ABSTRACT
Myasthenia gravis (MG) is characterized clinically by skeletal muscle fatigue following the excessive exercise. Interestingly most of MG patients manifest parallely also some abnormalities of the thymus.AMP-deaminase (AMPD) from human thymus was not a subject of studies up to now. In this paper, mRNA expression and some physico-chemical and immunological properties of AMPD purified from the thymus of MG patients were described. Experiments performed identified the liver isozyme (AMPD2) as the main isoform of AMPD expressed in this organ. The activity of AMPD found in this organ was higher than in other human non-(skeletal) muscle tissues indicating on role the enzyme may play in supplying of guanylates required for the intensive multiplication of thymocytes.
Subject(s)
AMP Deaminase/metabolism , Myasthenia Gravis/enzymology , Thymus Gland/enzymology , AMP Deaminase/genetics , Adult , Aged , Enzyme Activation , Female , Gene Expression , Humans , Male , Middle Aged , Myasthenia Gravis/genetics , Myasthenia Gravis/pathology , Thymus Gland/pathologyABSTRACT
In the present paper physico-chemical properties of AMP-deaminase purified from human liver neoplasm-hepatocellular carcinoma (HCC) were investigated and compared with these obtained for the enzyme from normal, unaffected tissue.
Subject(s)
AMP Deaminase/chemistry , Carcinoma, Hepatocellular/enzymology , Liver Neoplasms/enzymology , AMP Deaminase/immunology , Adenosine Monophosphate/chemistry , Catalysis , Electrophoresis, Polyacrylamide Gel , Humans , Hydrogen-Ion Concentration , Kinetics , Liver/pathology , Necrosis/pathology , Proteins/chemistryABSTRACT
AMP-deaminase from human liver was purified by two-step phosphocellulose chromatography, and SDS-PAG electrophoresis of the most active enzyme fraction eluted has been performed. The largest of the protein fragments revealed had a size (92 kDa) of an apparent full-size enzyme subunit, and reacted positively with antibodies produced against specific human ampd2 gene product. Three-day storage at cold room temperature modified significantly the electrophoretical pattern of the enzyme, evidencing continuous and progressive degradation of its structure. This is a first report evidencing the presence of apparent full-size form of human liver AMP-deaminase in preparation obtained from endogenous source.
Subject(s)
AMP Deaminase/chemistry , AMP Deaminase/isolation & purification , Liver/enzymology , Chromatography, Liquid , Electrophoresis, Polyacrylamide Gel , Humans , Isoenzymes/chemistry , Isoenzymes/isolation & purification , Molecular WeightABSTRACT
AMP-deaminase (EC 3.5.4.6) is a key enzyme of nucleotide breakdown involved in regulation of adenine nucleotide pool in the liver. Mechanisms regulating activity of the enzyme are not completely elucidated, till now. In this paper experimental data indicating on the potential regulatory significance of changes in oligomeric structure of the enzyme are presented. SDS-PAG electrophoresis of human liver AMP-deaminase revealed the presence of three enzyme fragments. Only largest of them (the protein fragments weighing 68 kDa) reacted immunologically with anti- (human liver) AMP-deaminase antibodies. At physiological pH 7.0, in the absence of regulatory ligands, reaction catalysed by human liver AMP-deaminase was strongly dependent on enzyme concentration used, with half-saturation constant (S0.5) values increasing significantly with the degree of enzyme dilution. Preincubation with activated long-chain fatty acids--substances promoting dissociation of oligomeric enzymes, inhibited the activity of AMP-deaminase studied nearly completely. Gel filtration on Sepharose CL-6B column demonstrated existence of at least three active oligomeric forms of human liver AMP-deaminase. We postulate that oligomeric structure of the enzyme is a factor determining regulatory profile of AMP-deaminase studied.
Subject(s)
AMP Deaminase/metabolism , Liver/enzymology , AMP Deaminase/chemistry , AMP Deaminase/isolation & purification , Blotting, Western , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Humans , MaleABSTRACT
The article presents current views on the possibility of the applying of the gene therapy for advanced heart failure treatment. The gene therapy which offers a completely new treatment of this disease, but it requires a lot of many further efforts in development of gene-transfer vectors, gene-delivery techniques and new target genes identification.
Subject(s)
Genetic Therapy/trends , Heart Failure/therapy , Apoptosis , Calcium/metabolism , Chronic Disease , Gene Transfer Techniques , Genetic Vectors , Heart Failure/physiopathology , Homeostasis , Humans , Myocardial Contraction , Myocardium/metabolism , Receptors, Adrenergic, beta/metabolismABSTRACT
The aim of the study was to assess the frequency and nature of headaches in patients with non-insulin dependent diabetes (NIDDM). The investigations included 154 patients with NIDDM, 90 females and 64 males aged between 30 to 65 years. Duration of diabetes varied from 6 months to 37 years. The control group comprised 106 persons. Of the 127 NIDDM patients complaining of headaches, 95 had migraine headaches and 32 tension-type headaches. In 50 patients the onset of migraine headaches occurred when the patients were afflicted with diabetes. In 45 patients migraine was diagnosed before they began to suffer from diabetes. In these patients the onset of diabetes significantly increased the average yearly number of headache days. In 21 patients tension-type headaches occurred in the course of diabetes. 11 patients had tension-type headaches before the onset of the disease. In these cases the onset of diabetes increased significantly the average yearly number of headache days. In the control group, migraine was diagnosed in 17 subjects and tension-type headaches in 28 subjects.