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PubMed1994

Epidermal growth factor inhibits amylase secretion and activation of phospholipase C in response to calcium-mobilizing secretagogues in rat pancreatic acini.

We recently showed that epidermal growth factor (EGF) inhibits cholecystokinin-octapeptide (CCK-8)-induced activation of phospholipase C and amylase release in isolated rat pancreatic acini. In the present study the effect of EGF on amylase release and inositol 1,4,5-trisphosphate (1,4,5-IP3) production in response to other calcium-mobilizing secretagogues, i.e. bombesin and carbachol, was examined in isolated pancreatic acini. EGF (17 nM) inhibited bombesin (100 nM)-stimulated amylase secretion from 10.3 +/- 1.7% to 0.8 +/- 1.6% of total above basal. Different from CCK-8, EGF reduced amylase release at both submaximal (< or = 1 microM) and supramaximal (> 1 microM) carbachol concentrations. Moreover, EGF (17 nM) inhibited bombesin-, carbachol-, and CCK-8-induced 1,4,5-IP3-production at five seconds after beginning of the incubation by 81 +/- 19%, 65 +/- 15%, and 60 +/- 12%, respectively. In conclusion, these results show that EGF inhibits amylase secretion in response to diverse calcium-mobilizing secretagogues in the exocrine pancreas and suggests that this inhibition is mediated by inhibition of phospholipase C.

Amylases↗
PubMed1979

[About the estimation of human parotid gland amylase in fractionated secretions (author's transl)].

The amylases are the main proteins in parotid secretions. In 30 probands the amylase secretion is observed under rest and gustatoric and parasympathicomimetic stimulation. A stimulation specific behaviour of amylase secretion is found. Under parasympathicomimetic stimulation by subcutaneous injection of Pilocarpin a high increase of amylase concentration is observed, in comparison to gustatoric stimulation where the concentration doesn't change. Different enzymatic activities of amylase under rest- and stimulation-conditions couldn't be found.

Adult↗
PubMed1993

[A case of lung cancer producing CA19-9 and amylase].

We report a case of lung cancer producing CA19-9 and amylase. A 58-year-old woman was admitted with dry cough and right chest pain. Chest X-ray and CT showed a mass shadow in the right lung field and right pleural effusion. Histological examination of a lung specimen obtained by TBLB and cytological examination of pleural effusion showed adenocarcinoma. The diagnosis of lung adenocarcinoma was made. CA19-9 values in serum and pleural effusion were very high. Amylase value was high in pleural effusion, but that in serum was normal. The amylase isozyme pattern was salivary-type. No abnormality was detected on abdominal CT and ultrasonography. In spite of treatment of the pleural effusion, the patient's condition gradually deteriorated and she died of respiratory failure. Histological examination of lung specimens obtained at necropsy showed moderately differentiated papillary type adenocarcinoma. Immunohistochemically, the tumor cells stained positively for both CA19-9 and amylase. We conclude that the lung cancer produced both CA19-9 and amylase.

Adenocarcinoma, Papillary↗
PubMed1993

[Construct of the stable-produced strain for the thermostable alpha-amylase].

The plasmid pE194 as a vector is used to subclone the thermostable alpha-amylase gene of B. licheniformis and construct recombinant plasmid pNW102. The plasmid pNW102 was transduced into B. subilis BF 7658 by bacteriophage PBS1. The B. subtilis BF7658 (pNW102) strain was treated at non-permissive temperature for a long time, and obtained many recombinant strains. This is the homologous recombination results between alpha-amylase genes of pNW102 and BF7658. The homologous recombination occurs at any site in alpha-amylase gene but there are some heat-spots. We have already screened 2 strains from the recombination strains which can stably produce the thermostable alpha-amylase in B. subtilis BF7658. The analysis of enzymology shows that the characters of the thermpstable alpha-amylase produced from the recombinants strains are the same with that of B. licheniformis.

Bacillus subtilis↗
PubMed1995

[Acquired amylase production induced by radiotherapy in a myeloma patient].

A 55-year-old patient with multiple myeloma (IgG-lambda) diagnosed in November 1988 was admitted because of bone pain throughout the body. After plasmapheresis and several courses of chemotherapy, a massive tumor of the left thoracic wall involving the rib appeared. Radiotherapy was performed to ameliorate the severe chest pain, after which myelomatous pleural effusion appeared on the left side. The serum, urine and pleural effusion revealed increased activity of amylase of the salivary type. Amylase activity was also detected in the supernatant of myeloma cells cultured from pleural effusion. We reviewed 12 cases of ectopic amylase-producing multiple myeloma. All the cases except one have been reported from Japan, and hyperamylasemia in these cases was detected at diagnosis or during course of the illness. Moreover, cytogenetic analysis of myeloma cells of previous reports revealed structural abnormalities including chromosome 1, near the amylase gene locus. This case also showed t (1; 10) (q 21?; q 26) by examination of 8 metaphase derived from bone marrow. These observations suggested that ectopic amylase production was induced by irradiation to the plasmacytoma of thoracic wall.

