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gelatinase/sarcome
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Regulation of gelatinase production and invasiveness by organ-specific fibroblasts in high- and low-metastatic clones from murine RCT sarcoma.
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Regulation of gelatinase production, invasiveness and migration activity by organ-specific fibroblasts from embryo, subcutaneous and lung tissues of mice were investigated in high-metastatic RCT+ and low-metastatic RCT- clones established from a poorly differentiated murine sarcoma. In the
Gelatinase and inhibitor expression in soft tissue sarcomas: lack of correlation with distant metastasis.
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The predominant mode of death for most patients with soft tissue sarcomas (STS) remains distant metastasis (DM). Current clinical predictors of DM are unreliable. Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) correlate with biologic aggression in other tumors.
Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts.
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Chicken embryo fibroblasts (CEF) transformed by Rous sarcoma virus (RSVCEF) secrete a 70-kDa metallo-gelatinase at elevated levels over that of normal CEF. The 70-kDa enzyme has been purified from RSVCEF conditioned medium and represents 1-3% of the total protein in the RSVCEF conditioned medium. A
Augmentation of metalloproteinase (gelatinase) activity secreted from Rous sarcoma virus-infected cells correlates with transforming activity of src.
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To search for the biochemical properties of cells relevant to transformation by p60v-src, we examined the activities and amounts of metalloproteinase (gelatinase) released from chicken embryonic fibroblasts infected with various mutants of Rous sarcoma virus by zymography and immunoblotting. While
Significance of serum type IV collagenolytic activities and gelatinase levels for detection of metastasis in murine RCT sarcoma.
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We investigated the usefulness of serum type IV collagenolytic activities and gelatinase levels as diagnostic markers of metastasis in the animal model of spontaneous lung metastasis by FITC-labeled type IV collagen degradation assay and zymographic analyses. High-metastatic RCT(+) and
Cloning of a 72 kDa matrix metalloproteinase (gelatinase) from chicken embryo fibroblasts using gene family PCR: expression of the gelatinase increases upon malignant transformation.
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Chicken embryo fibroblasts secrete a 72 kDa progelatinase that displays all of the characteristics of a matrix metalloproteinase. Employing reverse-transcription PCR and degenerate oligonucleotide primers that are specific for two highly conserved sequences found in all matrix metalloproteinases, a
Mechanisms of kaposis-sarcoma cell supernatant-induced vascular cell invasion.
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Kaposi's sarcoma (KS) is a highly angiogenic lesion frequently associated with acquired immune deficiency syndrome. Histologically the lesions appear to contain proliferative 'spindle shaped' cells with a mixed smooth muscle-endothelial-fibroblastic histotype and a conspicuous neovascularization,
The role of angiocidin in sarcomas.
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BACKGROUND
Angiocidin, first identified as a tumor-associated thrombospondin-1 (TSP-1) receptor, is a key mediator of tumor progression. TSP-1, an extracellular protein produced by stromal cells, up-regulates gelatinases and tumor cell invasion in epithelial malignancies. The authors recently
Enzymatic processing of collagen IV by MMP-2 (gelatinase A) affects neutrophil migration and it is modulated by extracatalytic domains.
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Proteolytic degradation of basement membrane influences the cell behavior during important processes, such as inflammations, tumorigenesis, angiogenesis, and allergic diseases. In this study, we have investigated the action of gelatinase A (MMP-2) on collagen IV, the major constituent of the
Expression of multiple matrix metalloproteinases and urokinase type plasminogen activator in cultured Kaposi sarcoma cells.
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Kaposi's sarcoma (KS) cells are considered to be of endothelial origin. KS lesions are characterized by hyperproliferation and an invasive phenotype. We have determined that KS cell cultures constitutively secrete multiple forms of several matrix metalloproteinases (MMPs) and an altered form of
Inhibition of matrix metalloproteinase 9 expression by a ribozyme blocks metastasis in a rat sarcoma model system.
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Matrix metalloproteinases (MMPs) have been implicated in tumor progression, but the exact roles that each member of this family may play in contributing to the behavior of malignant tumors are only beginning to be understood. MMP-9 (gelatinase B or the 92-kDa gelatinase/type IV collagenase)
Local activity of matrix metalloproteinases in a case of botryoid sarcoma.
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The aim of the study was to assess the activities of the collagenases type IV (matrix metalloproteinase type 2 [MMP-2] and matrix metalloproteinase type 9 [MMP-9]), also known as gelatinases, and the local activity of interstitial collagenase (matrix metalloproteinase type I[MMP-1]) in tissue
Resolution of TIMP-free and TIMP-complexed 70kDa progelatinase from culture medium of Rous sarcoma virus-transformed chicken embryo fibroblasts.
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Chicken embryo fibroblasts (CEF) produce a 70kDa progelatinase, a member of the matrix metalloproteinase family, and secrete elevated levels of the enzyme upon transformation by Rous sarcoma virus (RSV). This enzyme can be purified by affinity chromatography complexed with a 21kDa tissue inhibitor
Tissue and serum loss of metalloproteinase inhibitors in high grade soft tissue sarcomas.
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The activity of matrix metalloproteinases (MMPs) in degrading extracellular matrix is controlled by activation of pro-enzymes and inhibition of MMP tissue inhibitors (TIMPs). To assess proteolytic cascade imbalance in malignancy progression, the enzymatic activity of MMP2 and MMP9 and the expression
Matrix metalloproteinases in the progression and regression of Kaposi's sarcoma.
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BACKGROUND
Matrix metalloproteinases (MMPs) are associated with Kaposi's sarcoma (KS) tumorigenesis. To date, only a few MMPs have been studied in KS lesions. Their role in KS regression has not been investigated. The aim of this study was to evaluate the expression of multiple MMPs in developing
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