Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using an immunoenzymatic method, we studied lipase in the serum and urine of 23 controls, 22 chronic pancreatitis patients in symptomatic remission, and in 9 patients with proven pancreatic cancer. Serum and urine lipase and its fractional urinary clearance were compared with those of amylase and immunoreactive trypsin. Lipase immunoreactivity was detectable in the urine of 81.5% of the studied subjects (controls: 82%, chronic pancreatitis: 86%, pancreatic cancer: 66%); its output was higher than the upper limit of controls in 31.8% of chronic pancreatitis and in only 1 of pancreatic cancer, and it was significantly correlated with the urinary output of trypsin (r = 0.487, P less than 0.001), but not with that of amylase. A significant correlation was found between urinary output and serum levels for lipase, but not for trypsin or amylase. Fractional clearance of lipase was of the same magnitude as that of trypsin but only 0.1% that of amylase. 19% of chronic pancreatitis and pancreatic cancer showed a fractional clearance of lipase above the upper limit of controls, compared with 45% for trypsin and 3.2% for amylase. No difference in urinary clearance of the three enzymes was found between chronic pancreatitis and pancreatic cancer. In conclusion, although of no diagnostic relevance in pain-free patients with chronic pancreatic disease, this measurement can provide information on the mechanisms of renal excretion of pancreatic enzymes.
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PMID:Fractional urinary clearance of immunoreactive lipase in chronic pancreatic disease. 306 42

A murine monoclonal antibody (MAb), PA 8-15, was produced against a newly established human pancreatic adenocarcinoma cell line, SUIT-2. With the avidin-biotin immunoperoxidase technique, PA 8-15 MAb reacted strongly with 27 of 28 formalin-fixed paraffin-embedded pancreatic adenocarcinoma tissues. All six gall bladder carcinomas and all nine biliary tract carcinomas also showed positive reactions. In addition, PA 8-15 MAb reacted with gastric carcinomas (6/10), colorectal carcinomas (7/11), and some other primary adenocarcinomas. The distribution of PA 8-15 antigen on the same tissues of pancreatic cancer was different from those of CA 19-9 and DU-PAN-2 antigens and CEA. PA 8-15 MAb stained only the epithelium of the pancreatic duct, gall bladder and bile duct in normal adult tissues, and some normal fetal glandular epithelial cells. However, PA 8-15 MAb was not reactive with inflammatory or benign tumors of the digestive system except for the epithelium, as was seen in normal adults. Reactivity of PA 8-15 MAb with tissue specimens largely disappeared after treatment with neuraminidase, while oxidation with periodate or trypsin digestion did not alter the staining intensity, indicating that antigenic determinants may be at least partly of sialylated carbohydrate nature. These results suggest that PA 8-15 MAb detects a new oncofetal antigen in gastrointestinal cancers, especially of the pancreatico-biliary tract.
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PMID:Immunohistochemistry of human gastrointestinal cancer-associated antigen detected by monoclonal antibody PA 8-15. 313 Mar 61

From the clinical use of RIA-gnost trypsin kit, the following results were obtained. 1. Standard curve showed a steep and good curve was shown. 2. Incubation: The condition for the first incubation was set at the room temperature for 10-24 hours and that for the second incubation at the room temperature for 3-5 hours. With these settings, satisfactory results were obtained. 3. Reproducibility and recovery: The C.V. of the reproducibility and the recovery were considered superior, and the values were below 10% and +/- 3%, respectively. 4. Correlation between trypsin and serum elestase-1: An excellent positive correlation (coefficient of correlation r = 0.889) was shown. 5. Serum trypsin concentration of normal and pancreatic diseases: The normal range was from 100 to 500 ng/ml. Acute pancreatitis rose obviously. Diabetes mellitus and chronic pancreatitis was below 500 ng/ml and the pancreatic cancer showed a tendency to scatter in the range of 50-1,250 ng/ml. The above results indicated that serum trypsin can be easily measured with high precision by using this method. Thus the method is considered useful for the diagnosis of pancreatic diseases.
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PMID:[Clinical usefulness of a trypsin radioimmunoassay kit]. 322 76

