Decrease in trypsinogen concentration of pancreatic juices from patients with chronic pancreatitis.
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Chronic Disease↗
Biomedical subjects
C Figarella
Publications and source records attributed to C Figarella.
Plasma lactoferrin levels in patients with chronic calcifying pancreatitis.
Lactoferrin is a nonenzymatic secretory protein of human pancreas specifically increased in the external pancreatic secretion of patients with chronic calcifying pancreatitis. The possibility of an elevated concentration of plasma lactoferrin level in these patients needed to be explored even if the low pancreatic concentration of the protein did not favor this hypothesis. As expected, no increase could be observed between the plasma lactoferrin level of 16 patients with chronic calcifying pancreatitis (131 +/- 15 micrograms/l), compared to 17 controls (166 +/- 11 micrograms/l) and 15 patients with different organic diseases (187 +/- 18 micrograms/l).
Calcinosis↗
Alpha 1-proteinase inhibitor in pure human pancreatic juice.
The presence of alpha 1-proteinase inhibitor (alpha 1-PI) in pure human pancreatic juice was demonstrated. Its concentration was measured using the radial immunodiffusion technique and compared to transferrin and albumin concentrations. In normal pancreatic juice the mean alpha 1-PI level (expressed in percent of total protein) was 0.21 +/- 0.02, whereas the mean levels of the two other serum proteins were 0.14 +/- 0.01 for transferrin and 0.90 +/- 0.07 for albumin. These levels increased significantly in the juice of patients with chronic calcifying pancreatitis. The serum origin of alpha 1-PI present in pancreatic juice was demonstrated by the good correlation existing between alpha 1-PI and albumin as well as between transferrin and albumin. In addition, in each case the alpha 1-PI level was found to be higher in secretin-stimulated juice than in cholecystokinin-stimulated juice. A similar pattern was also found for albumin.
Blood Proteins↗
Alpha 1-proteinase inhibitor in pure human pancreatic juice. Characterization of a complexed form in patients with chronic calcifying pancreatitis and its significance.
Two forms of alpha 1-proteinase inhibitor (alpha 1-PI) were characterized in the pancreatic juice of patients with chronic pancreatitis, one free form and one form complexed with a proteinase. This complex is probably present in minute amounts in normal pancreatic juice which contains mainly free alpha 1-PI. The proteinase bound to alpha 1-PI has been identified as chymotrypsin A and the inhibitory activity of the free form of alpha 1-PI has been demonstrated. These data underline the rapid conversion of human proteolytic zymogens into active enzymes and demonstrate the increase of this activation phenomenon in the juice of patients with chronic pancreatitis.
Blood Proteins↗
Immunolocalization of (pre)kallikrein in porcine and human pancreas at the cellular and subcellular levels.
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Animals↗
[Immunochemical diagnosis of chronic calcifying pancreatitis].
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Albumins↗
Alkaline phosphatase and acid lysosomal hydrolases in pancreatic juice and fibroblast cell cultures of patients with chronic calcifying pancreatitis.
Nine lysosomal enzymes and alkaline phosphatase have been assayed in human pancreatic juice from controls and patients with chronic calcifying pancreatitis. Specific activities were evaluated by a nonparametric test (Wilcoxon) with a probability of 2 P less than or equal to 0.5. The values of acid phosphatase, alpha-glucosidase, beta-glucosidase and alpha-galactosidase are significantly higher in pathological juices; the values of alpha-mannosidase and beta-glucuronidase are also increased in the same patients but at the limit of significance. Alkaline phosphatase, beta-hexosaminidase and alpha-fucosidase follows the same trend but the values are not statistically significant between the two groups of patients. Studies on skin cultures of four patients with chronic calcifying pancreatitis demonstrate that the increased specific activities of lysosomal enzymes in the pathological juices do not correspond to a leakage of these enzymes into the extracellular space as described for cystic fibrosis.
Acid Phosphatase↗
Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region.
