[The effect of chemotherapy on bone metabolism in patients with non-small cell lung cancer]. / Wplyw chemioterapii na metabolizm kostny u chorych na niedrobnokomórkowego raka pluca.

UNLABELLED: In this study the influence of chemotherapy on bone metabolism in patients with III stage of non-small cell lung cancer has been evaluated. 30 patients (men) in average age 57.1 years were enrolled to this trial. The trial carried out on 2 groups of patients: group A consisted of 30 patients with NSCLC, group B of 15 patients without neoplastic process. In all participants bone scintigraphy was done and the following biochemical markers were measured: osteocalcin concentration, alkaline phosphatase's bone fraction, twenty-four-hour calcium and hydroxyproline urine excretion. In patients after two courses of chemotherapy (mitomycin, cisplatin, vinblastine) statistically significant reduction of serum concentration of osteocalcin, alkaline phosphatase, also reduction of calcium and hydroxyproline urine excretion have been observed. Scintigraphic examination of bones showed statistically significant decrease in resorption of isotope (MDP 99mTc) in patients after chemotherapy (p < 0.05). CONCLUSIONS: The study shows positive influence of chemotherapy on bone metabolism in patients with NSCLC. Patients treated with chemotherapy have bone metastases less frequently.

[Meigs syndrome--diagnostic difficulties]. / Zespól meigsa--trudnosci diagnostyczne.

Meigs' syndrome in 68 years woman with pleural effusion and ovarian tumour was described. The cause of the pleural liquid in Meigs' syndrome is still not clear. New views on the pathogenesis and diagnostic methods of pleural liquids causes were presented.

[Long-term corticosteroid therapy as a risk factor of osteoporosis in patients with asthma and chronic bronchitis]. / Dlugotrawla kortykosteroidoterapia jako czynnik ryzyka wystapienia osteoporozy u chorych na astme i przewlekle zapalenie oskrzeli.

This work evaluates frequency of steroid induced osteoporosis according to kind of steroid drugs (systemic, inhaled), dose and duration of treatment. In group of 80 young patients with asthma and chronic bronchitis the following examinations have been used: biochemical markers of bone turnover, X-ray of thoracic lumbar part of vertebral column and bone density in quantitative computed tomography of vertebrae L2-L4. Osteoporosis appeared in patients chronically treated with systemic steroids (prednisone) and in patients treated with inhaled steroids in typical dose as well. Usefulness of biochemical markers of bone turnover in connection with quantitative computed tomography in diagnostic of steroid induced osteoporosis has been confirmed.

Aspartic proteinase from Penicillium camemberti: purification, properties, and substrate specificity.

An acid proteinase from the culture filtrate of Penicillium camemberti was isolated in a two-step purification procedure by cation exchange chromatography and gel filtration. The enzyme is an aspartic proteinase inhibited by pepstatin, DAN, and EPNP, with a molecular mass determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of 33.5 kDa. The optimum activity for hydrolysis of denatured hemoglobin is around pH 3.4. The enzyme is highly specific for the aromatic and hydrophobic amino acid residue in insulin B-chain and, like pepsin, selectively splits only one Leu7-Met8 peptide bond in the squash trypsin inhibitor CMTI 1. The hydrolyzed bond can be resynthesized by P. camemberti proteinase at neutral pH.

[Sudden death in the course of sarcoidosis of the heart]. / Nagly zgon w przebiegu sarkoidozy serca.

A case of 46-years old patient with morphological diagnosis of hilar lymph nodes sarcoidosis is presented. Patient complained of mild degree of shortness of breath and easily fatigability. Chest X-ray examination showed enlargement of both hilar lymph nodes and slight increase in heart size. In electrocardiography (EKG)--left bundle branch block. It was diagnosed first degree sarcoidosis without involvement of lungs. It was beginning the steroid treatment because of suspicion of sarcoidosis of heart. Patient died suddenly in 17 day of treatment. Post mortem examination proved sarcoidosis of heart. In spite of cardiac involvement in sarcoidosis only a few patients have cardiac symptoms or signs.

