Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011860 (type 2 diabetes)
 57,723 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity and intracellular localization of two B-glycosidases i.e., N-acetyl-beta-D-glucosaminidase (NAG) and beta-glucuronidase (GR) was estimated by means of semi-quantitative histochemical methods in the peripheral blood neutrophils and lymphocytes from 52 patients with non-insulin dependent diabetes mellitus and compared with that in 67 healthy subjects of similar age and sex. The total neutrophil and lymphocyte count did not differ in the patients from that in the controls. The GR and the NAG activity indexes were significantly lower in the neutrophils from patients as compared with that in the control group. The number of lymphocytes with GR-positive and NAG-positive intact lysosomes were 200-fold and respectively 40-fold lower in the patients than in the healthy subjects. The authors discuss the significance of their observations with regard to the relationship between the enzymatic activity of the cells studied and their functional capabilities.
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PMID:The deficiency of B-glycosidases in leukocytes from patients with non-insulin dependent diabetes mellitus. 408

In untrained subjects, strenuous exercise provokes the appearance of oxidant stress markers in blood and muscle. On the other hand, trained muscle is resistant to oxidant stress unless exercise challenges the muscle glycogen supply. It is not known whether chronic high-intensity exercise alters the susceptibility of skeletal muscle to oxidant stress, whether there are gender-related differences in markers of oxidant stress, or whether elevating muscle glycogen stores by increasing dietary carbohydrate can minimize any exercise-related oxidant stress. To address these issues, collegiate rowers (12 men, 11 women) were randomly assigned to a moderate-(MOD, 5 g/kg body wt) or high-carbohydrate (HI, 10 g/kg) diet in a double-blind design and underwent strenuous training for 4 wk. Training in the A.M. was 40 min at 70% maximal O2 consumption (VO2); in the P.M. it was either three 2,500-m time trials (to assess power output) or aerobic and lactate tolerance training. Total daily training time was 65 min at 70% maximal VO2 and 38 min at > or = 90% maximal VO2. Thrice-weekly morning blood samples were assayed for serum creatine kinase (CK), plasma thiobarbituric acid-reactive substances (TBARS), and serum beta-glucuronidase (beta-Gluc). Weekly muscle biopsies were obtained for analysis of glycogen and, when tissue sample quantity allowed, TBARS. HI rowers produced more power and improved power more (10.7 +/- 1.0 vs. 1.6 +/- 1.6%) over the 4 wk than did the MOD rowers. Preexercise muscle glycogen concentration was maintained at 119 mmol/kg in MOD but increased 65% in HI rowers (P < 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:No evidence of oxidant stress during high-intensity rowing training. 833 41

Mitiglinide (MGN) is a new potassium channel antagonist for the treatment of type 2 diabetes mellitus. In the present study, a potential metabolic pathway of MGN, via carboxyl-linked glucuronic acid conjugation, was found. MGN carboxyl-glucuronide was isolated from a reaction mixture consisting of MGN and human liver microsomes fortified with UDP-glucuronic acid (UDPGA) and identified by a hydrolysis reaction with beta-glucuronidase and HPLC-MS/MS. Kinetic analysis indicated that MGN from four species had the highest affinity for the rabbit liver microsomal enzyme (K(m)=0.202 mM) and the lowest affinity for the dog liver microsomal enzyme (K(m)=1.164 mM). The metabolic activity (V(max)/K(m)) of MGN to the carboxyl-glucuronidation was in the following order: rabbit>dog>rat>human. With the assessment of MGN glucuronide formation across a panel of recombinant UDP-glucuronosyltransferase (UGT) isoforms (UGT1A3, UGT1A4, UGT1A6, UGT1A9, and UGT2B7), only UGT1A3 and UGT2B7 exhibited high MGN glucuronosyltransferase activity. The K(m) values of MGN glucuronidation in recombinant UGT1A3 and UGT2B7 microsomes were close to those in human liver microsomes. The formation of MGN glucuronidation by human liver microsomes was effectively inhibited by quercetin (substrate for UGT1A3) and diclofenac (substrate for UGT2B7), respectively. The MGN glucuronidation activities in 15 human liver microsomes were significantly correlated with quercetin (r(2)=0.806) and diclofenac glucuronidation activities (r(2)=0.704), respectively. These results demonstrate that UGT1A3 and UGT2B7 are catalytic enzymes in MGN carboxyl-glucuronidation in human liver.
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PMID:Carboxyl-glucuronidation of mitiglinide by human UDP-glucuronosyltransferases. 1735 41