Upon tryptic activation of pure human prophospholipase A2, a heptapeptide is released from the N-terminal part of the protein yielding active phospholipase A2 (EC 3.1.1.4). Both the kinetics of the activation process and the amino acid sequence of the activation peptide strongly resemble those of pancreatic zymogens of other mammalian sources. The kinetic properties of human phospholipase A2 and its zymogen are compared with those of the corresponding porcine enzyme using substrates present at micelles, molecular dispersed solutions or as monomolecular surface films. The most obvious difference between the human and porcine phospholipase A2 is the low enzyme activity of the former protein at pH 8.0 as compared to pH 6.0, both against micellar and monomeric substrates. Neither the Ca2+ binding properties nor the inhibition of the human enzyme using haloketones can easily explain this different pH optimum. The sequence analysis of the N-terminal region of the first 40 residues is reported.
Amino Acid Sequence↗
Salivary secretion in chronic pancreatitis with special reference to albumin and lactoferrin.
Saliva from one parotid gland was collected under citric acid stimulation in three groups consisting of 69 control subjects and two groups consisting of 25 patients with chronic and relapsing chronic pancreatitis. Mixed saliva was collected under mechanical stimulation from 10 patients and 6 control subjects. Flow rates and the contents of bicarbonate, amylase and protein were determined. In a subgroup of patients and controls albumin and lactoferrin were measured. Wide inter- and intraindividual variations of secretory values were observed and normal values (which are reported in detail) were highly dependent from conditions of stimulation. Secretory patterns were not significantly different between patients and control subjects. It is concluded that the alterations leading to an elevation of albumin and lactoferrin and a fall in other secretory values are restricted to the exocrine pancreas and do not affect salivary glands in chronic pancreatitis.
Adult↗
Immunocytochemical localization of pancreatic kallikrein in human acinar cells.
The immunological localization of kallikrein in human pancreatic tissue was studied at the optical and subcellular levels. Data obtained by light microscopy, using indirect immunofluorescence and immunoperoxidase techniques, demonstrate the presence of kallikrein in pancreatic acinar cells. Ultrastructural localization was performed by using the immunocytochemical protein A-gold technique. Kallikrein was found at the level of the rough endoplasmic reticulum and mainly in the zymogen granules of pancreatic acinar cells. Kallikrein was not found in the centro-acinar or duct cells.
Fluorescent Antibody Technique↗
Comparison of immunological and enzymatic properties of human urinary and pancreatic kallikrein.
Human urinary and human pancreatic kallikreins were compared by radioimmunoassay, immunoelectrophoresis, by their enzymatic activity using the substrate Ac-Phe-Arg-OEt and by their biological activity employing the dog blood pressure assay. The only significant difference observed was a higher anodal mobility of the urinary kallikrein under the conditions of immunoelectrophoresis.
Animals↗
Diagnosis of chronic pancreatitis by measurement of lactoferrin in duodenal juice.
Lactoferrin is a non-enzymatic secretory protein of human pancreas and is specifically increased in pancreatic juice of patients with chronic pancreatitis. Duodenal contents being easier to obtain than pure pancreatic juice, the possibility of using lactoferrin measurement in duodenal juice as a diagnosis test for chronic pancreatitis was explored. Forty-eight patients were studied. Duodenal juice was obtained devoid of salivary contamination by a special double lumen tube. Under these conditions lactoferrin secretion (concentration and output) is increased in patients with chronic pancreatitis. When expressed as the ratio of lactoferrin to lipase units, there was no overlap between chronic pancreatitis and other pancreatic disease or controls. The simplicity and the reproducibility of the technique on a material as readily available as duodenal juice confirms the diagnostic value of lactoferrin measurement in the assessment of patients with suspected pancreatic disease.
Adult↗
Immunolocalization of kallikrein in porcine pancreas at the ultrastructural level.
The immunological localization of kallikrein in porcine pancreatic tissue was investigated by an immunoferritin method and presented by electronmicroscopy. Kallikrein was found in the zymogen granules of the pancreatic acinar cells as well as in the golgian area of the same cells. On the same section, all the zymogen granules of all acinar cells gave a positive reaction. Kallikrein was not found in the centroacinar or interstitial cells.
Animals↗
The proteins of human pancreatic external secretion.
