Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011854 (type 1 diabetes)
 20,749 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Red cell phosphoglycerate kinase in insulin-dependent diabetes mellitus. 218 28

The activity levels of phosphoglyceromutase, Glucose-6-P-dehydrogenase. 3-P-Glyceratkinase and Glutathionreductase of the erythrocytes as well as 2,3-Diphosphoglycerate were determined in a total of 263 children suffering from juvenile diabetes mellitus. They were divided into two groups: 103 diabetics with a good state of metabolic control and 103 diabetics with a bad control. The results of 57 diabetic children were rejected. The enzyme activities have been shown to vary. PGM activity was increased in all diabetics, G-6-PDH only in such with bad condition of metabolic control. The activity of 3-PGK was significantly diminished, Glutathionreductase activity was indifferent in both groups. Until today we don't found results of other authors determining these enzymes. The changes of some enzyme activities in diabetics may be due to hormonal mechanisms by insulin.
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PMID:[Erythrocyte enzymes and 2,3-diphosphoglycerate in juvenile diabetics]. 715 16

Glutamic acid decarboxylase (GAD) is one of the major autoantigens found in insulin-dependent (Type 1) diabetes mellitus (IDDM). A novel hybrid form of GAD was created by fusing amino acids 1-101 of the human GAD67 protein to amino acids 96-585 of the human GAD65 protein. This hybrid GAD67/65 was expressed constitutively under the control of the phosphoglycerate kinase promoter (PGK1) in the yeast Saccharomyces cerevisiae. Enzymatically active GAD was prepared from yeast lysates by a one-step purification on an affinity column using GAD-1 antibody. The purified hybrid GAD67/65 was radiolabelled with iodine-125 and tested in an immunoprecipitation assay with IDDM sera. Results obtained using the recombinant yeast hybrid GAD67/65 were very similar to those obtained using 125I-labelled porcine GAD. Recombinant yeast hybrid GAD67/65 should have utility for diagnosis and presymptomatic detection of IDDM.
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PMID:Expression in Saccharomyces cerevisiae of antigenically and enzymatically active recombinant glutamic acid decarboxylase. 965 Feb 86