Amylases↗
PubMed1979

Renal handling of beta-2-microglobulin, amylase and albumin in acute pancreatitis.

The renal handling of beta-2-microglobulin, amylase and albumin was studied in patients with acute pancreatitis. The data were compared with results obtained from patients with glomerular proteinuria and from patients with tubular proteinuria. Initially during acute pancreatitis, the clearance ratio (clearance protein/clearance creatinine) for beta-2-microglobulin was increased dramatically (77-fold) compared to normals. After four to seven days this ratio had fallen and was elevated only 7-fold. The corresponding figures for amylase were 3.3 and 1.8 times and for albumin 9 and 5 times respectively. In glomerular disease, the clearance ratios for beta-2-microglobulin, amylase and albumin were increased 6, 1.1, and 154 times and in tubular disease 448, 1.1, and 28 times, respectively. The electrophoretic pattern of the urinary proteins during pancreatitis was mostly normal. In a few cases, slight tubular proteinuria was noticed. Amylase activity in serum and urine from patients with pancreatitis was found to sediment, (S20,W = 4.6) in a sucrose gradient, identical to amylase from normal serum and urine. The marked increase in the excretion of beta-2-microglobulin probably reflects interference of the kidney function at the proximal tubular level. Determinations of this protein in urine may be of value in studies of kidney dysfunction that can accompany pancreatitis.

Acute Disease↗
PubMed1996

The activity of alpha-amylase and its salivary isoenzymes in serum and urine of patients with neoplastic diseases of female reproductive organs.

The activities of alpha-amylase and its salivary isoenzymes were evaluated in serum and urine of 59 patients with ovary cancer, 10 women with endometrial carcinoma, 30 patients with cervical carcinoma and 20 women with other (nonmalignant) diseases of females reproductive system. An increased activity of alpha-amylase in serum was found in 39% of patients with ovarium carcinoma and in 23% of patients with cervical carcinoma. The activity of salivary alpha-amylase in serum was elevated in 89% of patients with ovary carcinoma and in 63% of patients with cervical carcinoma and in 20% of patients with endometrial carcinoma. Serum and urine of women with nonneoplastic diseases of reproductive system demonstrates normal values of salivary alpha-amylase activity. These observations allow to conclude that the assay of salivary alpha-amylase may be useful as an additional index in diagnostics of ovary and cervical carcinomas.

Adult↗
PubMed1995

The effect of pituitary adenylate cyclase activating polypeptide (PACAP) on amylase secretion from guinea pig pancreatic acini.

Pituitary adenylate cyclase activating polypeptide (PACAP) is a novel hypothalamic peptide, structurally related to vasoactive intestinal peptide (VIP). Our previous study in conscious dogs revealed that PACAP stimulated exocrine pancreatic secretion in a manner different from VIP. The objectives of this study were to characterize the effects of PACAP on amylase secretion and intracellular cAMP production in guinea pig pancreatic acini and to compare them with those of VIP and secretin. PACAP38 and PACAP27 (10(-10)-10(-8)M) stimulated amylase secretion from pancreatic acini in a concentration-related manner. The order of potency for amylase secretion was PACAP27 = VIP > PACAP38. The maximally stimulated amylase secretion by PACAP27 was not enhanced by VIP or secretin, but was synergistically increased by cholecystokinin and A23187. PACAP38 and PACAP27 (10(-2)-10(-7)M) increased intracellular cAMP levels in a concentration-related manner. The potency for cAMP production was PACAP38 = PACAP27 = VIP. These results suggest that PACAP38 and PACAP27, like VIP, directly stimulate amylase secretion from guinea pig pancreatic acini through alterations in cellular cAMP levels.

Amylases↗
PubMed1976

Amylase polymorphism: studies of sera and duodenal aspirates in normal individuals and in cystic fibrosis.