Human pancreatic external secretion is a mixture of proteins in solution in a strongly alkaline medium. 10% of proteins are constituted with non-digestive enzymes and proteins and mostly represented by serum-type proteins. 90% of proteins are digestive enzymes and zymogens necessary for digestion of proteins, lipids and carbohydrates present in diets. One prekallikrein is also secreted in pancreatic juice. The optimal pH of enzyme activities and the instability of most enzymes at acidic pH suggest that pancreatic secretion might not have a deleterious effect on gastric mucosa after duodenogastric reflux.
Gastric Mucosa↗
Immunocytochemical localization of lactoferrin in human pancreas.
Lactoferrin is a non-enzymatic secretory protein present in the acinar cells of human pancreas, and specifically increased in the pancreatic juice of chronic calcifying pancreatitis patients. Immunocytochemical localization of lactoferrin demonstrates its presence in the zymogen granules of the pancreatic acinar cell as well as in the endoplasmic reticulum cisternae. On the same section, only a few acini are positive but all cells within individual acini are similarly either positive or negative. The intensity of the reaction and the number of stained acini are greater in chronic calcifying pancreatitis patients.
Antigen-Antibody Complex↗
Lactoferrin and albumin in human pancreatic juice: a valuable test for diagnosis of pancreatic diseases.
Lactoferrin and albumin concentrations in pure pancreatic juice were studied by radial immunodiffusion in 81 patients. Lactoferrin concentration (% of total protein) was specifically increased in patients suffering from chronic calcifying pancreatitis (mean +/- SE: 0.169 +/- 0.024) and no overlap was observed with patients suffering from other pancreatic diseases (0.008 +/- 0.001), organic nonpancreatic diseases (0.011 +/- 0.001) and without organic disease (0.01 +/- 0.001). Lactoferrin concentration was not found to be correlated with chronic alcohol consumption or pancreatic insufficiency. Albumin concentration (% of total protein) was increased in patients suffering from chronic calcifying pancreatitis (5.55 +/- 0.49) and other pancreatic diseases (5.45 +/- 1.02). These values were significantly higher (P less than 0.001) than the corresponding values in patients with organic nonpancreatic diseases (1.66 +/- 0.16) and patients without organic diseases (1.46 +/- 0.22). Measuring lactoferrin and albumin in pancreatic juice may aid in the diagnosis of pancreatic disease and in the differentiation of chronic calcifying pancreatitis, even in the earliest stage, from other pancreatic diseases such as pancreatic carcinoma or acute pancreatitis.
Adult↗
Congenital pancreatic lipase deficiency.
A 5 1/2-year-old boy is reported with congenital lipase deficiency and the presence of colipase. He presented with greasy-oily stools since infancy, but growth and development have been normal. No other cause for exocrine pancreatic insufficiency could be found. Intraluminal (jejunal) fat digestion was defective, but some hydrolytic products of dietary long-chain triglyceride were present. The di- and monoglycerides were probably generated by pregastric lipases, although this was not measured directly. Amylase activity was depressed to some extent, a finding which could not be explained. Our studies do not clarify the issue of whether or not the absence of pancreatic lipase is explained as an inherited defect of lipase synthesis, or if it was acquired in utero or in the early postnatal period.
Amylases↗
Some properties of human pancreatic kallikrein and comparison with human trypsins and porcine kallikrein.
The properties of human pancreatic kallikrein purified from pancreatic juice were investigated. The enzyme is very stable at pH 8 but is rapidly inactivated at pH 2.6. It is a glycoprotein with a molecular weight of 35 000 as determined by gel filtration on Sephadex G-200. Contrary to the two human trypsins, human kallikrein like porcine pancreatic kallikrein is unable to hydrolyse casein and Met-Lys-bradykinin. Human pancreatic kallikrein is inactivated by diisopropyl fluorophosphate but not by chloro (N-p-toluolsulfonly-L-lysyl)methane. The enzyme does not react with various proteinase inhibitors (secretory pancreatic trypsin inhibitors, ovomucoid, lima bean and soybean trypsin inhibitors) but is inhibited by the Kunitz pancreatic trypsin inhibitor.
Animals↗