Visual Impairment in Hemodialyzed Patients-An IVIS Study.

Background and Objectives: The growing and aging population of hemodialysis patients has become increasingly disabled, with more complex comorbidities, and are older upon initiating dialysis. Visual impairment can adversely affect their quality of life and life satisfaction. Treatment evaluation should not only consider remission of the disease, but also the improvement of quality of life and life satisfaction. This is a single-center cross-sectional study. It was designed to evaluate visual impairment in hemodialyzed patients, its correlation with quality of life and life satisfaction, and its relationship to clinical outcomes in hemodialyzed patients. Materials and Methods: Seventy patients with chronic kidney disease undergoing hemodialysis and aged 18 years or older were recruited from a single Dialysis Unit. The Impact of Visual Impairment Scale (IVIS), WHOQOL-BREF, and Cantril Ladder questionnaires were utilized to assess both sociodemographic and clinical variables. Results: It was found that, among all assessed variables (i.e., sex, marital status, level of education, months on hemodialysis, history of kidney transplantation, Kt/V, URR, and UF), only age and central venous catheter placement were positively correlated with IVIS scores, while arteriovenous fistula and willingness to become a kidney transplant recipient were negatively correlated. Furthermore, a comparison between patients with moderate and severe visual impairment yielded supplemental data indicating that individuals whose dialysis access was through a dialysis catheter and those ineligible or unwilling to undergo transplantation suffered more often from severe visual impairment. This finding may be attributed to age. Conclusions: Older patients were predominantly observed to experience visual impairment. Patients intending to receive a kidney transplant and whose dialysis access was through an arteriovenous fistula were less prone to visual impairment, compared to those who may be ineligible or unwilling to receive transplantation and those with hemodialysis catheters. This phenomenon can be attributed to age-related distinctions in patients' suitability for specific dialysis access and transplantation. Those reporting visual impairment gave lower ratings in all four domains of their quality of life (comprising physical health, psychological health, social relationships, and environment) and in both present and anticipated five-year life satisfaction. More severe visual impairment was related to an additional reduction in physical health, social relationship, and environment domains, and in life satisfaction.

Characteristics of the Protoporphyrin IX Binding Sites on Human Serum Albumin Using Molecular Docking.

Human serum albumin (HSA) is the main plasma protein responsible for a distribution of drugs in the human circulatory system. The binding to HSA is one of the factors that determines both the pharmacological actions and the side effects of drugs. The derivative of heme, protoporphyrin IX (PpIX), is a hydrophobic photosensitizer widely used in photodynamic diagnosis and therapy of various malignant disorders. Using absorption and fluorescence spectroscopy, it has been demonstrated that PpIX forms complexes with HSA. Its binding sites in the tertiary structure of HSA were found in the subdomains IB and IIA. PpIX binds to HSA in one class of binding sites with the association constant of 1.68 × 105 M-1 and 2.30 × 105 M-1 for an excitation at wavelength λex = 280 nm and 295 nm, respectively. The binding interactions between HSA and PpIX have been studied by means of molecular docking simulation using the CLC Drug Discovery Workbench (CLC DDWB) computer program. PpIX creates a strong 'sandwich-type' complex between its highly conjugated porphine system and aromatic side chains of tryptophan and tyrosine. In summary, fluorescent studies on binding interactions between HSA and PpIX have been confirmed by the results of computer simulation.

Interactions of PCBs with human serum albumin: in vitro spectroscopic study.

Following absorption, polychlorinated biphenyls (PCBs) bind to albumin and are transported via blood into the target tissues. PCBs then accumulate in tissues and induce a variety of harmful chronic and developmental effects. The aim of the present study is to determine binding parameters, such as binding constant, quenching constant, and number of binding sites for three PCB congeners (PCB118, PCB126 and PCB153) in complex with human serum albumin (HSA). The binding parameters for the complexes of HSA-PCB118, HSA-PCB126, and HSA-PCB153 excited at 280 nm were compared with those excited at 295 nm. Quenching (static and dynamic) of HSA fluorescence was analyzed based on the Stern-Volmer method. Binding (Ka) constants were calculated according to the Scatchard method and analysis of non-linear regression was based on a two-component model with the Lavenberg-Marquardt algorithm. For all analyzed complexes, a single independent class of binding site for PCB congeners was found in HSA subdomain IIA. Tyrosine residues appear to play the most prominent role in binding of PCB126 to HSA, while tryptophan-214 played a dominant role in interactions of PCB153 with HSA. Among studied PCB congeners, PCB118 formed the most stable complexes with HSA. These results illustrate the importance of studies targeting the binding of PCBs to serum albumin as part of the strategy to understand and protect against toxicity of these environmental toxicants.

[Heat shock proteins in colorectal carcinoma]. / Bialka szoku termicznego a nowotwory jelita grubego.

Heat-shock proteins (HSP) are a group of proteins, whose production in induced as a intracellular response to different kinds of stresses. They are also included in the group of chaperones, which are involved in protein folding and repairing of denatured proteins in the cells. Because of the protective role of HSP on the cellular level, many studies are focused on the role of heat shock proteins in anti-carcinogenic effect. The present study is a review of the literature regarding the value of HSP in the carcinogenic process.

[Doctor Mikolaj Witczak's life and work]. / Zycie i dzialalnosc doktora Mikolaja Witczaka.

On the grounds of conducted research, the life and activities of Dr Mikolaj Witczak (1857-1918) have been reconstructed. The history of Jastrzebie Zdrój Spa has also been presented as one of the most remarkable European health resorts of the turn of the 19th century.