Papillon lefevre A rare syndrome

Papillon lefevre syndrome (PLS) belongs to a heterogeneous group of skin diseases that are characterized by hyperkeratosis of palms and soles and presence of severe and early onset periodontitis. Genetic studies have shown that mutation in the major gene locus of chromosome 11q14 with the loss of function of cathepsin C (CTSC) gene is responsible for PLS. Loss of CTSC function is responsible for the severe periodontal destruction seen clinically. This report represents classical signs and symptoms of PLS in a 6 year old girl.

Electrophoretic analysis of polypeptides and glycopeptides of erythrocyte membrane sampled from rats simulating mild insulin dependent diabetes mellitus.

In order to understand the molecular mechanism of reduced life span of diabetic erythrocyte, polypeptides and glycopeptides were analyzed by disc gel preparative sodium dodecyl sulphate polyacrylamide gel electrophoresis. An additional glycopeptide (244.5 kDa) and two additional polypeptides (39.81 and 144.5 kDa) were observed on glycopeptide and polypeptide gel profiles of mild insulin dependent diabetes mellitus (mIDDM) sample as compared to control. On the basis of molecular weight, their position on gel profile and their widely accepted nomenclature they were termed as glycosylated-ankyrin, membrane accreted glyceraldehyde-3-phosphate dehydrogenease (G 3-PD) and stress induced band 2.3 peptide. Earlier we have reported an increase in heterogeneity associated with increase in the population of aged fragile cells having altered membrane bound cation dependent ATPases, cytosolic dehydrogenase and hexokinase activities of mIDDM simulating rat erythrocyte sample. Significance of above observation in view of our earlier observation is discussed to explain the molecular mechanism of reduced life span of diabetic erythrocytes.

Activation of hexokinase by mild insulin dependent diabetes mellitus in rat erythrocytes.

In order to reveal sequel of events responsible for increase in red cell cytosolic glucose-6 phosphate (G-6P) content of diabetic patients the enzyme producing and transforming G-6P were assayed. Increase in the activity of hexokinase and decrease in phosphoglucoisomerase activity was observed in mild insulin dependent diabetes mellitus (mIDDM) rat erythrocytes. Increase and decrease in activity of hexokinase and phosphoglucoisomerase respectively will increase the cytosolic glucose-6 phosphate content. Thus any substance which autoregulate the activity of hexokinase and maintains critical level of G-6P necessary for generation of ATP and coenzymes (NADPH & NAD+) in the prevailing hyperglycemic state can be a potential therapeutic agent for diabetic patients.

Effect of alloxan induced mild insulin dependent diabetes mellitus on rat erythrocyte cytosolic dehydrogenases.

In order to understand how the red cell of mild insulin dependent diabetes mellitus rat perform the normal physiological function and maintain integrity cytosolic dehydrogenases were assayed. Lactate dehydrogenase produces the cofactor for glycolytic enzymes while glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase produces the coenzymes for oxygen radical scavanging enzymes. Decrease in activity of cytosolic dehydrogenase renders diabetic erythrocyte population more susceptible to oxidant stress.

Insulin-mimetic effect of (-) epicatechin on osmotic fragility of human erythrocytes.

(-) Epicatechin, a benzopyran extracted from the bark of Pterocarpus marsupium, is reported to have insulin like activity. The present work is undertaken to study the effect of insulin on erythrocyte osmotic fragility (OF) and then to evaluate the insulin-like role of (-) epicatechin on human erythrocytes. Insulin exerts a protective effect on erythrocyte OF and shows a dose response which is similar to other typical insulin effects i.e. a maximum at 0.1 nM and a lower effect at higher and lower concentration. (-) Epicatechin (1 mM) also shows protective effect, similar to insulin, on the OF. Ouabain (1 mM) has completely abolished the insulin effect on OF, and failed to have any effect on the action of (-) epicatechin, showing that (-) epicatechin and insulin act by a different mechanism of action while eliciting their protective effects on red cell OF.

In vivo effects of acetaminophen on rat RBC and role of vitamin E.

Non-therapeutic toxic dose (250 mg/kg) of acetaminophen (paracetamol), in vivo to albino rats significantly decreased red cell reduced glutathione (GSH) content and activity of (Na+, K+)-ATPase enzyme, whereas osmotic fragility (O.F.) was increased. However, no change was observed in the activity of glutathione reductase (GR) after acetaminophen treatment, while acetaminophen plus vitamin E treated rats showed significant increase in GR activity. Supplementation of vitamin E to the drug treated rats effectively brought the GSH content, (Na+, K+)-ATPase activity and O.F. back to almost normal. The results suggest that acetaminophen toxic dose treatment induces metabolic and membranal alterations making red cells prone to hemolysis, while vitamin E which is an antioxidant shows its ameliorating role to these changes.

Regulation of red cell acetylcholinesterase activity in diabetes mellitus.

Despite the fact that the significance of red cell membrane acetylcholinesterase (AChE) is unknown, this enzyme of red cell assumes importance since many of its properties have been found to be similar to purified enzyme form of brain tissues. Our investigations on the effect of insulin-dependent diabetes mellitus on red cell AChE revealed that the activity of this enzyme is significantly decreased in diabetes. Insulin treatment restored the activity to the normal level. Solubilization of normal, diabetic and insulin treated diabetic red cell membranes with Triton X-100 (0.2% v/v) caused a general decline in AChE activity, however the per cent decline in activity of diabetic enzyme was lower as compared to normal and insulin treated conditions. From our results it is inferred that the decreased red cell AChE activity in diabetes is due to lesser number of active enzyme molecules and also due to altered membrane microenvironment.

Red cell phosphoglycerate kinase in insulin-dependent diabetes mellitus.

Red cell phosphoglycerate kinase (PGK) activity was determined in normal individuals and patients with, type I (insulin-dependent) diabetes and insulin treated diabetes. The PGK activity was significantly (P less than 0.001) elevated in diabetes, however it is restored to normalcy after insulin treatment (normal 282.54 +/- 9.46, type I diabetic 342.06 +/- 6.24, insulin treated diabetic 292.66 +/- 7.12 IU/g haemoglobin at 37 degrees C). No significant alteration was observed in the percentage of PGK bound to the membrane fraction of red cells in all the three conditions. The results indicate that the increased PGK activity is a result of a regulatory mechanism induced by the fluctuation of ATP level in response to elevated Na:K pump rate of erythrocytes in type I diabetes mellitus.