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PubMed2000

Is fungal alpha-amylase in bread an allergen?

BACKGROUND: The enzyme alpha-amylase from Aspergillus oryzae used in bakeries to improve the bread quality has been identified as an inhalative allergen in baker's asthma. It is doubtful whether this enzyme can induce allergic sensitization in regular bread consumers. OBJECTIVE: To find out whether fungal alpha-amylase in bread and rolls retains its antibody-binding capacity and allergenicity after the baking procedure. METHODS: Rabbit antibodies directed to fungal alpha-amylase were used for the development of a two-site enzyme-linked immunosorbent assay (ELISA). This assay was used to analyse different fractions of bread and rolls baked with the usual amounts of alpha-amylase in comparison with control products without added enzyme. Competitive experiments between bakers' sera containing specific immunoglobulin (Ig) E to alpha-amylase and the rabbit antibodies were performed. Additionally, specific IgE binding to fungal alpha-amylase was inhibited by native or heated alpha-amylase. RESULTS: With the highly specific two-site ELISA for native alpha-amylase in the crust of bread bottom and sides, 2.3-7 ng antigenic alpha-amylase per gram crust were measured. No alpha-amylase could be detected in the crumb fractions. Rabbit antibodies to native alpha-amylase completely inhibited human IgE binding to alpha-amylase allergen disks. CONCLUSION: The results prove residual antibody-binding capacity of alpha-amylase in bread crusts and in the crust of some rolls. In comparison with the content of alpha-amylase in dough, between 0.1 and 20% of the antibody-binding capacity remained.

Animals↗
PubMed1998

Expression of beta-amylase from alfalfa taproots.

Alfalfa (Medicago sativa L.) roots contain large quantities of beta-amylase, but little is known about its role in vivo. We studied this by isolating a beta-amylase cDNA and by examining signals that affect its expression. The beta-amylase cDNA encoded a 55.95-kD polypeptide with a deduced amino acid sequence showing high similarity to other plant beta-amylases. Starch concentrations, beta-amylase activities, and beta-amylase mRNA levels were measured in roots of alfalfa after defoliation, in suspension-cultured cells incubated in sucrose-rich or -deprived media, and in roots of cold-acclimated germ plasms. Starch levels, beta-amylase activities, and beta-amylase transcripts were reduced significantly in roots of defoliated plants and in sucrose-deprived cell cultures. beta-Amylase transcript was high in roots of intact plants but could not be detected 2 to 8 d after defoliation. beta-Amylase transcript levels increased in roots between September and October and then declined 10-fold in November and December after shoots were killed by frost. Alfalfa roots contain greater beta-amylase transcript levels compared with roots of sweetclover (Melilotus officinalis L.), red clover (Trifolium pratense L.), and birdsfoot trefoil (Lotus corniculatus L.). Southern analysis indicated that beta-amylase is present as a multigene family in alfalfa. Our results show no clear association between beta-amylase activity or transcript abundance and starch hydrolysis in alfalfa roots. The great abundance of beta-amylase and its unexpected patterns of gene expression and protein accumulation support our current belief that this protein serves a storage function in roots of this perennial species.

Amino Acid Sequence↗
PubMed1994

The role of cereal and fungal amylases in cereal flour hypersensitivity.

To investigate the role of cereal alpha and beta-amylase in bakers' asthma, we have compared the IgE response of 30 wheat-flour-allergic individuals to barley alpha and beta-amylases with that of fungal alpha-amylase using radioallergosorbent test (RAST), RAST inhibition assays and Western blotting. RAST analysis showed 29 of the 30 subjects with inhalant induced cereal allergy had positive IgE to cereal amylases, but only 16 were positive to fungal alpha-amylase. Regression analysis showed an association between specific IgE to wheat-flour and to barley alpha-amylase (r = 0.70) and barley beta-amylase (r = 0.92) but a poor association with fungal alpha-amylase (r = 0.34). RAST inhibition showed minimal crossreactivity between barley alpha or beta-amylase and barley and fungal alpha-amylase. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting showed that non-reduced barley alpha-amylase had a molecular weight of 54 kDa and barley beta-amylase a molecular weight of 64 kDa. Reduced fungal alpha-amylase had a molecular weight of 54 kDa. Cereal alpha and beta-amylase appear to be important allergens in patients with allergy to flour.

Air Pollutants, Occupational↗
PubMed1999

Exposure-response relations of alpha-amylase sensitisation in British bakeries and flour mills.

