Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0677930 (primary tumor)
 20,210 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cancer invasion and metastasis remain the major causes of over 90% of patient deaths. Molecular imaging methods such as computed tomography (CT)/magnetic resonance imaging (MRI) can precisely assess primary regional lymph node invasion and distant organ metastasis via body scanning; however, such diagnostic methods are often utilized too late for cancer therapy. To date, pathologic methods mainly provide information on differentiation/proliferation and potential drug therapy biomarkers of primary tumors rather than precisely reveal tumor regional invasion and distant metastasis in the body. We hypothesized that quantification of membrane type-1 matrix metalloproteinase (MT1-MMP) levels in primary tumor tissue will provide a precise assessment of tumor regional lymph node invasion and remote organ metastasis. In this work, we developed peptide-coated Au clusters with intrinsic red fluorescence and a specific mass signal. When these clusters labeled MT1-MMP in tumor tissue sections derived from the xenograft lung carcinoma model, human lung carcinoma and human renal carcinoma, we could directly observe MT1-MMP via optical fluorescence microscopy and quantitatively detect the MT1-MMP expression level via laser ablation inductively coupled plasma mass spectrometry 2D mapping (2D-LA-Mass Mapping). By observing and quantifying the MT1-MMP expression level in primary human lung carcinoma and human renal carcinoma tissue sections, we precisely assessed the risk of primary tumor invasion/metastasis. Importantly, the accuracy of this pathologic method was verified by CT/MRI molecular imaging of cancer patients and traditional hematoxylin and eosin (H&E) staining/immunohistochemistry (IHC)/immunofluorescence (IF) pathologic studies of primary tumor tissues.
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PMID:The Precise Diagnosis of Cancer Invasion/Metastasis via 2D Laser Ablation Mass Mapping of Metalloproteinase in Primary Cancer Tissue. 3035 13

Matrix metalloproteinase-9 (MMP9) has been recognized to be an important factor in cancer invasion and metastasis. In contrast, decorin has been revealed to inhibit primary tumor development. The aim of the present study was to investigate the function of MMP9 and decorin in cervical cancer. Three experiments were performed to analyze the function of MMP9 and decorin in the invasion of cervical cancer by: i) Analyzing the expression of MMP9 and decorin by immunohistochemistry in 100 cervical specimens; ii) determining the concentration of decorin by an enzyme-linked immunosorbent assay (ELISA) using the human squamous cervical cancer cell line CaSki and human endometrial stromal cell line CRL4003 and iii) evaluating the invasion ability of CaSki cells in a cervical invasion model by an invasion assay. Immunohistochemistry revealed that MMP9 was overexpressed in microinvasive carcinoma (100.0%) but was less strongly expressed in normal or pre-malignant squamous epithelium (0-41.9%). In contrast, the activity of decorin in stroma adjacent to neoplastic cells was lower in microinvasive carcinoma (9.1%) compared with in normal or pre-malignant lesions (74.2-100.0%). An ELISA revealed that MMP9 released from CaSki cells resolved the decorin released from CRL4003 cells. An invasion assay demonstrated that the invasive ability of CaSki cells was suppressed by an MMP inhibitor, and decorin was released from CRL4003 cells. These data suggested that decorin prevented the invasion of malignant cells in uterine cervical cancer; however, MMP9 promotes cell invasion by destroying decorin.
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PMID:Association of matrix metalloproteinase-9 and decorin expression with the infiltration of cervical cancer. 3065 99


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