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)

In order to investigate modifications of serum levels of elastase 1, immunoreactive trypsin, alpha 1-antitrypsin and alpha 2-macroglobulin in chronic pancreatic disease, and to speculate on the possible relationships among these parameters, the enzymes and inhibitors were assayed in the sera of 33 control subjects, 34 pancreatic cancer, 28 chronic pancreatitis and 36 extra-pancreatic diseases. An increase of elastase 1, alpha 1-antitrypsin and alpha 2-macroglobulin was detected in pancreatic cancer, chronic pancreatitis and extra-pancreatic diseases; no changes were found for serum immunoreactive trypsin. Multiple regression analyses showed that only 7% of elastase 1 was explained by inhibitors with alpha 1-antitrypsin playing a major role. Inhibitors did not influence immunoreactive trypsin. Our data indicate that the variations of the serum levels of proteases and antiproteases in chronic pancreatic disease are probably independent of each other.
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PMID:Serum elastase 1 and immunoreactive trypsin in chronic pancreatic disease: is there any relationship with trypsin inhibitors? 242 33

This study was undertaken in order to ascertain the behaviour of amylase and trypsin fractional clearances in chronic pancreatic disease and to speculate on the factors involved. Renal tubular function was also assessed in these patients. An increase of both clearances was found in a number of patients with pancreatic cancer and chronic pancreatitis. Amylase urinary output seems to be mainly related to the circulating enzyme levels; urinary IRT is principally accounted for by a functional tubular impairment. Tubular damage was observed in a number of patients with chronic pancreatic disease. This was related to pancreatic inflammation in chronic pancreatitis and to several factors, among which jaundice and pancreatic damage, in pancreatic cancer.
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PMID:Renal involvement in chronic pancreatic disease: effects on trypsin and amylase plasma-urine transfer. 246 19

Using the ascites fractions of a cancer patient as an immunogen, we have recently prepared an interesting monoclonal antibody (MoAb), MUSE11 (IgG1), to a circulating pancreatic cancer-associated antigen (antigen MUSE11). Immunoperoxidase study revealed that antigen MUSE11 was detected in virtually all adenocarcinomas (especially pancreatic carcinoma), whereas it was either negative or faintly positive in their normal counterparts among the digestive organ tissues. Western blotting analysis and periodic acid-Schiff carbohydrate staining revealed that antigen MUSE11 is a Mr 300,000 glycoprotein that is clearly different from other high-molecular-weight glycoprotein antigens which have been used for detection of circulating antigens in pancreatic cancer patients. MoAb MUSE11 appears to react with a peptide epitope of this molecule, since periodic acid and neuraminidase treatment of the antigen did not affect the reactivity of MoAb MUSE11 with the antigen, but trypsin and protease treatment abolished the reactivity. The antigen MUSE11 was purified using affinity chromatography in conjunction with MoAb MUSE11. This antigen appears to be highly glycosilated with N-linked carbohydrate moieties, since treatment of the pancreatic carcinoma Panc-1 cells with tunicamycin reduced the molecular weight band to Mr 110,000. Once antigen MUSE11 has been purified by affinity chromatography, neither CA19-9 nor pancreatic oncofetal antigens can be detected, although they were present at very high levels in the crude ascitic starting material.
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PMID:Immunohistological and immunochemical characterization of a novel pancreatic cancer-associated antigen MUSE11. 247 76

Urinary excretion of alpha-glucosidase (AGL), gamma-glutamyltransferase (GGT) and ribonuclease (RNase), and serum amylase and immunoreactive trypsin (IRT) were determined in 38 control subjects, 48 patients with pancreatic cancer, 77 with chronic pancreatitis and 47 with extrapancreatic diseases in order to ascertain the presence of a renal tubular damage and to investigate its etiology. A significantly increased frequency of pathological results for all urinary enzymes was documented in the various groups of patients as compared to controls. Significant correlations were detected among AGL, GGT and RNase. Considering the subjects as a whole, GGT and RNase excretions correlated with serum IRT and amylase; the two urinary enzymes were found to be higher when jaundice was present. In chronic pancreatic disease enzymuria was related to increased serum pancreatic enzymes; in extrapancreatic diseases it was associated to hyperbilirubinemia. The vast majority of patients with pancreatic cancer and elevated urinary enzymes presented hepatic metastases and/or jaundice. We can conclude that an anatomical and functional tubular impairment is detectable in some patients with chronic pancreatic and extrapancreatic diseases. Tubular damage seems to least in part to be related to pancreatic inflammation and necrosis in chronic pancreatic disease, while jaundice may be found to play an important role in diseases of the hepatobiliary tract. In pancreatic cancer, liver dysfunction (presence of liver metastases and/or extrahepatic cholestasis) also appears to be involved in altering tubular cells.
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PMID:Renal tubular dysfunction in pancreatic cancer and chronic pancreatitis. 256 74

