Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011849 (diabetes)
 277,896 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This is a report investigating the methylglyoxal (MG) bypass in animals, by which D-lactate is produced from triosephosphate via MG. Rats were made diabetic using streptozotocin or starved for 72 h. D-Lactate and various metabolites related to it, such as L-lactate, pyruvate, methylglyoxal, glucose, and inorganic phosphate, were measured in the blood plasma, liver, and skeletal muscle of the rats. Diabetic and starved rats had significantly higher levels of D-lactate in plasma, liver, and skeletal muscle compared with the control group. In contrast, pyruvate levels in plasma, liver, and skeletal muscle was markedly lower than normal in diabetic and starved rats. L-Lactate level lowered markedly in plasma, liver, and skeletal muscle of starved rats and elevated in liver of diabetic rats. Differences between plasma L-lactate level for diabetes and control were not significant. MG level was significantly elevated in plasma and depressed in livers and muscles of starved rats as well as livers of diabetic rats. Hepatic glycerol content was markedly increased in those states. Enzyme activities related to D- and L-lactate, such as pyruvate kinase, phosphofructokinase, aldolase, and glyoxalase I, were measured in the livers of these rats. Pyruvate kinase activity decreased in these states, but other enzyme activities showed no significant changes. D-Lactate was much more excreted than L-lactate in the urine of diabetic and fasted rats compared with normal rats.
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PMID:Concentrations of D-lactate and its related metabolic intermediates in liver, blood, and muscle of diabetic and starved rats. 148 Aug 18

As the UV-B cataract and early stages of diabetic cataract in rats only touches the epithelium and anterior superficial cortex, a whole lens analysis is not meaningful, but a regional analysis with the freeze-sectioning device has to be performed. Scheimpflug photography with microdensitometric image analysis enables the scientist to discern in vivo single layers along the optical axis of the lens. UV-B cataracts (0.2 J/cm2, every 2nd day) and diabetic cataracts (Streptozotocin (STZ), 70 mg/kg BW) were induced in Brown-Norway rats. The stages of lens opacification were documented by Scheimpflug photography. 8 weeks after start of UV-B treatment and at several dates before onset of visible diabetic cataractous changes, the animals were sacrificed. The lenses were divided reproducibly into 4 or 7 parts such as an equatorial ring and several layers of the central cylinder from anterior to posterior part. The enzyme activity spectrum shows highly region related pattern that would not have been found in a whole lens analysis. Aldose reductase was activated before appearance of visible cataractous changes due to diabetes compared to normal lenses. In contrast Fructose-1,6-biphosphate-aldolase activity was lower before onset of visible changes than in normal lenses, but only within the 1st section where later visible cataractous changes of UV-B cataract could be detected.
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PMID:Regional enzymatic analysis of UV-B and streptozotocin induced diabetic cataract lens. 196 39

We experienced 5 cases of acute renal failure due to rhabdomyolysis during the last two years and investigated those etiologies. Diagnosis of rhabdomyolysis was established by the detection of elevated serum creatine phosphokinase, myoglobin, aldolase, myoglobinuria as well as by the clinical course. The respective underlying illness of the 5 cases were grand mal seizures, infection (high fever), heat stroke, diabetes mellitus with hyperosmolar nonketotic coma and cerebral infarction treated by barbiturate. In this investigation, however, any single cause was not enough as the etiologies of rhabdomyolysis. There were multiple factors responsible to rhabdomyolysis in each case, such as hypokalemia, hypophosphatemia, shock, arteriosclerosis, etc. Some cases could not be classified as traumatic or non-traumatic rhabdomyolysis. Thus, in one case, acute renal failure due to rhabdomyolysis induced by the combination of grand mal seizures and serum potassium/phosphate depletion. 2 cases recovered without hemodialysis. 3 cases died in multiple organ failure, included a case treated by hemodialysis. We conclude that acute renal failure due to rhabdomyolysis induced easily by numerous diseases and early diagnosis is recommended.
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PMID:[Investigation of etiologies for acute renal failure due to rhabdomyolysis in 5 patients]. 212 50

