ABSTRACT
The paper is dedicated to clinical and laboratory aspects of Diabetes Mellitus non-immune forms, such as neonatal Diabetes Mellitus, Maturity Onset Diabetes of young (MODY), DIDMOAD-syndrome, Wolframe syndrome, Alstrom syndrome and its determinating genes. The analysis of proper clinical results are present in this paper.
Subject(s)
Diabetes Mellitus , Genetic Predisposition to Disease , Hypoglycemic Agents/therapeutic use , Insulin , Age of Onset , Aged , Diabetes Mellitus/classification , Diabetes Mellitus/drug therapy , Diabetes Mellitus/epidemiology , Diabetes Mellitus/genetics , Diabetes Mellitus/metabolism , Female , Genome-Wide Association Study , Genotyping Techniques , Glucokinase/genetics , Glucokinase/metabolism , HLA-DR Antigens/genetics , Humans , Infant, Newborn , Insulin/genetics , Insulin/metabolism , Insulin/therapeutic use , Insulin Secretion , Insulin-Secreting Cells/drug effects , Insulin-Secreting Cells/metabolism , Male , Mutation , Pedigree , Transcription Factors/genetics , Transcription Factors/metabolismSubject(s)
Antibody Formation , Hybridomas/immunology , Plant Preparations , Plant Proteins , Toxins, Biological/immunology , Asialoglycoproteins/metabolism , Binding Sites, Antibody , Cell Survival/drug effects , Fetuins , Mistletoe/metabolism , Plant Lectins , Plants, Medicinal , Ribosome Inactivating Proteins, Type 2 , Ricin/immunology , Toxins, Biological/metabolism , Toxins, Biological/toxicity , alpha-Fetoproteins/metabolismSubject(s)
Antibodies, Monoclonal/biosynthesis , Hybridomas/drug effects , Lectins/pharmacology , Plant Preparations , Plant Proteins , Toxins, Biological/pharmacology , Animals , Cell Survival/drug effects , Cells, Cultured , Hybridomas/cytology , Hybridomas/immunology , Lectins/chemistry , Mice , Mice, Inbred BALB C , Radioligand Assay , Ribosome Inactivating Proteins, Type 2 , Toxins, Biological/chemistryABSTRACT
A chimeric toxic protein was prepared from the mistletoe lectin I A-chain and ricin B-chain by using the disulfide exchange reaction. Ricin and chimeric protein were indistinguishable in binding to immobilized asialofetuin in ELISA. The chimeric protein was more toxic for Jurkat cells than native mistletoe lectin I, but not as effective as native ricin. In the presence of NH4Cl, which enhances the toxicity of some toxins and immunotoxins, but does not influence ricin toxicity, both ricin and chimeric toxin had equal cytotoxic activity. The possibility is discussed that the ricin B-chain protects the ricin A-chain from degradation during delivery from the cell surface to the place where it is translocated into the cytosol.
Subject(s)
Lectins/chemistry , Mistletoe/chemistry , Plant Preparations , Plant Proteins , Plants, Medicinal , Recombinant Fusion Proteins/chemical synthesis , Ricin/chemistry , Toxins, Biological/chemistry , Asialoglycoproteins/metabolism , Biological Transport , Cells, Cultured , Cytosol/metabolism , Enzyme-Linked Immunosorbent Assay , Fetuins , Plant Lectins , Recombinant Fusion Proteins/metabolism , Ribosome Inactivating Proteins, Type 2 , Ricin/metabolism , alpha-Fetoproteins/metabolismABSTRACT
The obtained murine mAb LT27 (IgG2a) assigned to the cluster of differentiation CD27 was used to study the distribution of antigen CD27 among human lymphocytes scbpopulations in normal state and immunopathology. In normal donors the antigen CD27 was found to be expressed most frequently on CD4+ cells (90 +/- 8% of which coexpressed antigen CD27) and to the lesser extent on- CD8+ cells (only 77 +/- 28% of CD8+ cells carried antigen CD27). 79 +/- 12% of double negative lymphocytes (CD3+CD4-CD8-) expressed antigen CD27. In patients with hypogammaglobulinemia the proportion of CD4+CD27+/CD4+ and CD8+CD27+/CD8+ was significantly reduced to 80 +/- 11% (p < 0.01) and 45 +/- 19% (p < 0.001), respectively. The ratio CD4+CD27+/CD4+ varied insignificantly with the increase of CD4+ population, but the increase of the CD8+ population was accompanied by the definite tendency to a decrease of the ratio CD8+CD27+/CD8+. The distribution of CD27 antigen inside CD4+ and CD8+ subpopulations was found to be different from the distribution of CD29 and CD45RA antigens.
Subject(s)
Antibodies, Monoclonal/immunology , Antigens, CD/immunology , Antigens, Differentiation, T-Lymphocyte/immunology , Receptors, Immunologic/immunology , T-Lymphocyte Subsets/immunology , Agammaglobulinemia/immunology , Animals , Antibodies, Monoclonal/isolation & purification , Antigens, CD/analysis , CD4-CD8 Ratio , Child , Humans , Hybridomas/immunology , Immunologic Deficiency Syndromes/immunology , Mice , Tumor Necrosis Factor Receptor Superfamily, Member 7ABSTRACT
The prolonged nonintensive physical activity by swimming without load (12 +/- 2 h.) has no effect on the overall amount of fast and slow transported proteins of transport velocity in rat central and peripheral sensory fibres of the sciatic nerve. However, the rate of fast axonal transport in the motor fibres decreases by 18% and the amount of proteins by a factor of 2 as compared with control. The rate of slow axonal transport does not change, but the mean level of transported labeled proteins decreases by 1.9 times. The relatively short-term but more intensive activity (swimming with the load during 60 +/- 10 min.) provokes an increase of the rate by 10% and the overall amount of fast transported proteins by 2 times. The rest of the animals during 6 h. returns the above parameters to control values. A suggestion is made that the rate and the amount of transported proteins depend on the variations in functional state of the neurons and their axons.
Subject(s)
Axonal Transport/physiology , Nerve Tissue Proteins/metabolism , Neurons/physiology , Physical Exertion/physiology , Sciatic Nerve/physiology , Animals , Carbon Radioisotopes , Male , Nerve Fibers/physiology , Rats , SwimmingABSTRACT
14C-glycin was microinjected into the ventral horns of the spinal cord or spinal ganglions. The rate of fast and slow axoplasmic transport of proteins in the axons of motor and sensory neurons was studied by liquid scintillation. Motor fibers of the sciatic nerve manifested a marked decrease (P less than 0.05) in the rate of slow axoplasmatic transport of the labeled protein from 5.25 +/- 0,31 in 2-week-old rats to 3.45 +/- +/- 0.23 mm/day in 4-week-old animals and a significant increase in the rate of fast axoplasmic transport (P less than 0.05) from 99 +/- 13.2 (2-week-old rats) up to 198 +/- 18.9 mm/day (in 4-week-old rats). The two-week-old rats had higher rates (4.5 +/- 0.3 mm/day) of slow axoplasmic transport of the labeled protein in the central and peripheral axons of sensory neurocytes and lower rates of fast axoplasmic transport (126 +/- 14.7 mm/day) as compared with 4-week-old animals (3.75--4.1 +/- 0.25 -- slow transport; 144 +/- 23.34 mm/day -- fast transport). However, the differences described are not significant.
