Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001339 (acute pancreatitis)
 10,593 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

By using monoclonal antibody against human pancreatic secretory trypsin inhibitor (PSTI), we developed a highly sensitive, simple, and reliable two-site enzyme immunoassay system. The minimum amount of PSTI detected by this EIA is approximately 10 pg/ml when a 100 microliter aliquot of the sample is used. Good reproducibilities of within- and between-assay series and excellent recovery of exogenous PSTI from serum were observed. The correlation between the values obtained by the EIA and RIA methods was given by the linear regression equation, y = 1.09x + 4.6, for which the correlation coefficient (r) was 0.980 (n = 20). Antigenicity of the trypsin-PSTI complexes was found to be approximately 10% of that of PSTI. From these results, it seems that our recently developed EIA system for PSTI is useful in clinical testing for quantitation of PSTI in body fluids, for biochemical studies on synthesis and secretion of PSTI, and also for study of pathophysiological mechanisms involved in the development of acute pancreatitis and certain malignant neoplasms.
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PMID:A sensitive two-site enzyme immunoassay for human pancreatic secretory trypsin inhibitor (PSTI) using monoclonal antibodies. 307 18

Urinary trypsin inhibitors (UTIs) from the urine of a patient with acute pancreatitis consisted of three forms with different molecular weights. These were highly purified by ammonium sulfate precipitation, Sephadex G-75, SP-Sephadex C-25 and trypsin-Sepharose 4B column chromatography. The lowest molecular weight of UTIs was estimated to be 6,200 daltons. Moreover, five residues of N-terminal amino acids and a C-terminal amino acid were the same as those of pancreatic secretory trypsin inhibitor.
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PMID:Purification and some properties of a low molecular weight trypsin inhibitor from acute pancreatitis urine. 393 36

Serum immunoreactive pancreatic secretory trypsin inhibitor (PSTI) was measured by RIA. Serum PSTI levels were elevated in case of acute pancreatitis (15 of 15 cases: 317.7 +/- 155.6 ng/ml: Mean +/- SE) or pancreatic carcinoma (16 of 25 cases; 71.8 +/- 17.1 ng/ml), and in those with chronic renal failure (6 of 6 cases: 412.8 +/- 98.2 ng/ml). The molecular heterogeneity of elevated serum PSTI n such diseases was studied using chromatofocusing column chromatography. The results showed that serum PSTI was free from trypsin(-ogen) and was composed of at least three molecular forms of different isoelectric points. Two major forms were eluted around pH 8.2 (peak I) and 7.5 (peak II), with one minor form around pH 6.9 (peak III) from the column. The relative ratio of three forms differed with the disease state. Peak I was high in patients with pancreatic carcinoma, and peak II was high in patients with acute pancreatitis.
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PMID:Appearance mechanism and molecular heterogeneity of serum pancreatic secretory trypsin inhibitor (PSTI). 405 12

A clinical and biochemical analysis of 27 attacks of acute pancreatitis was made throughout the course of the disease. In severe attacks alpha 2-macroglobulin (alpha 2-M) decreased during the first days, reaching values in blood below 40% of the normal value. In addition, this remaining alpha 2-M had a decreased trypsin-binding capacity, indicating circulating alpha 2-M protease complexes. The inter-alpha-trypsin inhibitor concentration was also decreased, whereas alpha 1-proteinase inhibitor, antichymotrypsin, and pancreatic secretory trypsin inhibitor increased. All changes were most pronounced in the peritoneal fluid and were also closely correlated to the severity of the disease, assessed by both Ranson's and McMahon's classification systems. All patients with clinical complications had profound biochemical changes. In accordance with earlier findings, activation of both the complement and kinin systems seems possible in both blood and peritoneal fluid at the low alpha 2-M concentrations found in severe attacks.
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PMID:Protease inhibitors in acute human pancreatitis. Correlation between biochemical changes and clinical course. 608 96

A reliable radioimmunoassay (RIA) for human pancreatic secretory trypsin inhibitor (PSTI) has been developed. The method is highly sensitive (0.4 ng/ml), reproducible and specific. A good parallel relationship was observed between the standard curve and dilution curves for serum and urine. The PSTI bound to trypsin-alpha 2-macroglobulin complexes was found not to be immunoreactive, whereas a part of the psti-trypsin complex was immuno-reactive. In healthy individuals, serum PSTI level ranged from 5.4 ng/ml to 16.0 ng/ml, the average being 11.3 ng/ml (S.D. +/- 2.7). Elevated values were observed in patients with acute pancreatitis (highest value 3200 ng/ml), and in some patients with chronic relapsing pancreatitis.
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PMID:Radioimmunoassay for human pancreatic secretory trypsin inhibitor: measurement of serum pancreatic secretory trypsin inhibitor in normal subjects and subjects with pancreatic diseases. 615 49

High levels of immunoreactive pancreatic secretory trypsin inhibitor (PSTI) were demonstrated in the serum and peritoneal exudates of patients suffering from acute pancreatitis. Trypsin-like immunoreactivity in these fluids was found in complex with alpha 1-antitrypsin and in complex with alpha 2-macroglobulin and also as a free peak correlating to free trypsin(ogen). No trypsin-PSTI complexes or PSTI were demonstrated in the macroglobulin fraction of the peritoneal exudates. Saturated and partially saturated trypsin-alpha 2-macroglobulin complexes were prepared in vitro. PSTI was able to partially inhibit the BzArgNan-cleaving activity of both types of complexes in a slow dose-dependent non-linear reaction. Equilibrium was reached in each case within 1 h, but total inhibition was not reached even with large amounts of PSTI. Partially saturated trypsin-alpha 2-macroglobulin complexes were inhibited more readily than saturated complexes. The results support the concept of PSTI acting as a strictly local inhibitor of trypsin in compartments lacking plasma protease inhibitors.
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PMID:On the role of the pancreatic secretory trypsin inhibitor as an inactivator of trypsin-alpha 2-macroglobulin complexes in acute pancreatitis. 620 93