Antigens, recognized by human monoclonal antibody (HB4C5) generated from a lung cancer patient, were found to occur in porcine pancreas. The antigens-I and -II were purified from crude trypsin of porcine pancreas, only by Mono Q column chromatography, and were eluted at 260 and 300 mM NaCl in 10 mM Tris-HCl buffer, pH 7.4, respectively. These antigens differed from trypsin in molecular weight, elution pattern from the Mono Q column, and their reactivity with HB4C5. The molecular weights of the two antigens were almost the same at around 35000. These were used for serodiagnosis with an assay system based on 96-well immunoplates. The reactivities of antigens-I and -II with various sera were similar. When the reactivity of IgG in serum with antigen-II was measured, absorbance at 415 nm in the case of normal and lung cancer patients was 0.178 +/- 0.056 and 0.492 +/- 0.136 (p less than 0.005). The rates of positive reaction in ovary, larynx, uterus, lung and liver cancers were more than 50%, but the rates in stomach and breast cancers were less than 30%. Positive reaction was hardly detected in pancreas cancer and normal controls.
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PMID:Serodiagnosis of cancer, using porcine antigens recognized by human monoclonal antibody, HB4C5. 264 62

Feeding of raw soya flour or other trypsin inhibitors such as camostate is a well-established method for promoting growth of (pre)neoplastic foci induced in the exocrine pancreas of rats by azaserine. The effect of trypsin inhibitors is thought to be mediated through an increased release of cholecystokinin. Using the specific cholecystokinin receptor antagonist lorglumide (CR-1409), we performed a 16-wk study to investigate the potential of this drug in inhibiting growth of putative preneoplastic foci and to determine whether and to what extent cholecystokinin is responsible for the effect of trypsin inhibitors on pancreatic growth. After initiation with 30 mg/kg of azaserine at 19 days of age, six groups of 15 rats each received one of the following treatments: camostate, cholecystokinin-8, or gelatin control, either or not in combination with CR-1409, once daily, 3 days wk for 16 wk. Plasma cholecystokinin levels, measured 30 min after the stimulus, were similar after camostate and cholecystokinin octapeptide administration. After 16 wk the pancreata were removed, weighted, and quantitatively analyzed for the number and size of putative preneoplastic foci by light microscopy. Both camostate and cholecystokinin octapeptide stimulated pancreatic growth and development of acidophilic putative preneoplastic foci, whereas growth of basophilic putative preneoplastic foci was inhibited by camostate but stimulated by cholecystokinin. CR-1409 almost completely abolished the effect of cholecystokinin and was found to cause a significant decrease in the effects of camostate. It is concluded that (a) cholecystokinin plays a significant role in camostate-stimulated growth of acidophilic putative preneoplastic foci in rat pancreas and (b) CR-1409 inhibits growth of putative preneoplastic foci induced in rat pancreas by azaserine and hence may be of potential value for the treatment of pancreatic cancer in humans.
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PMID:Modulation by CR-1409 (lorglumide), a cholecystokinin receptor antagonist, of trypsin inhibitor-enhanced growth of azaserine-induced putative preneoplastic lesions in rat pancreas. 270 31

A human hybridoma clone (A4-33) was established by fusion of human lymphoblastoid cells, HO-323, with lymphocytes of axillary lymph nodes obtained from a breast cancer patient. This clone has been stable, producing IgM for over 24 months. Enzyme-linked immunosorbent assay (ELISA) showed that monoclonal antibody A4-33 reacted strongly to MCF-7, and weakly to PANC-1 and HT-29, but not to other human malignant cell lines. The reactivity of A4-33 to MCF-7 was markedly reduced by treatment with periodate, but not affected or enhanced by neuraminidase or trypsin. Immunoperoxidase staining of normal human tissue sections showed that A4-33 reacted to acinar and ductal cells of the mammary gland and to ductal epithelial cells of the salivary gland, sweat gland, pancreas and bile duct. With malignant tumor sections, A4-33 reacted to breast cancer, pancreatic cancer and parotid cancer. These results suggested that A4-33 recognized the antigen which commonly exists on ductal epithelial cells of the exocrine gland.
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PMID:A human monoclonal antibody derived from axillary lymph nodes of a breast cancer patient. 274 85