OBJECTIVES: To describe the levels of exposure to fungal alpha-amylase in British bakeries and flour mills, and to describe the relation between exposure to alpha-amylase and sensitisation to fungal alpha-amylase. METHODS: 495 personal flour dust samples were taken in seven British bakeries and flour mills and analysed for alpha-amylase with an immunoassay. Workers at the sites were asked to fill out questionnaires on work related symptoms, smoking history, and work history, and they were skin prick tested with common allergens and fungal alpha-amylase to assess sensitisation. RESULTS: Exposure to high concentrations of alpha-amylase occur in a few areas of British bakeries and flour mills, and there can be considerable differences in exposures to alpha-amylase between sites and between exposure groups, and even within similar exposure groups from different sites. Exposure to the highest concentrations of alpha-amylase was found in the dispensing and mixing areas of the bakeries (geometric mean (GM) 39.7 ng/m3). Exposure to alpha-amylase showed only a moderate correlation with concentrations of dust (r = 0.42) and flour aeroallergen (r = 0.46). The results also showed a relation between exposure to alpha-amylase and sensitisation to fungal alpha-amylase (prevalence ratio (PR) for medium exposure 3.9, 95% confidence interval (95% CI) 0.8 to 20.2, PR for high exposure 9.9, 95% CI 2.8 to 34.6) compared with the low exposure category). Atopic subjects had an increased risk of sensitisation, but this was not significant. CONCLUSION: This study suggests that exposure to alpha-amylase is a considerable health risk in British bakeries and flour mills. A small proportion of workers are exposed to alpha-amylase at concentrations that result in high rates of sensitisation. A reduction in exposure to alpha-amylase is likely to reduce this risk.

Adult↗
PubMed1987

Serum amylases in chronic and end-stage renal failure: effects of mode of therapy, race, diabetes and peritonitis.

Serum total amylase, pancreatic amylase and lipase activities were studied prospectively in 43 hemodialysis, 22 peritoneal dialysis and 22 chronic renal failure patients. None of the patients had symptoms of pancreatic disease at the time of study. Mean total amylase activities were similar and above the upper limit of normal in the 3 treatment groups. Total amylase was abnormal in 75% of the patients and exceeded twice the upper limit of normal in 24%. Blacks and nondiabetics had higher levels than whites and diabetic patients, respectively. Percentage pancreatic amylase exceeded the upper limits of normal in one third of the patients. Mean pancreatic amylase was above the upper normal limit in the 3 groups, and values were abnormal in 63% of all patients. Mean pancreatic amylase activity was significantly lower in peritoneal dialysis than in hemodialysis or chronic renal failure patients (p = 0.01). Pancreatic amylase activity was unaffected by race. The higher total amylase activity in blacks was due to increased salivary isoenzyme. Hemodialysis treatments did not change total amylase or pancreatic amylase activity. Mean lipase activity approximated the upper limit of normal in the 3 groups and values were abnormal in 42% of all patients. Serum total amylase and pancreatic amylase activity did not increase during episodes of peritonitis in the peritoneal dialysis group. Peritoneal dialysis, whether or not accompanied by peritonitis, was responsible for removal of only a small amount of amylase activity per day.(ABSTRACT TRUNCATED AT 250 WORDS)

Amylases↗
PubMed2003

Mode of alpha-amylase production by the shochu koji mold Aspergillus kawachii.

Aspergillus kawachii produces two kinds of alpha-amylase, one is an acid-unstable alpha-amylase and the other is an acid-stable alpha-amylase. Because the quality of the shochu depends strongly on the activities of the alpha-amylases, the culture conditions under which these alpha-amylases are produced were examined. In liquid culture, acid-unstable alpha-amylase was produced abundantly, but, acid-stable alpha-amylase was not produced. The acid-unstable alpha-amylase was produced significantly when glycerol or glucose was used as a carbon source, similarly to the use of inducers such as starch or maltose. In liquid culture, A. kawachii assimilated starch at pH 3.0, but no alpha-amylase activity was recognized in the medium. Instead, the alpha-amylase was found to be trapped in the cell wall. The trapped form was identified as acid-unstable alpha-amylase. Usually, acid-unstable alpha-amylase is unstable at pH 3.0, so its stability appeared to be due to its immobilization in the cell wall. In solid-state culture, both kinds of alpha-amylase were produced. The production of acid-stable alpha-amylase seems to be solid-state culture-specific and was affected by the moisture content in the solid medium.

Aspergillus↗
PubMed2001

A comparative immunohistochemical study on amylase localization in the rat and human exocrine pancreas.