In order to investigate the role of renal factors in affecting trypsinogen 1 metabolism and excretion in chronic pancreatic disease, serum immunoreactive trypsin (IRT), urinary IRT, gamma-glutamyltransferase (GGT), alpha-glucosidase (AGL) and RNase outputs and the molecular size distribution of serum and urine IRT were studied in 8 control subjects, 18 cases with pancreatic cancer, and 23 cases with chronic pancreatitis. Serum chromatography demonstrated that most immunoreactivity eluted as trypsinogen 1. Smaller amounts of immunoreactivity at higher molecular weights were also observed. Urine chromatography displayed both trypsinogen 1 and heavier molecular forms. An inverse linear correlation was noticed between creatinine clearance and serum trypsinogen 1 levels. Multiple regression analysis (urinary IRT output dependent and GGT, AGL, and RNase predictor variables) showed a significant linear correlation. RNase was found to be the most important parameter in explaining urinary IRT output. Mild variations in the glomerular function seem to be able to influence serum trypsinogen 1 levels. Urinary IRT excretion is principally explained by a disturbance in the tubular reabsorption of low molecular weight proteins, such as RNase.
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PMID:Renal factors in serum trypsinogen 1 metabolism and excretion in chronic pancreatic disease. 336 41

In patients with chronic pancreatitis, the development of exocrine pancreatic failure is generally thought to be an irreversible process. We found evidence to the contrary in a prospective study of 70 patients who were evaluated by endoscopic retrograde cholangiopancreatography and sequential measurements of stool fat, percent urinary PABA excretion, and serum trypsin during a follow-up time period of 1-4 yr. Initial p-aminobenzoic acid (PABA) testing showed exocrine failure in 51 patients, 35 of whom had low serum trypsin levels while 14 (27%) disclosed unexpectedly high trypsin concentrations. Ductal morphology was similar in patients with low and high trypsin values. In 8 of the latter cases, steatorrhea improved and pancreatic function tests became normal after pancreaticojejunostomy in 4 patients, alcohol abstinence in 3 patients, and spontaneous resolution of a pseudocyst in 1 patient. Pancreatic cancer was present in a further 3 patients. Of the 37 patients with low PABA and low trypsin at the outset, there was no improvement of exocrine function in 17 of 18 who were surgically treated. Conservative treatment had a similar effect in another 6 patients who were available for follow-up in this group. The mean duration of symptomatic disease was shorter (p less than 0.001) in patients with low PABA and high trypsin levels (1.4 +/- 1.2 yr) than in those with low PABA and low trypsin levels (4.5 +/- 1.3 yr). The results show that up to 20% of patients with chronic pancreatitis have exocrine pancreatic failure, which is apparently due to early ductal obstruction of a gland with preserved function; this situation can be suspected when low urinary PABA excretion and high serum trypsin levels are simultaneously found; and (c) exocrine failure may be reversible in these patients by using a pancreatic drainage procedure or alcohol abstinence. Such a peculiar pattern of pancreatic function tests may also suggest pancreatic cancer.
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PMID:Reversibility of exocrine pancreatic failure in chronic pancreatitis. 348 91

To estimate the diagnostic value of elastase output in the duodenal aspirates during a pancreozymin secretin test, elastase as well as amylase, chymotrypsin, trypsin, and lipase was determined in 46 controls and 61 patients with various disease. The elastase output decreased significantly in chronic pancreatitis (mild exocrine insufficiency 13 and advanced eight), pancreatic cancer (n = 10), and liver cirrhosis (n = 14) when compared with the controls. The outputs of the four other enzymes also decreased in chronic pancreatitis and pancreatic cancer, not in liver cirrhosis. Low elastase output was found in four of 13 chronic pancreatitis patients with mild exocrine insufficiency, whereas low outputs of the other enzymes were observed in only one or less of the 13. The ratio of elastase to amylase alone was significantly lower in the pancreatic diseases. The results suggest that elastase is the most susceptible enzyme to pancreatic dysfunction and that its output and its ratio to amylase output provide a valuable index to assess the enzyme secretory capacity in the pancreatic diseases.
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PMID:Elastase secretion in pancreatic disease. 384 84

