Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

The concentration in serum of cathodal trypsinogen has been studied in certain clinical and experimental situations. The concentration correlated with pancreatic amylase activity. Low levels were found in patients with malabsorption due to exocrine pancreatic insufficiency. The concentration rose after endoscopic retrograde cholangiopancreatographic examinations (ERCP). After ERCP, however, no trypsin was detected complexed with protease inhibitors, as is generally found in acute pancreatitis. The trypsinogen concentration in serum also rose in renal failure indicating a renal elimination route for the endogenous trypsinogen.
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PMID:Studies on the turnover of endogenous cathodal trypsinogen in man. 10 10

Surgical liver biopsy specimen of a women aged 58 with "biliary complaints" showed amyloid deposits of unknown nature. After a nearly two-years-course of the disease the patient died of cardiac and renal failure. Clinical findings and laboratory tests without abnormal serum globulins suggested primary amyloidosis. Morphologically amyloid was present in the heart, tongue, striated muscles and in many parenchymatous organs and endocrine glands. By electron microscopy no difference was revealed between the primary and secondary type, respectively. Differenciation between primary and secondary form of the amyloid could only be achieved by the demonstratin of resistance of the deposits against induced proteolysis with trypsin digestion under the polarization microscope. The same result was obtained in two cases of senile amyloidosis. The case presented indicates that increased level of pathologic globulins is not an obligatory phenomenon in primary amyloidosis.
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PMID:[Diagnostic problems of primary amyloidosis]. 15 8

Acute intravascular haemolysis and renal failure developed while a patient was taking triamterene. A direct antiglobulin test with a polyvalent reagent was positive. Serum caused agglutination of normal red cells in the presence of triamterene and caused an increase of partial haemolysis of both trypsin-treated erythrocytes and red cells from a patient with paroxysmal nocturnal haemoglobinuria (PNH) in the presence of complement. From the results of antibody-neutralization test and treatment with 2-mercaptoethanol, the presence of IgM antibody with lambda light chain could be demonstrated. The triamterene seemed to bind strongly to the red cells in vitro but in vivo there was no detectable adsorption to red cells. Haptenic inhibition was not demonstrated. From these results, it was assumed that this antibody was found to cross-react with methotrexate which has a structure similar to that of triamterene.
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PMID:Triamterene-induced immune haemolytic anaemia with acute intravascular haemolysis and acute renal failure. 49 78

Plasma immunoreactive glucagon (IRG) concentrations were measured in 36 patients with chronic renal failure (CRF) and 32 normal subjects. In addition, the components of circulating IRG were analyzed by gel filtration in the fasting state and after physiological stimuli. Fasting IRG was elevated (P less than 0.001) in CRF patients (534 +/- 32 pg/ml) compared with the levels found in healthy subjects (113 +/- 9 pg/ml). Oral glucose suppressed plasma IRG in CRF patients from a basal level of 568 +/- 52 to a nadir of 354 +/- 57 pg/ml (120 min). This degree of suppression (38%) was comparable to that found in normal subjects (basal = 154 +/- 20 to 100 +/- 23 pg/ml) at 120 min (35%). Intravenous infusion of arginine (250 mg/kg) resulted in a 71% rise in IRG in CRF patients and a 166% increase in normal subjects. Gel filtration of fasting plasma from CRF patients showed three major peaks. The earliest (A) was found in the void volume (mol wt greater than 40,000) and constituted 16.5 +/- 4.7% of the elution profile. The middle peak (B) eluted just beyond the proinsulin marker (approximately 9,000 mol wt) and constituted the largest proportion of the elution profile (56.5 +/- 3.4%). The third peak (C) coincided with the standard glucagon and [125I]glucagon markers (3,485 mol wt) and comprised 27.0 +/- 4% of the IRG profile. In contrast, only peaks A and C were found in fasting plasma of normal subjects (53.6 +/- 10.4% in A and 46.4 +/- 10.4 in C). After oral glucose, glucagon immunoreactivity in the 3,500 mol wt peak (C) was markedly suppressed, while the B peak in patients with CRF declined to a lesser extent. The A peak in both groups was unchanged. After an arginine infusion only the C peak increased in both groups of subjects. Gel filtration of plasma in 3 M acetic acid gave similar profiles to those obtained in glycine albumin buffer. Exposure of serum to trypsin indicated that the B and C peaks were digestible, while the A peak was resistant to the action of the enzyme. In one sample, peak C increased after a 2-h exposure of serum to trypsin. We conclude that circulating IRG in normal subjects and patients with CRF is heterogenous. The hyperglucagonemia of renal failure is largely due to an increase in IRG material of approximately 9,000 mol wt, consistent with proglucagon, although the 3,500 mol wt component is also considerably elevated (threefold). The significance of circulating IRG levels should be interpreted with caution until the relative biological activity of the three components is established.
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PMID:Heterogeneity of plasma glucagon. Circulating components in normal subjects and patients with chronic renal failure. 95 99

