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Stranica 1 iz 643 rezultatima
A thiol protease inhibitor released from cultured human malignant melanoma cells.
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A thiol protease inhibitor (TPI) was found in culture media of human malignant melanoma cells (Bowes) at 1.5 to 2.3 units/day/flask (full sheet, 75 sq cm). This amount well exceeded that for cultured nonmalignant cells (human fetal lung fibroblasts). In the intracellular region of the melanoma
Action of endogenous proteases on the distribution of tyrosinase isozymes in Harding-Passey mouse melanoma.
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A high percentage of the total tyrosinase found in Harding-Passey mouse melanoma occurs as a soluble form. This paper shows that melanosomal tyrosinase can be solubilized by several endogenous proteases to yield active tyrosinase. This enzyme, once proteolytically solubilized, can be further
Cysteine protease inhibitors isolated from human malignant melanoma tissue.
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Cysteine protease inhibitors that specifically reacted with several cysteine proteases were found in KSCN extract of human melanoma tissue. From 30 gm of the tissue, approximately 593.5 U inhibitor was obtained. The inhibitors were adsorbed on a papain-Sepharose column and could be eluted with 10
Proteases in cutaneous melanoma.
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From a great number of studies there is clear evidence that several extracellular proteolytic enzymes play an important role in various tumour-related processes. This review focusses on proteases in cutaneous melanoma. The current knowledge on and insights into the involvement of proteases in tumour
Protease-activated receptor-1 (PAR-1) promotes the motility of human melanomas and is associated to their metastatic phenotype.
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Protease-activated receptor-1 (PAR-1) is a unique G-protein-coupled receptor belonging to the protease-activated receptor family. Its activation leads to downstream signaling events that launch a variety of cellular responses related to tumor progression. PAR-1 expression has been associated to a
Molecular basis of complement resistance of human melanoma cells expressing the C3-cleaving membrane protease p65.
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The molecular mechanism of complement resistance of the human SK-MEL-170 melanoma cell line was investigated. The cells have been shown to express the C3b-cleaving membrane protease p65. To delineate the molecular consequences of the C3b-cleaving activity for the complement cytotoxicity, the
Up-regulation of Flotillin-2 is associated with melanoma progression and modulates expression of the thrombin receptor protease activated receptor 1.
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Flotillin 2 (flot-2) is a highly conserved protein isolated from caveolae/lipid raft domains that tether growth factor receptors linked to signal transduction pathways. Flot-2 protein and mRNA were increased in tumorigenic and metastatic melanoma cell lines in vitro, and the immunostaining intensity
Apoptosis protease activator protein-1 expression is dispensable for response of human melanoma cells to distinct proapoptotic agents.
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Loss of expression of the apoptosis protease activator protein-1 (APAF-1) in human melanoma is thought to promote resistance to programmed cell death by preventing caspase-9 activation. However, the role of the APAF-1-dependent pathway in apoptosis activated by cellular stress and/or DNA damage has
The field bean protease inhibitor has the potential to suppress B16F10 melanoma cell lung metastasis in mice.
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Metastasis is a characteristic and fatal feature of human malignancies. Its regulation is therefore of the utmost significance to clinicians. The present study was undertaken to determine whether a legume-derived protease inhibitor (PI) of trypsin/chymotrypsin, the field bean PI (FBPI), also has
Protease-Activated Receptors and other G-Protein-Coupled Receptors: the Melanoma Connection.
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The vast array of G-protein-coupled receptors (GPCRs) play crucial roles in both physiological and pathological processes, including vision, coagulation, inflammation, autophagy, and cell proliferation. GPCRs also affect processes that augment cell proliferation and metastases in many cancers
Proteases in cutaneous malignant melanoma: relevance as biomarker and therapeutic target.
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Cutaneous malignant melanoma is the most aggressive skin cancer. It is also the most rapidly spreading cancer in terms of worldwide incidence. Although it is detected by simple inspection and can be relatively easily removed or treated, differential diagnosis to other melanocytic lesions, lack of
Clinical significance of serum Protease-Activated Receptor-1 (PAR-1) levels in patients with cutaneous melanoma.
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BACKGROUND
Protease-Activated Receptor-1 (PAR-1) plays an important role in the pathogenesis of multiple malignancies and its expression strongly also affects the outcomes of cancer patients. The objective of this study was to determine the clinical significance of the serum levels of PAR-1in
Differences in induction of lysosomal protease activity by protease inhibitors in B16 melanoma cell lines.
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1. The effects of potent protease inhibitors in vitro (leupeptin, pepstatin and E-64[N-[L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl]agmatine]) on intracellular cathepsin B (EC 3.4.22.1), hemoglobin (Hb)-hydrolase and acid phosphatase (EC 3.1.3.2) from cultured B16 melanoma variants (B16-F1, F10
Induction and inhibition of cathepsin B and hemoglobin-hydrolase activity in murine B16 melanoma by thiol protease inhibitors.
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The effects of potent thiol protease inhibitors in vitro (leupeptin, antipain, chymostatin and E-64 (N-[N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl]agmatine) on intracellular cathepsin B and hemoglobin (Hb)-hydrolase from cultured B16 melanoma cells were studied. E-64 induced cultured B16
Extracellular Protease ADAMTS1 Is Required at Early Stages of Human Uveal Melanoma Development by Inducing Stemness and Endothelial-Like Features on Tumor Cells.
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Extracellular matrix remodeling within the tumor microenvironment has been recognized as a relevant dynamic framework during tumor growth. However, research on proteases that trigger this remodeling keeps revealing a wide range of actions including both pro- and anti-tumorigenic. The extracellular
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