Duodenal aspirates were obtained before, during, and after stimulation with secretin-cholecystokinin in 26 patients whose pancreatic function was classified as normal, moderately reduced, or severely reduced. The activities of gamma-glutamyltransferase (GGT), alkaline phosphatase (ALP), and 5'-nucleotidase (5NT) in the aggregated duodenal aspirate collected 10-40 min after stimulation showed marked overlap between the functional groups and lacked diagnostic value. For all three enzymes, the peak response occurred later in the severely impaired group than in those with normal pancreatic function. The three enzymes showed significant positive correlations with each other, and were negatively correlated with the output of trypsin and chymotrypsin and, in contrast with these proteolytic enzymes which were reduced in pancreatic disease, GGT, ALP, and 5NT all tended to increase with pancreatic disease. Contrary to a previous report, GGT did not serve as a useful index of pancreatic cancer in this study.
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PMID:Activities of gamma-glutamyl transferase, 5'-nucleotidase and alkaline phosphatase in human duodenal aspirate. 287 69

In order to investigate the role of circulating free trypsinogen and renal tubular dysfunction in affecting trypsin plasma-urine transfer, serum immunoreactive trypsin (IRT), its urinary output, IRT molecular size distribution, filtrable immunoreactive trypsin, gamma-glutamyltransferase and alpha-glucosidase outputs were studied in 6 control subjects, 9 patients with pancreatic cancer and 15 with chronic pancreatitis. The majority of immunoreactivity was always eluted at a molecular weight of about 24,000 and might therefore be considered as free trypsinogen. Variable amounts of IRT at higher molecular weights, possibly represented by trypsin-inhibitor complexes, were also detected. Increasing IRT levels were generally accounted for by free trypsinogen, regardless of the nature of the disease. Unlike serum free trypsinogen levels, renal tubular damage, evaluated by means of the excretion of two high-molecular weight urinary enzymes, seems to play a prominent role in explaining trypsin plasma-urine transfer.
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PMID:Molecular size distribution of immunoreactive trypsin and renal tubular dysfunction: role in trypsin plasma-urine transfer. 288 33

Plasma concentrations of human pancreatic polypeptide (HPP) parallel exocrine pancreatic secretion in response to stimulation with cholecystokinin. We determined prospectively the relationships among fasting HPP level, integrated HPP response to infusion of cholecystokinin, and output of trypsin and also the sensitivity, specificity, and predictive values of the fasting HPP level in the diagnosis of exocrine pancreatic disease. Our study group consisted of 19 patients with acute pancreatitis, 17 with chronic pancreatitis, and 25 with ductal adenocarcinoma of the pancreas and 27 control subjects. In the control patients and those with chronic pancreatitis, significant correlations were detected between HPP level and output of trypsin (P less than 0.001) in response to infusion of cholecystokinin and between fasting HPP and integrated HPP levels (P less than 0.004); no correlation was detected between HPP level and steatorrhea. The sensitivity, specificity, and negative and positive predictive values of the fasting HPP level for detection of either chronic pancreatitis or pancreatic cancer were similar and approximated 0.88, 0.67, 0.88, and 0.66, respectively. The HPP concentration had no value in detecting acute pancreatitis. Because the fasting HPP level has a high degree of negative predictability and is simpler to measure than the integrated HPP level or the output of trypsin, it may be a useful test in patients suspected of having either chronic pancreatitis or pancreatic cancer. A fasting HPP level of 125 pg/ml or greater could be used to exclude chronic pancreatitis or pancreatic cancer, but the finding of a value of less than 125 pg/ml necessitates use of other diagnostic tests for reliable determination of the presence of these diseases.
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PMID:Can plasma human pancreatic polypeptide be used to detect diseases of the exocrine pancreas? 298 84


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