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)

Two sisters presented with severe insulin resistance and markedly decreased insulin binding to erythrocytes, cultured fibroblasts, and transformed lymphocytes. The dose-response curve of insulin-stimulated amino acid uptake in the fibroblasts was shifted to the right. The molecular weight of the insulin receptor on the transformed lymphocytes from the patients was 210,000 and could not be dissociated to alpha- and beta-subunits by dithiothreitol treatment. However, the proreceptor was cleaved by trypsin, and this led to production of a 135,000-Mr alpha-subunit. Insulin binding to the trypsin-treated cells increased to the normal level, and insulin action was normalized. These results suggest that the failure of proreceptor cleavage produces hormone-resistant states and that a proreceptor syndrome may be a unique disease entity for hormone resistance.
Diabetes 1988 May
PMID:Insulin resistance by uncleaved insulin proreceptor. Emergence of binding site by trypsin. 336 Feb 20

Serum trypsin-like immunoreactivity and pancreatic isoamylase were measured in 302 insulin-dependent diabetic patients (166 men) using radioimmunoassay for the former and a photocolorimetric method for the latter. There was a significant correlation between the two enzymes (r = 0.67, p less than 0.0001) with lower concentrations of both trypsin-like immunoreactivity (208.8 micrograms/L) and pancreatic isoamylase (67.5 U/L) in diabetic patients as compared to controls (p less than 0.0001). Using multiple regression analysis, a statistically significant association was only apparent between enzyme concentrations and age at onset of diabetes (r = 0.31, p less than 0.0001). The results suggest that impaired exocrine pancreatic function may occur in an appreciable proportion of diabetic patients and also that a primary insult to the exocrine pancreas occurring at the time of endocrine injury may be a contributory factor.
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PMID:Serum concentrations of trypsin-like immunoreactivity and pancreatic isoamylase in insulin dependent diabetic patients. 337 27

The report discusses early-onset radiation injuries in the urinary bladder of more than 1000 patients with cancer of the cervix and corpus uteri. Clinical symptoms of such injuries were observed in 487 patients (44.3%). In 47 (10%), the lesions were pronounced. The degree of radiation-induced cystitis was evaluated on a 6-point scale used by WHO classification (1982). Said lesions mainly occurred at stage III of tumor and predominantly in cases of cancer of the corpus uteri. Complications development was stimulated by vascular lesions, diabetes mellitus and inflammatory processes in pelvic organs. Radiation injuries were treated by standard procedures as well as with immobilised trypsin administered in a cellulose powder vehicle. This method proved the most effective. Since patients suffering early-onset radiation-induced destructive injuries are at high risk of further exacerbation at later stages, they should be followed-up closely.
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PMID:[Prevention and treatment of early radiation reactions of the urinary bladder in patients with cancer of the cervix and corpus uteri]. 339 71

Previous studies have shown that met- and leu-enkephalins are present in extracts of whole pancreas obtained from guinea pigs and human cadavers. The present studies demonstrate that immunoreactive methionine (met)- and leucine (leu)-enkephalins present in rat pancreas are localized in islets of Langerhans. Immunohistochemical staining of fixed, whole pancreas indicated that only islet endocrine cells were heavily stained when any of four different met- and leu-enkephalin-directed antisera or an anti-BAM-22P (bovine adrenal medulla docosapeptide) antiserum was used. The peptides were characterized by a combination of gel-filtration chromatography, high-performance liquid chromatography (HPLC), and specific radioimmunoassay. Free met-enkephalin content in extracts of rat islets was 90-fold enriched over content in extracts of whole pancreas (1.72 +/- 0.35 versus 0.019 +/- 0.007 pmol/mg protein). Treatment with trypsin and carboxy-peptidase-B of high-molecular-weight peptides extracted from pancreas or islets resulted in release of additional met-enkephalin immunoreactivity, which was 39-fold enriched in islets compared with pancreas (5.90 +/- 0.58 and 0.153 +/- 0.032 pmol/mg protein, respectively). Total islet content (per milligram protein) of met-enkephalin-containing peptides was similar to that reported elsewhere for bovine hypothalamus. The immunohistochemical data as well as the enrichment of extractable enkephalins in islets compared with whole pancreas indicate that essentially all the met-enkephalin present in pancreas is localized in islets, while the presence of BAM-22P immunoreactivity in islets is consistent with biosynthesis of enkephalins in islet cells via a preprohormone, such as that described in the bovine adrenal medulla and rat brain.
Diabetes 1986 Jan
PMID:Opioid peptides in rat islets of Langerhans. Immunoreactive met- and leu-enkephalins and BAM-22P. 351 Jan 38

Oxidative phosphorylation and Ca2+-transport functions of liver mitochondria were normalized in rats with alloxane diabetes after peroral administration of phytoecdisteroids - ecdisterone and turkesterone (5 mg/kg) or nerobol (10 mg/kg) within 15 days. These drugs normalized the activity of NADH dehydrogenase and succinate dehydrogenase in respiratory chain of mitochondria, increased distinctly stability of the enzymes to the effect of such factors as heating, effect of phospholipase A2 or trypsin.
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PMID:[Comparative study of the effect of ecdysterone, turkesterone and nerobol on the function of rat liver mitochondria in experimental diabetes]. 377 12

