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PubMed:11920503 JSONTXT

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DisGeNET

Id Subject Object Predicate Lexical cue
T0 805-810 gene:4313 denotes MMP-2
T1 694-715 disease:C0476089 denotes endometrial carcinoma
R1 T0 T1 associated_with MMP-2,endometrial carcinoma

DisGeNET5_gene_disease

Id Subject Object Predicate Lexical cue
11920503-4#123#128#gene4313 805-810 gene4313 denotes MMP-2
11920503-4#145#150#gene4318 827-832 gene4318 denotes MMP-9
11920503-4#167#174#gene4323 849-856 gene4323 denotes MT1-MMP
11920503-4#180#187#gene7076 862-869 gene7076 denotes TIMPs 1
11920503-4#12#33#diseaseC0476089 694-715 diseaseC0476089 denotes endometrial carcinoma
123#128#gene431312#33#diseaseC0476089 11920503-4#123#128#gene4313 11920503-4#12#33#diseaseC0476089 associated_with MMP-2,endometrial carcinoma
145#150#gene431812#33#diseaseC0476089 11920503-4#145#150#gene4318 11920503-4#12#33#diseaseC0476089 associated_with MMP-9,endometrial carcinoma
167#174#gene432312#33#diseaseC0476089 11920503-4#167#174#gene4323 11920503-4#12#33#diseaseC0476089 associated_with MT1-MMP,endometrial carcinoma
180#187#gene707612#33#diseaseC0476089 11920503-4#180#187#gene7076 11920503-4#12#33#diseaseC0476089 associated_with TIMPs 1,endometrial carcinoma

PubMed_Structured_Abstracts

Id Subject Object Predicate Lexical cue
T1 165-496 BACKGROUND denotes The actions of the extracellular-matrix degrading enzymes, matrix metalloproteinases (MMPs), are implicated in tumorigenesis. The cellular localization of MMP-2, MMP-9, membrane type 1 (MT1)-MMP, tissue inhibitors of metalloproteinases (TIMPs) 1-3, and the presence of active gelatinases were investigated in endometrial carcinoma.
T2 506-1016 METHODS denotes Endometrial carcinomas were grouped according to histologic grade (Grades 1-3), depth of myometrial invasion (0, < 50%, > 50%) and the presence of vascular/lymphatic invasion. Twenty-nine endometrial carcinoma biopsies were investigated immunohistochemically to determine the tissue localization of MMP-2 (gelatinase A), MMP-9 (gelatinase B), MT1-MMP, and TIMPs 1-3. In situ hybridization was performed to localize MMP-2 and MMP-9 mRNA. The presence of active gelatinases was assessed using in situ zymography.
T3 1026-2329 RESULTS denotes Epithelial tumor cells were the main site of MMP-2, MMP-9, and MT1-MMP protein. Variable stromal cell localization was also observed, particularly in areas adjacent to tumor nests. Semiquantitative analysis revealed increases in MMP-9 and MMP-2 but not MT1-MMP staining scores in tumor epithelial cells in the transition from histologic Grade 1 to Grades 2 and 3. Matrix metalloproteinase-9 and MT1-MMP staining scores in tumor cells were significantly associated with the presence of myometrial invasion and vascular/lymphatic invasion, while MMP-2 did not correlate with these factors. In addition, MT1-MMP was co-localized with MMP-2, supporting its role in the activation of proMMP-2. Tumor cells from all histologic grades stained intensely for TIMP-2 and TIMP-3 proteins, while variable stromal staining was observed. In Grade 1 carcinomas TIMP-1 was predominantly immunolocalized to the stromal compartment with variable tumor cell localization being observed in Grades 2 and 3 carcinomas. Matrix metalloproteinase-9 and MMP-2 mRNAs were predominantly observed in tumor epithelial cells as well as in the stroma to varying degrees. In situ zymography revealed active forms of gelatinases at the cellular surface and in association with tumor epithelial cells within endometrial carcinoma tissues.
T4 2343-2605 CONCLUSIONS denotes These data suggest that increasing expression of MMPs and endometrial carcinoma progression are closely related. Active gelatinases are present in endometrial carcinoma, resulting in alterations to the microenvironment that promote tumor invasion and metastasis.