Results vary with regard to the upper limits of serum amylase seen in patients with renal failure, and very little has been reported with patients with renal insufficiency not yet requiring dialysis. To determine the level of serum amylase elevation in renal insufficiency and renal failure, we determined serum amylase values in 128 subjects with creatinine clearances less than 90 ml/min. Serum amylase remained in the normal range when creatinine clearance was greater than 50 ml/min, and did not become elevated until creatinine clearance was less than 50 ml/min. The highest serum amylase recorded in the absence of acute pancreatitis was 503 IU/L (normal, less than 128 IU/L). Serum lipase and trypsin values paralleled those for serum amylase; values remained normal when creatinine clearance was greater than 50 ml/min, and were normal or elevated when creatinine clearance was less than 50 ml/min. These results indicate that elevations of serum amylase (i.e., amylase greater than 128 but less than 500 IU/L) in asymptomatic patients with impaired renal function are not evident until creatinine clearances fall below 50 ml/min, and probably do not represent acute pancreatitis.
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PMID:Serum amylase in patients with renal insufficiency and renal failure. 169 13

The serum amylase concentration reflects the balance between the rates of amylase entry into and removal from the blood. Hyperamylasemia can result either from an increased rate of entry of amylase into the circulation and/or a decreased metabolic clearance of this enzyme. The pancreas and salivary glands have amylase concentrations that are several orders of magnitude greater than that of any other normal tissue, and these two organs probably account for almost all of the serum amylase activity in normal persons. A variety of techniques are now available to distinguish pancreatic from salivary-type isoamylase. Pancreatic hyperamylasemia results from an insult to the pancreas, ranging from trivial (cannulation of the pancreatic duct) to severe (pancreatitis). In addition, loss of bowel integrity (infarction or perforation) causes pancreatic hyperamylasemia due to absorption of amylase from the intestinal lumen. Hyperamylasemia due to salivary-type isoamylase is observed in conditions involving the salivary glands. In addition, this type of hyperamylasemia occurs in conditions in which there is no clinical evidence of salivary gland disease, such as chronic alcoholism, postoperative states (particularly postcoronary bypass), lactic acidosis, anorexia nervosa or bulimia, and malignant neoplasms that secrete amylase. Hyperamylasemia can also result from decreased metabolic clearance of amylase due to renal failure or macroamylasemia (a condition in which an abnormally high-molecular-weight amylase is present in the serum). Patients with abdominal pain and a markedly elevated serum amylase (more than three times the upper limit of normal) usually have acute pancreatitis, and additional serum enzyme testing is not helpful. Patients with smaller elevations of serum amylase often have conditions other than pancreatitis, and measurement of a serum enzyme more specific for the pancreas (pancreatitic isoamylase, lipase or trypsin) is frequently of diagnostic value in such patients.
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PMID:Where does serum amylase come from and where does it go? 170 56

SDS-polyacrylamide gel electrophoresis and immunoblot were applied to analysis of plasma proteins immunologically related to inter-alpha-trypsin inhibitor (ITI). In this system, anti-ITI sera were able to identify ITI and other components with an Mr near 120 kDa which would be degradation products of ITI by limited proteolysis. An anti-UTI (urinary trypsin-inhibitor) serum could detect, beside these derivatives, two minor components (Mr values near 90 and 60 kDa). Analysis of perchloric acid supernatants of plasma samples, using the same technic, induced visualization of a new component, similar to urinary trypsin inhibitor which could not be detected by direct analysis. This one was also characterized in a higher content in pathological samples (renal failure and infectious diseases).
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PMID:Plasma proteins immunologically related to inter-alpha-trypsin inhibitor. 245 40