Elastase 1 and immunoreactive trypsin were assessed by a RIA technique in the sera of 29 control subjects, 24 pancreatic cancer patients, 22 patients with chronic pancreatitis and 31 with extra-pancreatic diseases to ascertain and compare their usefulness in chronic pancreatic disease diagnosis. Increased levels of elastase 1 were detected in 60.9% of pancreatic cancer and in 61.1% of chronic pancreatitis patients; low values were found in only two subjects with pancreatic disease. A close correlation between the two enzymes was found in patients suffering from pancreatic cancer and chronic pancreatitis. These data suggest that serum elastase 1, as well as immunoreactive trypsin, is of limited value in chronic pancreatic disease diagnosis; increased levels of the two enzymes always occur simultaneously; low immunoreactive trypsin values together with normal elastase 1 serum levels are detectable in a number of patients with chronic pancreatitis and severe exocrine insufficiency.
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PMID:Serum elastase 1 in chronic pancreatic disease. 384 21

Pancreatic secretory trypsin inhibitor (PSTI) is a 6000-dalton peptide, that occurs in high concentrations in the pancreas and in pancreatic juice. It is thought to be synthesized by pancreatic acinar cells. We have recently reported the findings of an identical trypsin inhibitor at high concentrations in the urine of patients with gynecological malignancy. Therefore, we have named the inhibitor tumor-associated trypsin inhibitor (TATI). We have now studied patients who have undergone total pancreatoduodenectomy for pancreatic cancer or chronic pancreatitis. By radioimmunoassay (RIA), we found normal levels of this inhibitor in the serum and urine of pancreatectomized patients. The absence of pancreas was confirmed by measuring serum trypsin. By gel filtration and HPLC it was found that PSTI/TATI occurring in pancreatectomized patients was indistinguishable from that found in connection with pancreatitis and ovarian cancer.
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PMID:Pancreatic secretory trypsin inhibitor-like immunoreactivity in pancreatectomized patients. 393 45

Trypsin/creatinine clearance ratio--a recently proposed screening test for pancreatic cancer--was assessed in 45 subjects (17 control subjects, 15 patients with pancreatic cancer, and 13 with chronic pancreatitis). A statistically significant increase of the ratio was detected not only in pancreatic cancer, but also in chronic calcifying pancreatitis. Thus, the previously reported clinical usefulness of the test in pancreatic cancer diagnosis was not substantiated by the present data. Although not fully investigated as yet, reasons for an abnormal ratio are probably independent of the neoplastic or inflammatory nature of the pancreatic disease. Science renal enzyme excretion (alpha-glucosidase, gamma-glutamyltranspeptidase, leucine aminopeptidase) was not found to be invariably elevated when trypsin/creatinine clearance ratio was increased, tubular damage cannot be assumed as constituting the only reason for an altered clearance ratio.
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PMID:Role of trypsin/creatinine clearance ratio in the differential diagnosis of chronic pancreatic disease. 616 44

A radioimmunoassay for determination of human pancreatic elastase 1 was developed and the interaction of pancreatic elastase 1 with serum protease inhibitors (alpha 2-macroglobulin and alpha 1-antitrypsin) was investigated. Gel filtration studies showed that immunoreactive elastase 1 was present in serum and intact plasma as a complex with alpha 1-antitrypsin. Proelastase 1 in human pancreatic juice did not bind to protease inhibitors. But, after incubation with human serum or after activation with bovine trypsin, it was present as a complex with alpha 1-antitrypsin. The pancreatic elastase 1 content of the serum, measured by radioimmunoassay, was found to be influenced by the contents of both serum alpha 2-macroglobulin and alpha 1-antitrypsin. A significant inverse correlation was observed between the serum immunoreactive elastase 1 and alpha 2-macroglobulin contents in various hepatic diseases. The concentration of serum immunoreactive pancreatic elastase 1 was 1.79 +/- 0.62 ng/ml (mean +/- SD) in 28 normal controls. Its concentration was significantly increased in patients with acute pancreatitis, and although its concentration varied widely in patients with pancreatic cancer, its average concentration in these patients was significantly elevated.
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PMID:Radioimmunoassay of human pancreatic elastase 1. In vitro interaction of human pancreatic elastase 1 with serum protease inhibitors. 619 79


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