23 research outputs found

    Agricultural Academy

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    Pulmonary alveolar proteinosis (PAP) is a heterogenous disorder of genetic or acquired etiologies characterized by intraalveolar accumulation of lipoproteinaceous material. The clinical course of the disease is variable, ranging from spontaneous remission to respiratory failure. The aim of the present study was to compare the biochemical and biophysical characteristics of broncho-alveolar lavage (BAL) from a patient with PAP, during the whole lung lavage (WLL) taken after each stage of the procedure. For this purpose biochemical and biophysical analysis of the clinical samples were made. The phospholipids (PLs) and the proteins concentrations of the samples were measured. For determination of protein content in broncho-alveolar lavage samples Lowry protein assay (Peterson's modifi cation) was used. The PL's concentration was determined via extraction by the method of Blight and Dyer. Thin-layer chromatography was used for determining the phospholipid profi le of the separate phospholipid components. In addition, by using the method of Axisymmetric Drop Shape Analysis, the surface characteristics: equilibrium, maximal and minimal surface tension during 10 cycles of compression-decompression in the dynamic conditions, were determined. Our results showed consecutive proteins and phospholipids content decrease during the procedure. Logically, the equilibrium surface tension was increased as a result of the decreased Phospholipids/Proteins ratio. After WLL the physiological condition of the patient was improved. The present study will be of great interest for effective implementation of the procedure of whole lung lavage in the clinical practice

    INACTIVATION OF PULMONARY SURFACTANT BY LYSOPHOSPHATIDYLCHOLINE

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    ABSTRACT The aim of the study is to examine the influence of the lysophosphatidylcholine (lysoPC

    Molecular mobility in the monolayers of foam films stabilized by porcine lung surfactant.

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    Certain physical properties of a range of foam film types that are believed to exist in vivo in the lung have been investigated. The contribution of different lung surfactant components found in porcine lung surfactant to molecular surface diffusion in the plane of foam films has been investigated for the first time. The influence of the type and thickness of black foam films, temperature, electrolyte concentration, and extract composition on surface diffusion has been studied using the fluorescence recovery after photobleaching technique. Fluorescent phospholipid probe molecules in foam films stabilized by porcine lung surfactant samples or their hydrophobic extracts consisting of surfactant lipids and hydrophobic lung surfactant proteins, SP-B and SP-C, exhibited more rapid diffusion than observed in films of its principal lipid component alone, L-alpha-phosphatidylcholine dipalmitoyl. This effect appears to be due to contributions from minor lipid components present in the total surfactant lipid extracts. The minor lipid components influence the surface diffusion in foam films both by their negative charge and by lowering the phase transition temperature of lung surfactant samples. In contrast, the presence of high concentrations of the hydrophillic surfactant protein A (SP-A) and non-lung-surfactant proteins in the sample reduced the diffusion coefficient (D) of the lipid analog in the adsorbed layer of the films. Hysteresis behavior of D was observed during temperature cycling, with the cooling curve lying above the heating curve. However, in cases where some surface molecular aggregation and surface heterogeneity were observed during cooling, the films became more rigid and molecules at the interfaces became immobilized. The thickness, size, capillary pressure, configuration, and composition of foam films of lung surfactant prepared in vitro support their investigation as realistic structural analogs of the surface films that exist in vivo in the lung. Compared to other models currently in use, foam films provide new opportunities for studying the properties and function of physiologically important alveolar surface films
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