The clinical usefulness of serum pancreatic secretory trypsin inhibitor (PSTI) in pancreatic diseases was evaluated. The mean serum PSTI level of 41 healthy normal persons was 9.4 ng/ml (ranging from 5.2 to 16.7 ng/ml). Serum PSTI levels were abnormally raised in all patients with acute pancreatitis ranging from 35.0 to 4500 ng/ml, but were almost within normal range in patients with chronic pancreatitis, pancreatic cyst, acute abdominal emergencies such as perforated ulcer and intestinal obstruction, and macroamylasemia. There was no correlation between serum PSTI levels and total or pancreatic-type isoamylase activity. Patients with acute pancreatitis in whom the elevation of serum PSTI was transient and occurred after that of serum amylase activity had relatively mild symptoms and recovered along with normalization of serum PSTI levels. On the other hand, patients whose serum PSTI values became increased coincidentally with serum amylase activity and remained elevated, had severe clinical symptoms and unfavorable clinical outcome. Of 2 patients who underwent partial pancreatectomy, the serum PSTI level increased markedly in one who developed postoperative pancreatitis but not in the other without pancreatitis. In contrast to patients with acute pancreatitis, the serum response to the secretin stimulation in patients with chronic pancreatitis, was only small and transient, reaching the maximum at 10 min after administration of secretin. These results suggest that measurement of serum PSTI concentration may be useful in the diagnosis of acute pancreatitis and that the degree of rise and the duration of the elevated levels of serum PSTI are closely related to the severity of acute pancreatitis.
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PMID:Serum pancreatic secretory trypsin inhibitor in pancreatic disease. 620 36

This study has traced the behavior of rat anionic trypsin-like immunoreactivity and pancreatic secretory trypsin inhibitor (PSTI) immunoreactivity in the serum of rats undergoing bile-pancreatic duct infusions of buffered solutions with and without the addition of the bile salt taurocholate. Enzymatic analysis of alpha-amylase was also done. A mild pancreatic inflammation followed infusion of buffer alone, as determined by gross inspection of the pancreas and the behavior of serum levels of the above proteins. Animals infused with buffer and 4% taurocholate had major inflammatory changes, including gross hemorrhage into the gland, and marked elevations in serum levels of the three proteins studied. Graphic analysis of the serum levels revealed distinct sharp rises in the serum levels of all three proteins in the taurocholate group. In the buffered saline group only an initial sharp rise was present, followed by a prolonged decrease back towards base-line values. The immunoreactive trypsin in the taurocholate group was present in three fractions with different molecular weights: trypsin in complex with protease inhibitors, trypsinogen, and trypsinogen, and degradation products. PSTI immunoreactivity showed the molecular size of free inhibitor and that of degradation products. The presence of trypsin in complex with protease inhibitors indicates the formation of active trypsin during acute pancreatitis, which is further supported by the presence of degradation products of trypsin and PSTI.
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PMID:Pancreatic secretory proteins in sera from rats before and after induction of experimental pancreatitis. 661 80

The elimination of human pancreatic secretory trypsin inhibitor (PSTI) from the circulation of man has been examined in two human volunteers. Serial samplings of blood and urine were made for 55 h, after a rapid intravenous infusion of 125I-labeled human PSTI. The findings demonstrated a rapid initial elimination from the circulation. Within 30 min only 30% of the infused label remained (T1/2, 6 min). This was accompanied by the rapid appearance in the urine of radiolabel. Our results indicate that PSTI would prove a poor diagnostic marker for acute pancreatitis late in the course of the disease. This is opposed to the findings of Ogawa et al., who reported prolonged elevated circulating levels of PSTI weeks into the disease. However, they also noted rises of PSTI during acute pancreatitis in excess of 10 times the levels we have noted. Further exploration of population differences and the behavior of PSTI during acute pancreatitis are necessary to help resolve these findings.
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PMID:Elimination of pancreatic secretory trypsin inhibitor from the circulation. A study in man. 667 29

Experimental porcine pancreatitis was induced by the injection of taurocholate into the pancreatic duct. Recombinant human pancreatic secretory trypsin inhibitor (25 mg) was administered to each animal in one of three different ways: into the pancreatic duct (n = 5), into the abdominal cavity adjacent to the pancreas (n = 2) or intravenously (n = 2). The intrapancreatic turnover was assessed during 6 h using a microdialysis technique. The intraglandular concentration, measured by enzyme-linked immunosorbent assay, was highest after injection of rhPSTI into the pancreatic duct and substantially lower after intravenous and intraperitoneal administration. The intrapancreatic half-life of the inhibitor after intraductal administration was considerably longer (3-6 times) in pigs with pancreatitis than has previously been found in the normal gland. These facts argue in favour of the intraductal administration route in future trials of antiprotease treatment in acute pancreatitis.
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PMID:Intrapancreatic turnover of recombinant human pancreatic secretory trypsin inhibitor in experimental porcine pancreatitis. 763 56


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