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)

Diabetic and normal cell lines from Chinese hamster kidneys were cultured in media containing 35SO4 and 3H-glucosamine. Glycosaminoglycans (GAG) were extracted and analyzed from the media, trypsin, and cell pellet by enzymatic and electrophoretic procedures. Significant increases in the hyaluronic acid content were noted in all three fractions of diabetic GAGs when compared with normals. In addition, an increased heparan sulfate content and decreased chondroitin sulfate amounts were noted in diabetic cell lines. These data suggest that in vivo changes in GAG types and amounts in diabetic kidneys seen by others may also be seen in cultured cells.
Diabetes 1981 May
PMID:Analysis of glycosaminoglycan from diabetic and normal Chinese hamster cells. 678 29

Exposure of sections of ileal mucosa to enzymatic digestion with trypsin and carboxypeptidase B reveals a population of immunofluorescent cells after incubation with a specific C-terminally directed antiglucagon serum. These cells, unreactive before enzyme treatment, were identified as L-cells by their immunoreactivity to antiglicentin serum and to cross-reacting (N-terminal) antiglucagon sera. The presence in the L-cells of antigenic sites characteristic of the glucagon-containing cells (A-cells) emphasizes the close relationships between these two cell types, and it further supports the hypothesis of glicentin as a glucagon precursor.
Diabetes 1980 Feb
PMID:Transformation of glicentin-containing L-cells into glucagon-containing cells by enzymatic digestion. 698 2

The relationship between diabetes mellitus and the exocrine pancreatic function was evaluated in 29 patients with insulin-dependent diabetes mellitus by measuring cathodic trypsin-like immunoreactivity (TLI) and the enzymatic activity of pancreatic isoamylase in serum before and 90 min after breakfast and insulin. Thirty healthy subjects served as reference group. Median fasting serum concentrations in the diabetic subjects were significantly lower than in the reference subjects: for TLI 143 and 299 micrograms trypsin standard/l and for pancreatic isoamylase 43 and 101 U/l, respectively (p less than 0.001 for both). A positive correlation between TLI and pancreatic isoamylase was present in the diabetics (Sperman's rho = 0.56, p less than 0.01). The serum concentrations of TLI and pancreatic isoamylase were not related to the duration of diabetes, daily insulin dose or glycemic control measured by blood glucose and total glycosylated hemoglobins. Cathodic TLI and pancreatic isoamylase in serum were not influenced by food and insulin.
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PMID:Serum concentration of cathodic trypsin-like immunoreactivity and pancreatic isoamylase in insulin-dependent diabetes mellitus. 705 64

Measurement of serum concentration of trypsin by RIA-Gnost Trypsin kit (Hoechst-Japan) was evaluated. The clinical usefulness of measuring serum trypsin level in diabetic patients was assessed. The measurement of trypsin using the radioimmunoassay (RIA) kit revealed good precision and reproducibility with intraassay error ranging from 3.6 to 5.5% in C.V. corresponding to mean trypsin concentration of 236.5-838.7 ng/ml and interassay error ranging from 8.1 to 11.1%. Tests for recovery and dilution were satisfactory for clinical use. Clinical materials included 35 normal subjects, 88 diabetics, 22 patients with liver diseases, 3 with acute pancreatitis, 7 with chronic pancreatitis and 3 with chronic renal failure. Serum trypsin concentration in normal controls was 157.6 +/- 59.9 ng/ml (m + 1 S.D.). Diabetic patients treated with diet therapy alone revealed serum trypsin level of 203.6 +/- 74.8 ng/ml (n = 50). In diabetics treated with sulfonil urea serum trypsin was 171.3 +/- 83.0 ng/ml (n = 25). In patients receiving insulin serum trypsin level was 90.5 +/- 49.0 ng/ml (n = 13). In patients with liver diseases, acute pancreatitis, chronic pancreatitis and chronic renal failure serum trypsin concentration were 236.9 +/- 88.0, 520.1 +/- 80.0, 113.0 +/- 75.6, and 2557 +/- 2771 respectively. Our results may indicate impaired pancreatic exocrine function in patients with severe diabetes mellitus. Increased serum trypsin level in diabetics treated with diet therapy may be due to stimulated excretion of trypsin resulted from restricted food intake. However, further study in larger number of patients is needed.
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PMID:[Evaluation of measuring serum trypsin by radioimmunoassay and clinical application for the study on the exocrine function in diabetics (author's transl)]. 708 13

To investigate abnormalities in peripheral nerve myelin in experimental diabetes, we studied the effects of the proteolytic enzymes trypsin and alpha-chymotrypsin on the proteins of this membrane, obtained from the sciatic nerves of normal rats and from animals made diabetic with streptozotocin. The dominant effect of the proteolytic enzymes was to incompletely degrade the major membrane protein (mol. wt. 28,000), with the appearance of new protein (mol. wt. 20,000). Using myelin isolated from the nerves of diabetic animals, the reaction was approximately one-half that of the controls (P less than 0.01) for both enzymes. When, however, the myelin protein affected by trypsin and chymotrypsin was isolated from the membrane and then incubated with the proteolytic enzyme, its proteolysis was complete and took place at the same rate in the diabetic animals and controls. These findings suggest that, in this model of experimental diabetes, there is an alteration in the structure of peripheral nerve myelin that inhibits interaction between the protein in the membrane bilayer and two water soluble proteolytic enzymes. This alteration could not be demonstrated in protein isolated from the membrane, suggesting that the change relates to the interaction of the protein and other components of myelin, rather than to chemical alteration in the protein per se.
Diabetes 1981 Apr
PMID:Effect of experimental diabetes on the susceptibility of myelin proteins to proteolysis. 720 63