Prior genetic studies of the human pancreatic amylase (Amy2) locus have been directed principally to the electrophoretic analysis of serum and urine, on the assumption that these fluids receive negligible contributions from the salivary (Amy 1) locus. In support of that assumption was the observation that the isozyme bands were lacking in patients with cystic fibrosis and in a postpancreatectomy patient. We have examined the sera of 97 patients having cystic fibrosis and find normal levels of serum amylase. On electrophoresis, three-quarters of the cystic fibrosis patients have a pattern (F-pattern) not observed in normal sera. The pattern is characterized by the absence of Pa 1. Comparative electrophoresis and mixing experiments indicate that the F-pattern is of salivary origin and is unmasked in cystic fibrosis by the absence of a pancreatic contribution. The normal serum pattern is considered to be an admixture of salivary and pancreatic amylase. On the assumption that duodenal fluids might more closely reflect the pancreatic (Amy 2) locus, electrophoretic studies were performed on 148 normal individuals and 37 individuals with cystic fibrosis. Electrophoretic phenotypes in duodenal aspirates are more complex than previously reported in studies of urine and serum; presumably because of the higher concentrations of amylase in the aspirates. Comparative electrophoresis and mixing experiments indicate that the phenotypes observed in duodenal aspirates also reflect admixture of pancreatic and salivary amylase. This recognition of pancreatic and salivary admixture in sera fortunately does not alter our prior understanding of the genetics of the Amy 2 polymorphism. The extensive studies which led to the delineation of the Amy 2 polymorphism were essentially based on the presence or absence of a variant band which proves now to be outside the zone of admixture.

Amylases↗
PubMedDate not supplied

[Production and concentration of saliva and salivary amylase in obese children].

The objective of the present study was to study the profile of salivary amylase in obese children. The study was conducted on 58 children, 29 of whom were identified as obese (obese group) and 29 as non-obese (control group). The parameters for the assignment to the two groups studied were the W/H ratio of the NCHS and the tricipital skinfold. The children in the obese group presented percentiles of 90 or more for both curves. Saliva was collected after chemical stimulation with lemon juice using a standardized technique. The weight of secreted saliva and the concentration and total production of salivary amylase over a period of five minutes were determined in the samples collected. The results demonstrated that, among the control children, amylase concentration and total production were significantly higher in boys than in girls. Among the obese children, boys presented significantly higher salivary secretion than girls. Obese boys presented a significantly lower amylase concentration compared to control, a fact that was not observed for girls. Total salivary amylase production was not reduced among obese boys, suggesting that the decreased enzyme concentration in obese subjects is compensated for by greater salivary secretion.

Amylases↗
PubMed1998

Immobilization of alpha-amylase on poly(vinyl alcohol)-coated perfluoropolymer supports for use in enzyme reactors.

The suitability and potential for the use of poly(vinyl alcohol) (PVA)-coated solid perfluoropolymers in immobilized-enzyme engineering have been evaluated by using alpha-amylase from Bacillus licheniformis for the hydrolysis of starch. alpha-Amylase was covalently immobilized on PVA-coated poly(tetrafluoroethylene-hexafluoropropylene) (PVA-FEP) by covalent coupling with the use of p-beta-sulphate-(ethyl sulphonide)-aniline, 2,4,6-trichloro-1,3,5-triazine, 1.1'-carbonyldi-imidazole and 2,2, 2-trifluoroethanesulphonyl chloride activation procedures, and also for comparison with cyanogen bromide-activated Sepharose 4B. In all cases, immobilization greatly improved the thermostability of the alpha-amylase and its resistance to inactivation by 6 M urea. Also the enhancements of enzymic activities with increased temperature were higher for the immobilized enzymes than for the soluble enzyme, and the immobilized alpha-amylases were well suited to the continuous hydrolysis of starch conducted at elevated temperatures. Although the specific activities of the enzymes immobilized on PVA-FEP were lower than for that immobilized to Sepharose 4B, these novel supports showed far superior strength. The enzymes immobilized on PVA-FEP were able to be readily recovered from stirred batch bioreactors for repeated reuse, whereas the enzymes immobilized to Sepharose were fractured and fragmented under similar conditions of stirring. A conventional fixed-bed bioreactor was found to be unsuitable for continuous starch hydrolysis owing to an unacceptable build-up of pressure drop across the bed. However, an expanded bed reactor containing alpha-amylase immobilized on solid PVA-coated perfluorocarbon showed great potential for the continuous hydrolysis of starch. Only 20% of the enzyme activity was lost after use for 3 weeks at 72 degrees C. It is concluded that PVA-coated solid perfluorocarbon is a highly promising support for use in immobilized enzyme engineering.

Adsorption↗
PubMed1998

[Effect of changes of amino acids of N-terminal region of the mature protein on secretion of alpha-amylase in B. subtilis].

