ABSTRACT
The authors investigated the dependence of increasing serum oncomarkers CEA, Cyfra-21, NSE, TU M2-PK on survival in 739 patients with nonsmall cell lung cancer. The tests for the determination of the content of CEA, Cyfra-21, NSE in blood serum have low sensitivity and are of little use for the diagnosis of lung cancer. The tests because of their simplicity and low cost can be used for the detection of groups of patients with preliminarily diagnosed nonsmall cell lung cancer needing additional methods of examination for more exact staging of the disease and exclusion of remote metastases and more active using adjuvant method of treatment. The use of tumor pyruvate kinase can be perspective for clinical oncopulmonology. However, due to its low specificity, further experiences are required for using this oncomarker in the group of patients with nonsmall cell lung cancer.
Subject(s)
Antigens, Neoplasm/blood , Biomarkers, Tumor/blood , Carcinoembryonic Antigen/blood , Carcinoma, Non-Small-Cell Lung/blood , Keratin-19/blood , Lung Neoplasms/blood , Phosphopyruvate Hydratase/blood , Pyruvate Kinase/blood , Adult , Aged , Aged, 80 and over , Carcinoma, Non-Small-Cell Lung/pathology , Carcinoma, Non-Small-Cell Lung/surgery , Diagnosis, Differential , Female , Follow-Up Studies , Humans , Immunoenzyme Techniques , Immunoradiometric Assay , Luminescent Measurements , Lung Neoplasms/pathology , Lung Neoplasms/surgery , Male , Middle Aged , Neoplasm Staging , PrognosisABSTRACT
The paper deals with a description of a procedure of immunoradiometric assay of glutathione S-transferase pi in blood serum. A significantly increased level of said enzyme of more than 9.85 ng/ml in 75% of patients with different cancers of the lung has been established, as compared with non-tumor pathologies. These findings point to the feasibility of application of this enzyme in lung cancer diagnose.
Subject(s)
Biomarkers, Tumor/blood , Glutathione Transferase/blood , Lung Neoplasms/diagnosis , Diagnosis, Differential , Humans , Lung Diseases/diagnosis , Lung Neoplasms/enzymology , Predictive Value of TestsSubject(s)
Lasers , Skin/radiation effects , Animals , Histidine Ammonia-Lyase/metabolism , Histidine Ammonia-Lyase/radiation effects , Lipid Peroxides/metabolism , Lipid Peroxides/radiation effects , Mice , Photochemotherapy , Quaternary Ammonium Compounds/pharmacology , Skin/drug effects , Skin/metabolismSubject(s)
Insecticides/toxicity , Liver/drug effects , Organophosphorus Compounds , Skin Absorption/drug effects , Skin/drug effects , Animals , Dose-Response Relationship, Drug , Histidine Ammonia-Lyase/analysis , Liver/enzymology , Rats , Skin/enzymology , Time Factors , Urocanate Hydratase/bloodSubject(s)
Imidazoles/analysis , Laser Therapy , Photochemotherapy , Skin Diseases/drug therapy , Skin/analysis , Urocanic Acid/analysis , Adolescent , Adult , Aged , Child , Child, Preschool , Female , Humans , Male , Middle AgedSubject(s)
Imidazoles/therapeutic use , Pruritus/drug therapy , Scabies/drug therapy , Urocanic Acid/therapeutic use , Child , Female , Humans , Male , Skin/drug effectsABSTRACT
A dependence of activity of histidase from rat liver and skin on the agents affecting the activity of the adenylate cyclase systeme was studied in vitro. Under conditions optimal for the activity of liver phosphorylase protein kinase the skin extract histidase was activated 2-3-fold. This is indicative of a possibility of regulation of the skin histidase activity via the adenylate cyclase system by modification of enzyme by phosphorylation-dephosphorylation, which is performed by 3':5'-AMP-dependent protein kinase. Theophylline at concentrations of 10(-4) M and 10(-3) M activates partially purified histidase (both liver and skin forms), probably in the course of direct interaction with the enzyme.
Subject(s)
Ammonia-Lyases/metabolism , Cyclic AMP/physiology , Histidine Ammonia-Lyase/metabolism , Liver/enzymology , Skin/enzymology , Adenylyl Cyclases/metabolism , Animals , Cyclic AMP/pharmacology , Enzyme Activation , Osmolar Concentration , Phosphorylase Kinase/metabolism , Rats , Theophylline/pharmacologyABSTRACT
In rat skin the histidase activity was observed 2--3 days before delivery; it was increased at the first days of postnatal development, achieving a maximal level at the 5th day and then it was decreased (within 2--3 weeks of postnatal development) to the level activity, which was found in adult animals. Concentration of urocaninic acid in skin correlated with the histidase activity. Content of urocaninic acid in skin and the histidase activity were altered under effect of administration of cylic-3',5'-AMP, dibutyryl cyclic-3',5'-AMP, glucagon, sodium fluoride, theophylline, actinomycin D and cycloheximide.
Subject(s)
Ammonia-Lyases/metabolism , Cyclic AMP/physiology , Histidine Ammonia-Lyase/metabolism , Skin/enzymology , Age Factors , Animals , Animals, Newborn/metabolism , Dactinomycin/pharmacology , Embryo, Mammalian/enzymology , Enzyme Activation/drug effects , Female , Glucagon/pharmacology , Pregnancy , Rabbits , Rats , Sodium Chloride/pharmacology , Sodium Fluoride/pharmacology , Theophylline/pharmacology , Urocanic Acid/biosynthesisABSTRACT
A dependence of rat liver urocaninase activity on the agents affecting the adenylate cyclase system was studied in vitro and in vivo. Urocaninase is considerably activated after the injection of glucagone, NaF, theophylline and 3',5'-AMP. Under conditions optimal for the protein kinase activity of phosphorylase the urocaninase of liver extracts was activated 7-fold on the average. The nezyme retains its activity after gel-filtration through Sephadex G-25 and is capable of inactivation in the presence of Mg2+ and of reactivation after addition of ATP and 3',5'-AMP. These data suggest a possibility of regulation of mammalian liver urocaninase activity by 3',5'-AMP-dependent phosphorylation of the enzyme. Derivatives of hypoxanthine (theophylline and caffeine) in concentration 10(-4) M activate urocaninase in liver extracts 2--3 and 1.5-fold respectively. The activation is probably not due to the 3',5'-AMP phosphodiesterase inhibition, since another phosphodiesterase inhibitor--papaverine--has no activating effect on urocaninase.