This study measured axonal transport of 6-phosphofructokinase (PFK) and aldolase activities in the sciatic nerves of rats with short-term streptozotocin-induced diabetes. The diabetic rats showed deficits in anterograde (69% of controls; p less than 0.001) and retrograde (33% of controls; p less than 0.01) accumulations of PFK activity as well as its content per unit length of unconstricted sciatic nerve (86% of controls; p less than 0.05). There were no accumulation deficits in aldolase activity in the nerves of the diabetic rats, although the activity per unit length of unconstricted nerve was deficient (81% of controls; p less than 0.05). Treatment of diabetic rats with mixed bovine brain gangliosides (10 mg/kg of body weight/day, i.p.) did not affect the deficit in PFK activity in unconstricted nerve (84% of ganglioside-treated controls; p less than 0.01), but all the other defects in enzyme activities were prevented completely. The diabetic rats also showed a reduction of 7% (p less than 0.01) in sciatic nerve dry weight per unit length, which was prevented by ganglioside treatment. In contrast, the reduced motor nerve conduction velocity, accumulation of polyol pathway metabolites, and depletion of myo-inositol, characteristic of untreated short-term diabetes, were unaffected by ganglioside treatment.
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PMID:Ganglioside treatment of streptozotocin-diabetic rats prevents defective axonal transport of 6-phosphofructokinase activity. 245 37

The structural peculiarities of rabbit muscle aldolase accompanying enhancement of the aldolase activity in diabetes are described from the data of tryptophan phosphorescence at the room temperature and fluorescence polarization. It is shown that the pathology-concomitant conformational changes occur in both the hydrophobic part and NAD-binding site of the enzyme. The character of the structural changes in the hydrophobic part of the protein in diabetes and an increase in the enzymic activity are similar to that observed in normal aldolase after its interaction with NADH and are believed to be associated with the enhancement of the rigidity in the Trp-147 environment.
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PMID:[Structuro-functional characteristics of aldolase from rabbit muscles in diabetes]. 318 55

Analysis of slow axonal transport in sciatic and primary visual systems of BB rats with spontaneous diabetes of 2.5-3.5 months duration revealed a delay in transport of the neurofilament (NF) subunits, tubulin, actin, and the 60, 52, and 30 kDa polypeptides in both systems. The polypeptides examined were not affected uniformly. Rather, the transport of the 60, 52, and 30 kDa polypeptides and the rapidly moving component of tubulin, all constituents of the slow component b (SCb) of axonal transport, appeared to be more severely delayed than the transport of polypeptide constituents of the slow component a (SCa), such as NF and the slow-moving tubulin. Transport was not impaired in diabetic BB rats maintained normoglycemic with optimal doses of insulin. A 52 kDa polypeptide constituent of SCb was identified as neuron-specific enolase, and the 30 and 60 kDa polypeptides are likely to be aldolase and pyruvate kinase; all 3 are glycolytic enzymes. Morphometric analysis revealed that the cross-sectional area of sciatic axons was increased proximally at the level of the motor roots and decreased distally at the level of the tibial nerve. The changes in slow transport and caliber observed in central and peripheral axonal systems of diabetic BB rats are virtually identical to those previously described in rats with streptozotocin-induced diabetes, another model of insulin-dependent diabetes. In both models, the alterations of axonal caliber are likely to be secondary to the impairment of axonal transport.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Experimental diabetic neuropathy: similar changes of slow axonal transport and axonal size in different animal models. 336 21

It is shown that the activity of aldolase synthesized in rabbit muscles under diabetes is higher than that at normal state. This fact is probably a result of some structural alterations in NAD-binding site with Trp-291 and -311 in it which overlaps a considerable part of C-terminal region of the protein. The hydrophobic part of the enzyme containing Trp-147 under diabetes seems to remain unaltered. This consideration is based on the longwave shift in aldolase fluorescence lambda max (from 320 to 324 nm) under this pathology, suggesting a transition of Trp-291 and -311 into more polar environment and is confirmed by the disappearance of the difference in lambda max in the NADH presence. The NADH-originated shift in lambda max position for the both proteins ended at the same wave-length at 314 nm. The position of lambda max at 324 nm resulting from possible structural modification of NAD-binding site under diabetes correlates with an increase in the Stern-Volmer quenching constant value (from 4359 to 7500 M-1 for aldolase under normal and diabetic states, respectively). These quenching data evidence in favour of the suggestion on the existence of two classes of tryptophanyls in the aldolase molecule.
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PMID:[Comparative study of the structural characteristics of aldolase in rabbit muscles in normal states and in alloxan diabetes]. 377 81