One possible route to cataract formation may be via the carbamoylation of lens proteins due to increased concentrations of cyanate in the body resulting from uraemia associated with renal failure and with severe diarrhoea. Carbamoylation of gamma-II-crystallin, which is found in the lens core, could alter the surface charge network of the molecules, resulting in aggregation, increased light-scattering and hence cataract. We have attempted to locate the site(s) of carbamoylation in gamma-II-crystallin. gamma-II-Crystallin was isolated by gel chromatography and ion-exchange chromatography. gamma-II-Crystallin was then carbamoylated by incubation with potassium [14C]cyanate, followed by citraconylation and digestion with trypsin to give peptides that were separated by high-resolution ion-exchange chromatography. The amino acid compositions of the radioactive peptides were compared with the expected peptide composition for gamma-II-crystallin. The radioactive peptide compositions, which agreed with the theoretical peptides, all matched with the N-terminal region of gamma-II-crystallin and had in common the presence of the N-terminal glycine residue. It appears that the alpha-amino group of the N-terminal glycine was the main site of carbamoylation. This site forms part of the charge network on the surface of gamma-II-crystallin.
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PMID:Site of carbamoylation of bovine gamma-II-crystallin by potassium [14C]cyanate. 259 Jan 75

Amyloid fibrils were isolated from kidney tissue of a cow afflicted with renal failure caused by spontaneous reactive amyloidosis. These fibrils were reduced and alkylated, and the amyloid subunit protein was isolated on a column of Sepharose CL6B. The protein was fragmented with both trypsin and Staphylococcus protease, and the resultant peptides were separated by high-performance liquid chromatography. Sequence analysis gave the complete primary structure of the protein with overlaps of the tryptic peptides confirmed by the Staphylococcus protease peptides. Comparison of the bovine amyloid A (AA) amino acid sequence with human protein AA demonstrates complete invariability from human position 33 to 45 and a very high degree of homology from positions 16 to 29 and 46 to 63. These data indicate that these portions of the molecule may be significant factors in amyloid fibrilogenesis. The bovine AA protein shows a blocked amino terminus, as is the case with the dog and the cat AA proteins. In addition, this protein contains an insertion of nine amino acid residues between human positions 69 and 70. The existence of an additional six residues after position 76 makes the bovine AA an unusually large 90 amino acid peptide. These findings point to a high tolerance for mutation in the carboxyl end of the molecule.
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PMID:A unique insertion in the primary structure of bovine amyloid AA protein. 290 53

The factors causing a decline in renal perfusion were studied in anaesthetized dogs with acute pancreatitis 4 h after the forceful injection of bile into the pancreatic duct. In 11 such dogs, glomerular filtration rate (GFR) decreased by 40.4% from the control state (P less than 0.05), whereas the clearance of para-aminohippurate (CPAH) declined by 50.2%. These changes were associated with a 15.3% decline in cardiac output (P less than 0.05) and a 26.2% fall in plasma volume. Glomerular morphology was entirely normal. When hypovolemia was prevented by infusing homologous plasma over the 4-h period of observation, the normally observed decline in GFR, CPAH, and cardiac output was prevented. The decline in plasma volume, associated with a rising hematocrit and declining plasma protein concentration, and the associated decrement in renal perfusion, could be entirely duplicated by the infusion of trypsin, chymotrypsin, elastase, and phospholipase A2 (but not lipase or amylase) into normal dogs. These perturbations also were prevented by the concurrent infusion of 4% albumin in saline. At 24 h, however, the renal failure became unresponsive to volume replenishment. We conclude that the decline in renal perfusion in dogs at 4 h with acute pancreatitis is entirely due to hypovolemia, induced by the release of specific enzymes from the inflamed gland, which causes the loss of protein-rich plasma from the vascular space.
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PMID:Renal failure in dogs with experimental acute pancreatitis: role of hypovolemia. 378 59


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