The mutant plasmid pAmy413C, in which G takes the place of A at the 271 position of alpha-amylase gene on the pAmy413 from B. licheniformis, was constructed by site-direct mutagenesis. At the N-terminus of the mature alpha-amylase, amino acid +2Asn was substituted by +3Asp in the wild type protein. Then, the alpha-amylase output of the mutant plasmid pAmy413C in B. subtilis was 2.02-2.57 times higher than that of the wild type pAmy413C in the same strain. The amino acid sequencing at the N-terminus of the matural alpha-amylase revealsed that the recognition site of signal peptidase I moved one amino acid upstream, from Ala-(+2)Asn to AlaAla-(+3) Asp. That is, the +2Asn of the wild type was changed to the +3Asp of the mutant. The secondary structural analysis showed that a 14-cycle structure formed in the alpha-amylase mRNA when the free energy was -51.7 kcal. In this case, the mutant is identical with the wild type. The difference between them is that G at 271 position is no longer paired with U at 211 position, hence, a G-overhang is formed. The secondary structural analysis of protein showed that one amino acid diminished in the turn structure of amino acid at 33-37 position, and this very amino acid is involed in an alpha-helix structure. In short, all the changes mentioned above in conformation and charged amino acids contribute to the increase in the protein secretion in B. subtilis.

Amino Acid Sequence↗
PubMed1976

[Effusions rich in amylase without pancreatitis. 14 cases].

This study involved 14 cases or pleural effusions or ascites rich in amylase and unrelated to chronic pancreatitis, a pseudo-cyst of the pancreas or acute pancreatitis. A pleural effusion rich in amylase may be secondary to a pancreatic neoplasm but this possibility seems rare. Amylase-containing effusions related to a nonpancreatic neoplasm are more common. The lesion is in general an advanced pleuro-pulmonary carcinoma, frequently an adenocarcinoma. The amylase activity of neoplastic effusion fluid is significantly increased but although levels similar to those of certain pancreatic effusions may be seen, very high figures would appear to be rare. Finally, two cases of amylase-rich pleural effusions were related to a pleuro-digestive fistula and one left-sided effusion was secondary to abdominal trauma.

Adenocarcinoma↗
PubMed2001

Cyst fluid levels of carcinoembryonic antigen, carbohydrate antigen 19-9, squamous cell carcinoma antigen, and amylase in thyroglossal duct and branchial cleft cysts.

Cyst fluid was aspirated from five thyroglossal duct cysts (TDCs) and four branchial cleft cysts (BCCs). The cyst fluid levels of carcinoembryonic antigen (CEA), carbohydrate antigen (CA) 19-9, squamous cell carcinoma antigen (SCC), and amylase were measured and compared between the two types of cyst. The enzyme immunoassay technique was used for CEA and CA19-9, while SCC and amylase levels were measured by the immunoradiometric assay and nitrophenol method, respectively. Immunostaining for CEA, CA19-9, and amylase was also performed. The serum levels of these markers in both groups of patients were within the normal ranges. In contrast, their cyst fluid levels were extremely high. There was no significant difference in the cyst fluid levels of CEA and SCC between the two types of cyst; however, the cyst fluid from the TDCs showed significantly higher levels of CA19-9 and significantly lower levels of amylase compared with that from the BCCs. Immunostaining revealed expression of CA 19-9 in nearly half the columnar epithelial cells in the TDCs, but not in the squamous epithelial cells in the BCCs. CEA and amylase were not found in the epithelial cells of either type of cyst. These findings seem to reflect the difference in etiology between TDCs and BCCs.

Adult↗
PubMed2001

Apocrine secretion of amylase and exocytosis of trypsin along the midgut of Tenebrio molitor larvae.

Amylase and trypsin were purified from Tenebrio molitor midgut larvae and used to raise antibodies in a rabbit. A Western blot of T. molitor midgut homogenates, after sodium dodecyl sulfate-polyacrylamide gel electrophoresis using amylase and trypsin antisera, showed only bands co-migrating with the purified enzymes. The antisera were used to localize the enzymes by immunofluorescence and immunogold labeling. Amylase occurs in a few regularly disposed anterior midgut cells. Non-amylase-secreting anterior midgut cells are proposed to be water-absorbing cells based on morphology and dye movements. Amylase is found inside vesicles originating from Golgi areas that seem to fuse together before their release along with the now disorganized apical cytoplasm (apocrine secretion). Trypsin precursors are observed inside small vesicles near the apical plasma membrane of posterior midgut cells, suggesting an exocytic mechanism of secretion, followed by putative trypsin activation. Apocrine secretion is thought to be an adaptation to enhance the dispersion of secretory vesicle contents released from a water-absorbing epithelium, whereas exocytosis is an efficient secretory mechanism in a water-secreting epithelium.