An aspartic proteinase from Fusarium moniliforme. Purification and general properties.

An acid proteinase from the culture filtrate of Fusarium moniliforme was purified by acetone precipitation, gel filtration and ion-exchange chromatography. The final enzyme preparation was homogeneous on polyacrylamide gel electrophoresis. The apparent molecular weight was estimated to be 38 000, based on sodium dodecyl sulfate gel electrophoresis and an isoelectric point of pH 4.90. The optimum pH was found to be 3.2 when measured with denatured hemoglobin as substrate. The enzyme showed maximum stability in the pH range 3.0-5.5. Pepstatin, 1,2-epoxy-3-(p-nitrophenoxy)propane and diazoacetyl-DL-norleucine methyl ester strongly inhibited the proteinase activity, whereas thiol reagents, serine-type proteinase inhibitors and metal-chelating reagent had no significant effect. The data indicate that the proteinase from F. moniliforme is an aspartic proteinase which possesses milk-clotting activity.

Aspartyl proteinase from cucumber (Cucumis sativus) seeds. Preparation and characteristics.

Aspartyl proteinase (EC 3.4.23) from cucumber seeds was purified by ammonium sulphate fractionation, chromatography on immobilized pepstatin and gel filtration on Sephacryl S-200. The preparation obtained, homogeneous on polyacrylamide-gel electrophoresis in acidic and alkaline media, has a molecular mass of 42,000, pI of 5.2, and shows the highest activity with denatured haemoglobin at pH 3.2. The proteinase is stable in slightly alkaline medium, whereas it is inactivated in acidic medium, especially in the presence of NaCl. The enzyme activity is affected neither by the inhibitors of serine proteinases, sulfhydryl-proteinases and metalloproteinases, nor by divalent metal ions, whereas the enzyme is inactivated by the inhibitors of aspartyl proteinases: 1,2,3-epoxy(p-nitrophenoxy)propane, diazoacetyl-DL-norleucine and pepstatin.

Specificity of acid protease from Fusarium moniliforme.

Specificity of acid protease from Fusarium moniliforme was investigated using beta chain of oxidized insulin. The enzyme is highly specific for the bonds involving aromatic and hydrophobic amino acid residues. It shows high affinity for the following bonds: Leu(15)-Tyr(16), Tyr(16)-Leu(17), Phe(24)-Phe(25), Phe(25)-Tyr(26), and somewhat lower for other three bonds: His(10)-Leu(11), Leu(11)-Val(12) and Tyr(26)-Thr(27) in oxidized beta chain of insulin.

Rat interferons. Homologous and heterologus rat serum activity.

Serum proteins from normal rat serum and induced with Sindbis virus were separated on Sephadex G-100. Interferon activity was studied in a system of homologous REC and heterologous LG cells. Proteins of normal serum as well as induced serum emerged in two peaks separated by a deep saddle. Four hours after induction, the serum gave two peaks with similar interferon activity in both cell systems. After 8-hour induction, two interferons were also obtained, but activity in the heterologous system was much lower than in the homologous system. Electrophoresis in polyacrylamide gel and on paper showed that interferon activity is connected mainly with the alpha1-globulin fraction.

Proteins in mouse embryonic cell (MEC) culture fluids following interferon induction.

A study was made on the proteins and interferon activity in supernatant culture fluids from mouse fibroblast cultures induced with Newcastle disease virus, and in controls. The studied materials showed low protein content, the concentration of proteins depending on the length of time from induction to their collection. Proteins from induced and control cultures were separated on CM-Sephadex C-50 and by electrophoresis in polyacrylamide gel. No difference was found in the character of proteins from control materials and from materials induced 24 hours after infection; the elution profile was the same, and the distribution of electrophoretic fractions was similar. Interferon activity was not accompanied by the appearance of a new protein fraction. However, 5--10 hours after induction differences were noted in electrophoretic mobility and a marked reduction in the number of protein fractions occurred in control and stimulated culture fluids.