Source:http://linkedlifedata.com/resource/pubmed/id/10230352
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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0005456,
umls-concept:C0011900,
umls-concept:C0017262,
umls-concept:C0027651,
umls-concept:C0042149,
umls-concept:C0185117,
umls-concept:C0205183,
umls-concept:C0205282,
umls-concept:C0206658,
umls-concept:C0245382,
umls-concept:C0252527,
umls-concept:C0443199,
umls-concept:C0607430,
umls-concept:C2911684
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pubmed:issue |
5
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pubmed:dateCreated |
1999-5-18
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers,
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Hemagglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0002-9173
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
111
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
623-31
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10230352-Adult,
pubmed-meshheading:10230352-Aged,
pubmed-meshheading:10230352-Antigens, Differentiation,
pubmed-meshheading:10230352-Binding Sites,
pubmed-meshheading:10230352-Biological Markers,
pubmed-meshheading:10230352-Female,
pubmed-meshheading:10230352-Galectin 1,
pubmed-meshheading:10230352-Galectin 3,
pubmed-meshheading:10230352-Hemagglutinins,
pubmed-meshheading:10230352-Humans,
pubmed-meshheading:10230352-Laminin,
pubmed-meshheading:10230352-Middle Aged,
pubmed-meshheading:10230352-Multivariate Analysis,
pubmed-meshheading:10230352-Muscle, Smooth,
pubmed-meshheading:10230352-Uterine Neoplasms
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pubmed:year |
1999
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pubmed:articleTitle |
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.
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pubmed:affiliation |
Laboratory of Histology, Faculty of Medicine, Université Libre de Bruxelles, Brussels, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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