Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0149521 (chronic pancreatitis)
 7,199 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Duodenal juice collected after administration of Boot's pancreozymin and secretin to patients with various pancreatic diseases was subjected to deoxyribonuclease I (DNase I) assay, as well as measurements of total volume, amylase output and maximum bicarbonate concentration. It was observed that the DNase I output is well correlated with each of three factors. The DNase I output was much lower in patients with chronic pancreatitis or pancreatic cancer than in control subjects, and DNase I output was even found to be low in patients suspected of having chronic pancreatitis, who did not give abnormal resulsts with other assay methods. These results imply that DNase I output may be a good indicator of exocrine function of the pancreas, and thus may be useful for early detection of pancreatic diseases.
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PMID:Clinical studies on human pancreatic deoxyribonuclease I. 44 86

Serum Deoxyribonuclease (DNase) of normal persons and of patients with chronic pancreatitis, pancreatic cancer, Diabetes Mellitus, or other malignant diseases was determined with (32P) DNA as substrate. Serum DNase activity was much lower in patients with chronic pancreatitis, pancreatic cancer, or other malignant diseases than in control subjects, and serum DNase activity was almost normal in patients with Diabetes Mellitus. There was no correlation between serum DNase and serum amylase, but there was a good correlation between serum DNase and DNase I output in duodenal juice. There was an inverse correlation between serum DNase and serum RNase. These results imply that in the diagnosis of possible pancreatic disorders serum DNase may be a good indicator and thus may be useful for the detection of malignant diseases.
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PMID:Clinical investigation of serum deoxyribonuclease: II. Clinical studies of serum deoxyribonuclease activity in pancreatic disease. 52 Jul 66

In patients with pancreatic cancer deoxyribonuclease I (DNase I) serum levels were compared with those of other known pancreatic enzymes. Serum deoxyribonuclease I, elastase 1, immunoreactive trypsin, amylase and phospholipase A2 were determined in 40 healthy controls, 28 patients with pancreatic cancer, 49 with chronic pancreatitis and 40 with extra-pancreatic diseases. The analysis of variance showed a significant difference among groups for serum DNase I values. However, none of the 3 groups of patients had a mean deoxyribonuclease I value higher than that of the healthy controls. In pancreatic cancer and chronic pancreatitis patients, increases in the 4 pancreatic enzymes values were found in percentages that were higher than those for DNase I. A significant correlation was found between DNase I and phospholipase A2, but not between DNase I and elastase 1, immunoreactive trypsin and amylase serum activities. The findings indicate that deoxyribonuclease I serum determination is an even less satisfactory index of pancreatic malignancy than the other pancreatic enzymes. Rather than expressing pancreatic damage, any variations in this enzyme appear more likely to reflect an aspecific phenomenon.
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PMID:Deoxyribonuclease I serum activity in pancreatic cancer. 235 55

Pancreatic cancer secretory protein profiles were shown to be different from normals by a microcomputer-assisted analysis of isoelectric focusing patterns. Two acidic protein band regions (pI 3.0 and 4.5) of the pancreatic carcinoma profiles were significantly increased, and eight protein bands (pI 3.7, 5.0, 5.5, 6.5, 6.9, 7.3, 8.0, greater than 10.0) were significantly decreased. Highly significant decreases occurred at pH 7.3 (chymotrypsinogen) and at pH 5.0 (procarboxypeptidase Al, DNase I) in nonactivated specimens. The ratio between the absorbance points at 2.08 and 2.63 cm from the anode in each protein pattern differentiated the pancreas cancer specimens from the control group. Profiles found for the control group gave pI values similar to those found in the literature. The potential value of these findings in the search for tumor markers warrants further investigation as to whether these specimens can be differentiated from those from chronic pancreatitis patients.
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PMID:Human pancreatic secretory protein profiles in the search for tumor markers. 688 65

Human pancreatic Deoxyribonuclease I (DNase I), inhibitor was partially purified from duodenal juice of healthy subjects collected in the Pancreozymin-Secretin test, by a procedure which included ammonium sulfate fractionation, DEAE cellulose fractionation, Sepharose 4B affinity chromatography, and gel filtration. The final preparation inhibited DNase I only, and had no inhibitory activity on pancreatic RNase, and trypsin. The inhibitor had a molecular weight of approximately 40,000, as determined by gel filtration, and showed the same mobility as skeletal muscle actin on SDS gel electrophoresis. Then clinical studies were made on the DNase I inhibitor in duodenal juice obtained after administration of Pancreozymin and Secretin to patients with various pancreatic diseases. In patients with suspected chronic pancreatitis with whom the ordinary test, containing the assay of the total volume, amylase output and maximum bicarbonate concentration of duodenal juice had produced normal results, the DNase I inhibitor output was observed to be higher than that in control subjects. While it was lower in patients with confirmed chronic pancreatitis than in control subjects. There results imply that DNase I inhibitor output may be an indicator of the pancreatic inflammation state and be useful for the early detection of pancreatic diseases.
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PMID:Biochemical and clinical studies on human pancreatic deoxyribonuclease I inhibitor. 745 Mar 90

The SPINK1 gene, encoding the human pancreatic secretory trypsin inhibitor, is one of the major genes involved in predisposition to chronic pancreatitis (CP). In this study we have assessed the potential functional impact of 11 SPINK1 promoter variants by means of both luciferase reporter gene assay and electrophoretic mobility shift assay (EMSA), using human pancreatic COLO-357 cells as an expression system. The 11 promoter variants were found to be separable into three distinct categories on the basis of the reporter gene assay results viz loss-of-function, gain-of-function and functionally neutral. These findings, which were validated by EMSA, concurred with data from previous deletion studies and DNase I footprinting assays. Further, binding sites for two transcription factors, HNF1 and PTF1, were newly identified within the SPINK1 promoter by virtue of their being affected by specific variants. Combining the functional data with epidemiological data (derived by resequencing the SPINK1 promoter region in French, German and Indian CP patients and controls), then allowed us to make meaningful inferences as to each variant's likely contribution to CP. We conclude that only the three promoter variants associated with a loss-of-function (ie, -53C>T, -142T>C and -147A>G) are likely to be disease-predisposing alterations.
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PMID:Assessing the pathological relevance of SPINK1 promoter variants. 2161 Jul 53