgestation in the implantation site and during the second half of gestation remain elevated in the placenta but decline in the uterus. Separate mechanisms for regulating expression of galectin-3 on opposite sides of the feto-maternal interface are indicated.
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PMID:Spatio-temporal pattern for expression of galectin-3 in the murine utero-placental complex: evidence for differential regulation. 960 64

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.
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PMID:Galectin fingerprinting in tumor diagnosis. Differential expression of galectin-3 and galectin-3 binding sites, but not galectin-1, in benign vs malignant uterine smooth muscle tumors. 1023 Mar 52

The expression and immunohistochemical localization of galectin-3, a beta-galactoside-binding protein, was studied in several mouse tissues. Galectin-3 expression was low in the cerebrum, heart, and pancreas, and moderate in the liver, ileum, kidney, and adrenal gland. High expression of galectin-3 was found in the lung, spleen, stomach, colon, uterus, and ovary. The results of Western blot analysis largely matched the immunohistochemical findings for galectin-3. These findings suggest that galectin-3 is differentially expressed in a variety of organs in the mouse. This study provides valuable information for research on galectin-3.
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PMID:Expression and immunohistochemical localization of galectin-3 in various mouse tissues. 1722 70

The protein levels and immunohistochemical localization of galectin-3, which is a beta-galactoside-binding protein, were studied in the cow reproductive organs. Using Western blot analysis, galectin-3 was detected at low levels in the ovary and oviduct, at moderate levels in the uterus, and at high levels in the cervix. Using immunohistochemistry, galectin-3 was immunolocalized in macrophages in the interstitium, in cells in the atretic follicles, and in luteal cells in the regressing corpus luteum, but not in the growing follicles in the ovary. In the oviduct, galectin-3 was detected in some macrophages in the lamina propria, submucosa and muscle layers, as well as in some cells in the covering epithelium. In the uterus, galectin-3 was immunolocalized in some epithelial cells and in some macrophages in the submucosa, but not in the endometrial glands at the non-pregnant stage. In the cervix, galectin-3 was immunolocalized in many mucus-secreting cells in the mucosa and in a few macrophages in the submucosa and muscle layers. Based on its localization, we postulate that galectin-3 in the covering epithelium is involved in the mucosal defense system, and that galectin-3-positive macrophages in all tissues are involved in either cell survival or death. In addition, galectin-3 plays an important role in the regression of follicles and the corpus luteum.
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PMID:Immunohistochemical localization of galectin-3 in the reproductive organs of the cow. 1854 Dec 90

Endometrioid adenocarcinoma (EAC) of the uterus can show varying patterns of invasion, 1 of which, "MELF," is characterized by the presence of microcystic, elongated, and fragmented glands. However, at present, little is known of the functional alterations in neoplastic cells that are associated with the different patterns of myometrial invasion, including those in MELF. Galectin-3 is a widely distributed and multifunctional carbohydrate binding protein that has been shown to influence many aspects of tumor development and progression, but there are limited and conflicting data regarding galectin-3 expression in EAC. In this study, galectin-3 immunoreactivity was investigated in 22 EACs with specific comparison of staining in the "conventional" endometrioid-type tumor glands and in areas exhibiting MELF pattern invasion. Cytoplasmic galectin-3 was present in all tumors although <50% of cells were stained in approximately one-third of the cases. Nuclear staining was evident in 11 cases, but usually only in a small proportion of cells. The neoplastic epithelium within MELF areas showed a consistent reduction in protein expression, often contrasting with the adjacent galectin-3-positive conventional glands and reactive stromal cells. Conversely, intravascular tumor foci often showed cytoplasmic and nuclear galectin-3 immunoreactivity. The microanatomical variation in galectin-3 expression in EAC suggests that there are localized functional alterations in the neoplastic epithelium and the surrounding stroma during the invasive process. As MELF pattern invasion is associated with the loss of galectin-3 expression, there may be implications for the use of galectin inhibitors in the treatment of endometrial carcinomas and other malignancies.
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PMID:Galectin-3 expression in uterine endometrioid adenocarcinoma: comparison of staining in conventional tumor glands and in areas of MELF pattern myometrial invasion. 2088 56

Endometriosis is an enigmatic disease of unknown etiology and pathogenesis, which is defined as the presence of endometrial glands and stroma outside the uterus. The most widely accepted theory to explain endometriosis is probably the transplantation of an endometrial fragment during menstruation to ectopic sites, but the development of endometriosis is extremely complex and includes the adherence to the peritoneal surface and secondary invasion of the underlying tissues. In this study, we have investigated the potential role of galectin-3 (gal-3), a member of a group of carbohydrate-binding proteins, which plays a major role in cell adhesion, migration, angiogenesis, and invasion. The expression of gal-3 has been carried out by immunohistochemistry, according to the different phases of cycle in 50 cases of endometriosis (peritoneal endometriosis: n=10; ovarian endometriosis: n=10; deeply infiltrating endometriosis: n=30) and in 34 cases of eutopic endometrium (10 without endometriosis and 24 with endometriosis). In the proliferative and secretory phases of the cycle, the nuclear and membranous gal-3 expression was higher, first in each variant of the endometriosis than in the eutopic endometrium (P<0.05), and second in the eutopic endometrium of women with endometriosis than in eutopic endometrium of women without endometriosis. Our data suggest that gal-3 may have a potential role in the development of endometriosis.
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PMID:Galectin-3 is overexpressed in various forms of endometriosis. 2103 Aug 59

Galectin-1 and galectin-3 are abundantly expressed at implantation sites in the uterus, suggesting their involvement in the establishment of pregnancy. In this study, we examined the expression and localization of galectin-1 and galectin-3 in fallopian tubes from nonpregnant women, and in those presenting with tubal ectopic pregnancy. There was no significant difference in the expression of either galectin-1 (LGALS1) or galectin-3 (LGALS3) transcripts in the fallopian tube across the menstrual cycle. Their expressions in the fallopian tube were inversely correlated to each other (r = -0.5134, p < 0.0001) and differentially localized. Galectin-1 protein was abundant in the stroma of nonpregnant fallopian tubes, whereas galectin-3 was mainly localized to the epithelium, notably to the cilia of ciliated cells and the apical cytoplasm of secretory cells. In ectopic pregnancies, LGALS3 expression was significantly reduced (p < 0.0001), but LGALS1 expression did not change when compared to nonpregnant fallopian tubes collected during the mid-secretory phase. The percentage of fallopian tube epithelial cells expressing galectin-3 in cilia tended to be reduced (p = 0.0685), with an accompanying loss of a normal ciliary structure, while nuclear galectin-3 increased (p < 0.05) in ectopic pregnancies. Epithelial immunostaining for galectin-1 tended to be elevated in fallopian tubes from women with ectopic pregnancy. Coculture of human trophoblast origin SW71 cells significantly increased LGALS1 expression in human fallopian tube epithelial OE-E6/E7 cells, suggesting that trophoblast-derived products regulate LGALS1 expression in the oviductal epithelium. These findings imply a differential contribution of galectin-1 and galectin-3 in the homeostasis of human fallopian tubes and in the pathophysiology of ectopic pregnancy.
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PMID:The Expression and Cellular Localization of Galectin-1 and Galectin-3 in the Fallopian Tube Are Altered in Women with Tubal Ectopic Pregnancy. 2635 45


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