Regina Danielewicz

ORCID: 0000-0002-6990-9808
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Research Areas
  • S100 Proteins and Annexins
  • Advanced Glycation End Products research
  • Protein Hydrolysis and Bioactive Peptides
  • Protease and Inhibitor Mechanisms
  • Physiological and biochemical adaptations
  • Cardiac Ischemia and Reperfusion
  • Antimicrobial Peptides and Activities
  • Peptidase Inhibition and Analysis
  • Signaling Pathways in Disease
  • Electrochemical sensors and biosensors
  • Animal Nutrition and Physiology
  • Photoreceptor and optogenetics research
  • Cardiac Valve Diseases and Treatments
  • Biochemical effects in animals
  • Free Radicals and Antioxidants
  • Cancer Research and Treatments
  • Microfluidic and Capillary Electrophoresis Applications
  • Nanopore and Nanochannel Transport Studies
  • Cancer, Hypoxia, and Metabolism
  • Computational Drug Discovery Methods
  • Meat and Animal Product Quality
  • Erythrocyte Function and Pathophysiology
  • Lipid Membrane Structure and Behavior
  • Cardiac Arrest and Resuscitation

Wroclaw Medical University
1990-2021

Enolase, is a glycolytic enzyme ubiquitous in higher organisms, where it forms tissue specific dimers of isoforms, also found the cytoplasm fermentative bacteria. The aim this work was to identify enolase-like proteins cell wall some Gram-negative bacteria using antibodies against human β-enolase, an isoenzyme skeletal and heart muscles. Cell outer membrane protein (OMP) preparations were obtained from 9 strains Enterobacteriaceae one Pseudomonas aeruginosa. Specific enzymatic enolase...

10.1016/j.femsim.2005.01.005 article EN FEMS Immunology & Medical Microbiology 2005-02-05

Methylglyoxal (MG) was studied as an inhibitor and effective glycating factor of human muscle-specific enolase. The inhibition carried out by the use a preincubation procedure in absence substrate. Experiments were performed anionic cationic buffers showed that enolase methylglyoxal formation enolase-derived glycation products arose more effectively slight alkaline conditions presence inorganic phosphate. Incubation 15 micromolar solutions enzyme with 2 mM, 3.1 mM 4.34 MG 100 phosphate...

10.1080/14756360802187679 article EN Journal of Enzyme Inhibition and Medicinal Chemistry 2008-10-02

Matrix metalloproteinase 2 (MMP-2) is activated in hearts upon ischemia-reperfusion (IR) injury and cleaves sarcomeric proteins. It was shown that carvedilol nebivolol reduced the activity of different MMPs. Hence, we hypothesized they could reduce MMPs activation myocytes, therefore, protect against cardiac contractile dysfunction related with IR injury. Isolated rat were subjected to either control aerobic perfusion or injury: 25 min perfusion, followed by 20 global, no-flow ischemia,...

10.3390/ph14121276 article EN cc-by Pharmaceuticals 2021-12-07

Enolase - a glycolytic enzyme is also expressed on the surface of eukaryotic cells such as macrophages, neutrophils, endothelial, neuronal, tumor cells. Surface enolase plasminogen receptor plays an important role in myogenesis, tumorgenesis and angiogenesis. Determination localization cell lines may give rise to elucidation its function The cellular muscle-specific isoform normal rat cardiomyocytes (H9c2, embryonic heart-derived line) sarcoma (R1) line reported here. Immunocytochemical...

10.2478/v10042-008-0075-7 article EN cc-by-nc-nd Folia Histochemica et Cytobiologica 2009-01-14

Enolase is a conservative protein. Its cellular enzymatic activity catalyzes the conversion of 2-phospho-d-glycerate (2-PGA) to phosphoenolpyruvate (PEP) product in glycolysis pathway. This enzyme also has multifunctional nature participating several biological processes. work aims determine effect water polarization on catalytic enolase. The experiments have been set based concept that water, polar dielectric, may undergo phenomenon electric polarization, decreasing its configurational and...

10.1021/acsomega.0c05199 article EN cc-by-nc-nd ACS Omega 2021-02-01

Human α- and β-enolases are highly homologous enzymes, difficult to differentiate immunologically. In this work, we describe production, purification properties of anti-α- anti-β-enolase polyclonal antibodies. To raise antibodies, rabbits were injected with enolase isoenzymes that purified from human kidney (α-enolase) skeletal muscle (β-enolase). Selective antibodies obtained by affinity chromatography on either or β-enolase-Sepharose columns. On Western blots, directed against β-enolase,...

10.1016/j.bbrep.2018.05.008 article EN cc-by Biochemistry and Biophysics Reports 2018-06-17
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