1. Measurements were made of the activities of nine glycolytic enzymes in epididymal adipose tissues obtained from rats that had undergone one of the following treatments: starvation; starvation followed by re-feeding with bread or high-fat diet; feeding with fat without preliminary starvation; alloxan-diabetes; alloxan-diabetes followed by insulin therapy. 2. In general, the activities of the glycolytic enzymes of adipose tissue, unlike those of liver, were not greatly affected by the above treatments. 3. The ;key' glycolytic enzymes, phosphofructokinase and pyruvate kinase, were generally no more adaptive in response to physiological factors than other glycolytic enzymes such as glucose phosphate isomerase, fructose diphosphate aldolase, triose phosphate isomerase, glycerol 3-phosphate dehydrogenase, phosphoglycerate kinase and lactate dehydrogenase. 4. Adiposetissue pyruvate kinase did not respond to feeding with fat in a manner similar to the liver enzyme. 5. Glyceraldehyde phosphate dehydrogenase had a behaviour pattern unlike the other eight glycolytic enzymes studied in that its activity was depressed by feeding with fat and was not restored to normal by re-feeding with a high-fat diet after starvation. These results are discussed in relation to the requirements of adipose tissue for glycerol phosphate in the esterification of fatty acids. 6. A statistical analysis of the results permitted the writing of linear equations describing the relationships between the activities of eight of the enzymes studied. 7. Evidence is presented for the existence of two constant-proportion groups amongst the enzymes studied, namely (i) glucose phosphate isomerase, phosphoglycerate kinase and lactate dehydrogenase, and (ii) triose phosphate isomerase, fructose diphosphate aldolase and pyruvate kinase. 8. Mechanisms for maintaining the observed relationships between the activities of the enzymes in the tissue are discussed.
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PMID:The effect of dietary and hormonal conditions on the activities of glycolytic enzymes in rat epididymal adipose tissue. 424 55

We have examined the role of fructose as a substrate for the mammalian lung. Isolated and ventilated rat lungs were perfused for 2 h in the presence of either [U-14C]- or [5-3H]fructose. Fructose utilization, 3H2O production, and lactate and pyruvate production were measured. Insulin had no effect on the production of radiolabeled lactate. The 14C label from [U-14C]fructose was incorporated into the neutral lipids, phospholipids, fatty acid moiety, and deacylated fraction of lung. The apparent Km and maximum velocity of enzyme reaction for fructose utilization were 0.5 mM and 75 nmol X h-1 X g dry wt-1, respectively. Recovery of fructose 1-phosphate and fructose 1,6-diphosphate after perfusion with fructose, as well as detection of fructokinase, aldolase, and triokinase activities in the lung homogenates, suggested that fructose had been metabolized via phosphorylation through fructose 1-phosphate. Activities of fructose-metabolizing enzymes were not altered by the induction of diabetes, hypophysectomy, or starvation. These results suggest that mammalian lungs may utilize fructose to synthesize fatty acids, which in turn are used for phospholipid biosynthesis. The utilization of fructose by lung does not seem to be affected by nutritional or hormonal conditions.
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PMID:Fructose utilization by lung. 632 66

The fractions of lipoproteids, lactate dehydrogenase (LDH), malate dehydrogenase (MDH) and their isoenzymes as well as the fructoso-1-phosphate aldolase (F-1-PhA) and cholinesterase (ChE) activity were studied in 220 patients with diabetes mellitus, of which 156 had diabetes mellitus combined with ischemic heart disease (IHD). It was shown that the level of atherogenic lipoproteids is augmented in all the forms of diabetes mellitus and its latent stage, their highest content being seen in the disease, aggravated by IHD. An elevated level of pre-beta-lipoproteid atherogenic fraction was more common in diabetics with IHD. An increased F-1PhA and LDH5 activity was observed in all the patients examined, whereas in severe diabetes mellitus a decrease in the ChE activity was seen. The composed table of changes in the enzyme activity and atherogenic lipoproteid levels in diabetes mellitus combined with IHD, significantly differing from those of the diabetics without IHD, can be used for early IHD diagnosing in diabetes mellitus patients.
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PMID:[Diagnostic coefficients of ischemic heart disease in diabetes mellitus]. 688 7


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