Specific radioimmunoassays for the 7-S domain of type IV collagen and the fragment P1 of laminin were used to quantify these basement membrane proteins in human kidney cortex at different ages and in some patients with diabetes mellitus. The antigens were solubilized by treating the tissue samples with the proteolytic enzymes collagenase, trypsin and pepsin. Total collagen content (as indicated by hydroxyproline concentration) increased with age, and the proportion of the collagen that could be solubilized by any enzyme treatment decreased. The type IV collagen concentration increased significantly with age, whereas the laminin concentration tended to decrease. In the one case of a type I diabetic the amounts of both antigens exceeded those in the age matched controls. In four type II diabetics the results were comparable with those for other aged cases. The distribution of the proteins was studied using the peroxidase-antiperoxidase method. The staining intensity and thickness of both antigens increased with age in the mesangium and Bowmans capsules, the change in type IV collagen staining being more evident. In diabetic patients these changes were more pronounced and other basement membranes appeared thicker in the stainings. These results indicate that basement membrane material accumulates in the kidney cortex during aging and that an alteration takes place in the composition of the basement membranes, the proportion of type IV collagen increasing and that of laminin decreasing.
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PMID:Effect of age and diabetes on type IV collagen and laminin in human kidney cortex. 378 96

A convenient procedure is described for the purification of rat trypsin. Tissue was homogenized and extracted at pH 4 and the soluble fraction purified by a two-step affinity chromatography. After polyacrylamide gel electrophoresis at pH 8.8, the purified enzyme was resolved into 1 major and 2 minor bands all of which possessed trypsin-like enzyme activity. Antibodies to rat trypsin were raised in rabbits and utilized in establishing a sensitive radioimmunoassay procedure for the enzyme. The assay was adapted to study the levels of the enzyme in the circulation of normal Wistar and spontaneously diabetic Bio Breeding Wistar rats before onset of insulin-dependent diabetes mellitus in a longitudinal fashion. In the normal rat, serum levels of immunoreactive trypsin were higher in younger animals and showed a decline after weaning. This pattern was also seen in the Bio Breeding Wistar rats. In about half the number of Bio Breeding Wistar rats, serum immunoreactive trypsin levels were much higher than in normal rats. These results may imply that in some Bio Breeding Wistar rats the disease may be associated with inflammatory lesions of the exocrine pancreas.
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PMID:Rat trypsin: purification, radioimmunoassay and age-related serum levels in normal and spontaneously diabetic BB Wistar rats. 383 85

Based on a study of the kininogenase activity of the total plasma kallikrein in the presence of 3 concentrations of the soybean inhibitor trypsin (0.5, 1.0, 10.0 micrograms/ml) one can measure at a time the activity of tissue kallikrein (without specifying the source) and the activity of 3 forms of plasma kallikrein, including its adsorption on kaolin that characterizes the conformational structure of the enzyme. Examination of 10 healthy subjects and 136 patients revealed a 10 to 20-fold increase in the content of tissue kallikrein in plasma of 70% of diabetes mellitus patients and a 2.5 to 3-fold elevation in 50% of patients with chronic occupational bronchitis, and in 30% of patients suffering from chronic hepatitis. The method suggested makes it possible to have a better insight into the physiological and pathogenetic role of the kinin system and may be used for laboratory control over the treatment efficacy.
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PMID:[Method for determining kallikrein of tissue origin in blood plasma and its clinical significance]. 384 14

Antibodies have been raised against biosynthetic human proinsulin that show less than 1% cross-reactivity with human insulin and C-peptide. A sensitive (IC50 0.16 pmol/ml; minimum detectable concentration 0.004 pmol/ml) radioimmunoassay has been developed using this antiserum and 125I-proinsulin that will measure proinsulin-like immunoreactivity in human serum without the need for prior separation of insulin or C-peptide. In healthy, fasted subjects (N = 23), the serum proinsulin concentration was 0.015 +/- 0.001 pmol/ml (mean +/- SEM). In six healthy subjects, serum proinsulin rose to 250% of basal after 120 min in response to 100 g oral carbohydrate, but to only 130% after 60 min following 25 g oral carbohydrate. The proinsulin/total immunoreactive insulin ratio and the proinsulin/C-peptide ratio fell sharply after both high and low carbohydrate loads. Endogenous human serum proinsulin-like immunoreactivity released into the circulation after 100 g carbohydrate was eluted from a Mono Q high-performance, ion-exchange column with the same retention time as biosynthetic human proinsulin. Treatment of biosynthetic proinsulin with trypsin under mild conditions led to a decrease in proinsulin-like immunoreactivity concomitant with an increase in C-peptide and insulin-like immunoreactivity, indicating that the proinsulin-specific antiserum did not preferentially recognize intermediates of proinsulin cleavage.
Diabetes 1985 May
PMID:Measurement of circulating human proinsulin concentrations using a proinsulin-specific antiserum. 388 62

In the present experiments, we have correlated the distribution of 125I-insulin on the surface of rat hepatocytes with the dissociation of 125I-insulin from the cell. When 125I-insulin interacts with isolated rat hepatocytes at 15 degrees C, an increasing proportion of the bound ligand becomes nondissociable under the influence of acid pH (6.0), trypsin (0.5 mg/ml), or an excess of unlabeled insulin (10(-6) M). Under these conditions, only a small percentage of the labeled material is internalized as determined by quantitative electron microscope (EM) autoradiography. This progressive nondissociability of the ligand parallels its movement from microvilli to coated pits and its progressive concentration in these later surface specializations. These data suggest that receptors in different domains of the plasma membrane may have different dissociation rates for the ligand.
Diabetes 1985 Oct
PMID:Redistribution of 125I-insulin on the surface of rat hepatocytes as a function of dissociation time. 389 2


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