Journal Article↗
PubMed2000

Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2.

An additional amylase besides the typical alpha-amylase was detected in the cytoplasm of Bacillus subtilis SUH4-2, an isolate from Korean soil. The corresponding gene encoded a maltogenic amylase, which hydrolyzed cyclodextrin or starch to maltose and glucose; pullulan to panose; acarbose to glucose and acarviosine-glucose. Maltogenic amylase of B. subtilis SUH4-2 transferred sugar molecules to form various branched oligosaccharides upon the hydrolysis of substrates. The enzyme existed in a monomer-dimer equilibrium with a molar ratio of 3:2 in 50 mM KH(2)PO(4)-NaOH buffer (pH 7.0). The maltogenic amylase is most likely to be associated with carbohydrate metabolism in the cytoplasm, since the nucleotide sequence of the gene was highly homologous to the yvdF gene of B. subtilis 168, which is located in a gene cluster involved in maltose/maltodextrin utilization.

ATP-Binding Cassette Transporters↗
PubMed2002

Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus alpha-amylases in a diluted anionic surfactant solution.

The effects of an anionic surfactant, sodium dodecyl sulfate (SDS), on the kinetic behavior in the hydrolysis of amylose with two bacterial alpha-amylases from Bacillus amyloliquefaciens and B. licheniformis were studied. The catalytic rates of both amylases in the present study showed sigmoidal kinetics with increased concentration of added SDS; the rates were increased in the range below the critical micelle concentration (cmc) and then markedly decreased above the cmc. The catalytic rate of the alpha-amylase from B. amyloliquefaciens was more sensitive to the added surfactant than that of the alpha-amylase from B. licheniformis. The diluted SDS at concentrations below the cmc was responsible for the preferential formation of the enzyme-substrate (E-S) complex, and the hydrolytic catalysis of both enzymes was apparently accelerated. Thermodynamic parameters for the E-S complex formation revealed that the apparent enthalpy and entropy changes of both amylases were increased by the addition of the diluted SDS. It is suggested that the increase in hydrolytic rate by the addition of SDS is due to the larger increase in the entropy changes for the E-S complex formation than in the enthalpy changes.

Journal Article↗
PubMed2002

Association of alpha-amylase and the R1 protein with starch granules precedes the initiation of net starch degradation in turions of Spirodela polyrhiza.

In turions of Spirodela polyrhiza (L.) Schleiden, net degradation of storage starch is controlled by a special low fluence response of phytochrome requiring illumination for several days. This light effect has been used to study protein-starch interactions that occur prior to and during net degradation of starch. Following various pretreatments on S. polyrhiza turions, native starch granules were isolated and two fractions of starch-related proteins were distinguished: proteins enclosed within the starch particles (starch-internalized proteins) and those attached to the surface (starch-associated proteins). The pattern of starch-associated proteins as resolved by SDS-PAGE was more complex than that of starch-internalized proteins and varied depending upon the pretreatment of the turions. Two starch associated proteins were identified immunochemically as alpha-amylase (EC 3.2.1.1) and the R1 protein (Lorberth et al. (1998) Nature Biotechnology 16: 473-477). Dark-pretreatment of non-dormant turions does not induce starch net degradation. Under these conditions, alpha-amylase and R1 were bound to the surface of the starch granules. Continuous illumination with red light induces a rapid degradation of starch. Within the first 24 h of illumination the level of starch-associated alpha-amylase transiently increased and subsequently decreased rapidly. Similarly, the amount of the starch-associated R1 also decreased during illumination. The dissociation of both alpha-amylase and R1 from the starch granules preceded the decrease in starch content. However, binding of the two proteins to starch granules remained unchanged when the turions did not perform net starch degradation (as observed during continuous darkness, orthophosphate deficiency, or dormancy of the turions). Thus, during net starch degradation, so far unidentified changes are postulated to occur at the surface of the starch particles that are relevant for protein binding. This conclusion was supported by in vitro studies in which the binding of purified beta-amylase (EC 3.2.1.2) to starch granules isolated from turions following various pretreatments was monitored. The enzyme did bind to starch granules prepared from dark-stored turions (in which starch degradation had not been initiated), but not to those isolated from illuminated (starch degrading) turions.

Journal Article↗