The present study has been designed to work out the factors regulating the fasting serum levels of trypsin-like immunoreactivity in chronic pancreatitis. One hundred patients with chronic pancreatitis have been included and studied during a painless phase of the disease. No relationships have been observed between serum trypsin-like immunoreactivity and the presence of pancreatic calcifications. Serum immunoreactive trypsin levels showed a gradual decline parallel to the progressive impairment of bicarbonate and enzyme (trypsin and chymotrypsin) outputs in duodenal aspirates during pancreatic secretory studies. Therefore, serum trypsin-like immunoreactivity levels are thought to reflect the functional capacity of the exocrine pancreas. Reduced levels of trypsin-like immunoreactivity were detected in almost all patients with diabetes and steatorrhea. However, the finding of low levels also in a minority of chronic pancreatitis patients with normal endoscopic retrograde cholangiopancreatography or pancreatic secretory tests points to other factors which, in addition to the atrophy of the pancreatic parenchyma, may influence the circulating levels of trypsin-like immunoreactivity in chronic pancreatitis.
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PMID:Circulating trypsin-like immunoreactivity in chronic pancreatitis. 723 74

In 111 children and juveniles aged 7--27 years suffering from insulin-dependent diabetes mellitus the immunoreactive plasma human pancreatic trypsin was measured by means of the method RIAGnost-Trypsin-test, Behring. Decreased plasma trypsin was measured at the onset of diabetes already. In patients with diabetes with a period of 8--13 years the trypsin values were found to be significantly lower (79.6 +/- 35.3 ng/ml) than in these suffering from diabetes 0--3 years (100,4 +/- 36.9 ng/ml). None of all these patients had clinical pancreatic disease. Abnormalities in exocrine pancreatic function occur in patients with insulin-dependent diabetes mellitus, which is not confined to pancreatic islets only. Until today clinical consequences not can be drawn.
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PMID:[Trypsin deficiency in diabetes mellitus of children and adolescents (author's transl)]. 728 27

A survey is given of 26443 cataract operations at the University Eye Hospital of Graz in the years 1950-1980. Different phases are evident: 1. Extraction with a forceps. 2. A phase of expression. 3. Extraction by means of an erysiphake. 4. Extraction with a cryo-extractor. Enzymatic zonulolysis is of particular importance and performed with trypsin only. Almost all cataract operations are performed by enzymatic zonulolysis with trypsin. Details of the operation technique are pointed out. The connections between cataract surgery and increased intraocular pressure, vitreous body complications and retina and mentioned. Complications during and after operation and problems of anesthesia are discussed. Different special questions like cataract diabetes, cataract and myopia, cataracta complicata, cataracta congenita, cataracta traumatica and cataracta secundaria are pointed out. Our opinion is also given on combined operations like cataract and glaucoma, cataract and keratoplasty or binocular cataract operation. The correction of aphakia by means of intraocular lenses or refractive keratoplasty is discussed.
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PMID:[30 years of cataract operation (author's transl)]. 731 61

Fasting serum trypsin concentration and pancreatic trypsin output, stimulated by secretin and cholecystokinin-pancreozymin, were measured in 18 patients with insulin-dependent diabetes, to assess a possible correlation between these two indices of exocrine pancreatic function. Serum trypsin concentration was subnormal in 13, and pancreatic trypsin output was decreased in 14 patients, but there was no significant correlation between the two measurements. There was no correlation between serum trypsin and residual beta cell function measured by plasma C-peptide immunoreactivity (CPR). After an interval of four years serum trypsin measurements were repeated in 11 subjects. All individual trypsin levels were lower than the previous results, the difference being highly significant (t = 9.0; p < 0.001). Serum trypsin concentration therefore represents a qualitative index of reduced exocrine pancreatic function in diabetes, but has no value in quantitating the degree of deficiency.
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PMID:Serum trypsin concentration and pancreatic trypsin secretion in insulin-dependent diabetes mellitus. 739 96

Serum immunoreactive trypsin (SIT) concentrations measured in 616 children with diabetes of recent onset were low, in both boys and girls, in comparison with reference ranges established in patients with non-diabetic, non-infectious illnesses. The mean SIT concentration was 60% of the mean reference level in children tested within three weeks of the onset of diabetes, and about 40% in patients tested six months after the onset of diabetes. Very low SIT levels were found in about 10% of patients, most of whom had no measurable SIT by the assay procedure employed. These very low SIT concentrations were more frequent in older children aged 6-15 years, and in children tested at about 5-6 months after onset. Repeat tests on some of the children showed that the very low SIT levels were generally present for only a limited period.
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PMID:Serum immunoreactive trypsin concentrations in diabetic children. 743 Apr 1


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