Diagnostic value of white blood cell parameters for COVID-19: Is there a role for HFLC and IG?

Introduction: As the Coronavirus disease 2019 (COVID-19) pandemic is still ongoing with patients overwhelming healthcare facilities, we aimed to investigate the ability of white blood cell count (WBC) and their subsets, high fluorescence lymphocyte cells (HFLC), immature granulocyte count (IG), and C-reactive protein (CRP) to aid diagnosis of COVID-19 during the triage process and as indicators of disease progression to serious and critical condition.

Methods: We collected clinical and laboratory data of patients, suspected COVID-19 cases, admitted at the emergency department of University General Hospital of Ioannina (Ioannina, Greece). We selected 197 negative and 368 positive cases, confirmed by polymerase chain reaction test for severe acute respiratory syndrome coronavirus 2.

Drosophila oogenesis as a bio-marker responding to EMF sources.

The model biological organisms Drosophila melanogaster and Drosophila virilis have been utilized to assess effects on apoptotic cell death of follicles during oogenesis and reproductive capacity (fecundity) decline. A total of 280 different experiments were performed using newly emerged flies exposed for short time daily for 3-7 d to various EMF sources including: GSM 900/1800 MHz mobile phone, 1880-1900 MHz DECT wireless base, DECT wireless handset, mobile phone-DECT handset combination, 2.44 GHz wireless network (Wi-Fi), 2.

1H NMR study of the enantioselective binding of lambda- and delta-[Ru(bpy)2(m-bpy-GHK)]Cl2 to the deoxynucleotide duplex d(5'-C1G2C3G4A5A6T7T8C9G10C11G12-3')2.

The interaction of the diastereomeric complexes Lambda- and Delta - [Ru(bpy)(2)(m - GHK)]Cl(2), (GHK = glycine-histidine-lysine) to the deoxynucleotide duplex d(5'-CGCGAATTCGCG-3')(2) was studied by means of (1)H NMR spectroscopy. The diastereomers interact with the oligonucleotide duplex differently. The Delta - [Ru(bpy)(2) (m - GHK)]Cl(2) is characterized by major groove binding close to the central part of the oligonucleotide, with both the peptide and the bipyridine ligand of the complex involved in the binding.

Interaction of Cu(II)with His-Val-Gly-Asp and of Zn(II) with His-Val-His, two peptides at the active site of Cu,Zn-superoxide dismutase.

His-Val-His and His-Val-Gly-Asp are two naturally occurring peptide sequences, present at the active site of Cu,Zn-superoxide dismutase (Cu,Zn-SOD). We have already studied the interaction of His-Val-His=A (copper binding site) with Cu(II) and of His-Val-Gly-Asp=B (zinc binding site) with Zn(II). As a continuation of this work and for comparison purposes we have also studied the interaction of Zn(II) with His-Val-His and Cu(II) with His-Val-Gly-Asp using both potentiometric and spectroscopic methods (visible, EPR, NMR).