Κατερίνα Οικονομοπούλου

ORCID: 0000-0002-5497-4025
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About
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Research Areas
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Blood Coagulation and Thrombosis Mechanisms
  • Joseph Conrad and Literature
  • Classical Antiquity Studies
  • Peptidase Inhibition and Analysis
  • Protease and Inhibitor Mechanisms
  • Rheumatoid Arthritis Research and Therapies
  • Classical Philosophy and Thought
  • Spondyloarthritis Studies and Treatments
  • Autoimmune and Inflammatory Disorders Research
  • Complement system in diseases
  • Psoriasis: Treatment and Pathogenesis
  • Historical and Architectural Studies
  • Historical, Religious, and Philosophical Studies
  • Byzantine Studies and History
  • Adipose Tissue and Metabolism
  • Adipokines, Inflammation, and Metabolic Diseases
  • Connective Tissue Growth Factor Research
  • Monoclonal and Polyclonal Antibodies Research
  • Marine Sponges and Natural Products
  • Biblical Studies and Interpretation
  • Historical and Literary Studies
  • Historical and Linguistic Studies
  • Mast cells and histamine
  • Venous Thromboembolism Diagnosis and Management

University Health Network
2009-2024

Krembil Research Institute
2017-2024

Krembil Foundation
2022

University of Toronto
2004-2020

University of Patras
2020

Toronto Western Hospital
2016-2018

University of Calgary
2007-2016

Mount Sinai Hospital
2006-2016

Research Network (United States)
2016

Western University
2016

Serine proteinases like thrombin can signal to cells by the cleavage/activation of proteinase-activated receptors (PARs). Although is a recognized physiological activator PAR(1) and PAR(4), endogenous enzymes responsible for activating PAR(2) in settings other than gastrointestinal system, where trypsin activate PAR(2), are unknown. We tested hypothesis that human tissue kallikrein (hK) family regulates PAR signaling using following: 1) high pressure liquid chromatography (HPLC)-mass...

10.1074/jbc.m513138200 article EN cc-by Journal of Biological Chemistry 2006-08-03

We tested the hypothesis that human tissue kallikreins (hKs) may regulate signal transduction by cleaving and activating proteinase-activated receptors (PARs). found hK5, 6 14 cleaved PAR N-terminal peptide sequences representing cleavage/activation motifs of PAR1 PAR2 to yield receptor-activating peptides. activated calcium signalling in rat PAR2-expressing (but not background) KNRK cells. Calcium HEK cells co-expressing was also triggered hK14 (via PAR2) hK6 PAR2). In isolated platelets do...

10.1515/bc.2006.104 article EN Biological Chemistry 2006-01-01

Currently, there are no effective biomarkers for ovarian cancer prognosis or prediction of therapeutic response. The objective this study was to examine a panel 10 serum biochemical parameters their ability predict response chemotherapy, progression and survival patients. Sera from patients were collected prior during chemotherapy analysed by enzyme-linked immunosorbent assay CA125, kallikreins 5, 6, 7, 8, 11, B7-H4, regenerating protein IV Spondin-2. odds ratio hazard 95% confidence...

10.1038/sj.bjc.6604630 article EN cc-by-nc-sa British Journal of Cancer 2008-09-02

Abstract Emerging evidence indicates that serine proteases of the tissue kallikrein-related peptidases family ( KLK ) are implicated in tumorigenesis. We recently reported ectopic expression KLK4 and KLK14 colonic cancers their signaling to control cell proliferation. Human peptidase 7 (KLK7) is often dysregulated many cancers; however, its role colon tumorigenesis has not yet been established. In present study, we analyzed KLK7 15 cancer lines 38 human tumors. cells, mRNA was observed,...

10.1515/hsz-2014-0142 article EN Biological Chemistry 2014-08-06

Immunoassay measurements of human kallikrein-related peptidases (KLKs) such as prostate-specific antigen (KLK3) are great value diagnostic indices cancer. Despite extensive knowledge the abundance immunoreactive KLKs in normal and cancer-related settings, there is little information available about proportion KLK that represents active enzyme samples. Using KLK6 a prototype enzyme, we have developed an assay using serine proteinase-targeted activity-based probe coupled to antibody capture....

10.1515/bc.2008.086 article EN Biological Chemistry 2008-05-15
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