OBJECTIVE: To localize amylase enzyme immunohistochemically in the pancreatic acinar cells of rats and humans using polyclonal sheep anti-human amylase antibody, and to compare between the intensities of their amylase-immunostaining. METHODS: Indirect immunofluorescence method was applied on formaldehyde-fixed, and paraffin-embedded pancreatic sections obtained from adult male Wistar rats and autopsied human samples. Primary incubation was performed using sheep anti-amylase antibody followed by secondary incubation with fluorescein isothiocyanate-labeled rabbit anti-sheep IgG serum. Control tests of amylase immunospecificity were also undertaken either by incubation with primary antibodies previously pre-adsorbed with an excess of human pancreatic amylase, or only with secondary antibodies. RESULTS: The amylase immunofluorescence was positively and homogenously detected in all acinar cells of both rat and human pancreatic stained sections. The immunostaining was clearly demonstrated in the cell apices and peri-nuclear areas, but it was consistently brighter and more intense in the human acinar cells compared with that of the rat pancreas. Control tests of amylase immunofluorescence revealed the specificity of the antibodies applied for amylase localization in rat and human pancreas. CONCLUSION: Although many previous immunohisto- and cytochemical reports have successfully localized amylase in the pancreas of different mammalian species, but all of them have used locally prepared anti-amylase antibodies. The present report successfully illustrates immuno-localization of amylase in the pancreatic acinar cells of rats and humans using commercial polyclonal sheep anti-human pancreatic amylase antibodies, and also suggests their useful application in the immunochemical studies on various mammalian species. Additionally, the results indicate a structural similarity between the human and rat pancreatic amylases, a concept required further exploration.

Amylases↗
PubMed1989

A single gene directs synthesis of a precursor protein with beta- and alpha-amylase activities in Bacillus polymyxa.

The Bacillus polymyxa amylase gene comprises 3,588 nucleotides. The mature amylase comprises 1,161 amino acids with a molecular weight of 127,314. The gene appeared to be divided into two portions by the direct-repeat sequence located at almost the middle of the gene. The 5' region upstream of the direct-repeat sequence was shown to be responsible for the synthesis of beta-amylase. The 3' region downstream of the direct-repeat sequence contained four sequences homologous with those in other alpha-amylases, such as Taka-amylase A. The 48-kilodalton (kDa) amylase isolated from B. polymyxa was proven to have alpha-amylase activity. The amino acid sequences of the peptides generated from the 48-kDa amylase showed complete agreement with the predicted amino acid sequence of the C-terminal portion. The B. polymyxa amylase gene was therefore concluded to contain in-phase beta- and alpha-amylase-coding sequences in the 5' and 3' regions, respectively. A precursor protein, a 130-kDa amylase, directed by a plasmid, pYN520, carrying the entire amylase gene, had both beta- and alpha-amylase activities. This represents the first report of a single protein precursor in procaryotes that gives rise to two enzymes.

Amino Acid Sequence↗
PubMed1994

A new rapid immunoinhibition pancreatic amylase assay: diagnostic value for pancreatitis.

A new rapid immunoinhibition pancreatic amylase assay was compared to total amylase and lipase in an unbiased sample of 1005 emergency department patients with suspicion of pancreatitis, of which 55 had a final diagnosis of pancreatitis. Imprecision of the assays for both amylases (less than 2.5%) were better than for lipase (less than 6.1%). Correlation (R2) of pancreatic amylase with total amylase was 0.991 but only 0.789 with lipase. Using Receiver Operator Characteristics analysis, the best diagnostic cutoff point for all three enzymes was near the upper limit of the reference interval. With pancreatic amylase, sensitivity, specificity, and predictive values for positive and negative results are, respectively, 85.5, 92.5, 39.8, and 99.1%; we found similar values for lipase but poorer values (78.2, 92.0, 36.1, and 98.7%) for total amylase. Tests combination did not improve the diagnostic performance significantly. In the diagnosis of pancreatitis, pancreatic amylase (p = 0.037) and lipase (p = 0.049) had better diagnostic performance than total amylase. The correct diagnosis of pancreatitis could be achieved in 47 instead of 43 patients with either pancreatic amylase or lipase as opposed to total amylase among 1005 patients in this study. We conclude that pancreatic amylase and lipase are incrementally better diagnostic tools than total amylase for the diagnosis of pancreatitis.

Acute Disease↗
PubMed1990

Cloning and expression of raw-starch-digesting alpha-amylase gene from Bacillus circulans F-2 in Escherichia coli.

The raw potato-starch-digesting alpha-amylase gene of Bacillus circulans F-2 was cloned for the first time in Escherichia coli C600, using plasmid pYEJ001. The recombinant plasmid, named pYKA3, has a 5.4 kb insert from a chromosome of the donor bacterium. Subcloning of this amylase gene gave plasmid pHA300 which carried 3.15 kb of the inserted DNA. The transformed bacterium, E. coli C600 (pYKA3), produced the amylase in the periplasmic space, whereas it is secreted outside the cell in the donor bacterium. The cloned raw-starch-digesting alpha-amylase has a molecular weight of 93,000 on SDS-PAGE, and its action pattern was absolutely the same as that of the potent raw-starch-digestible amylase produced by B. circulans F-2. The periplasmic amylase produced by the transformed E. coli (pHA300) could digest raw starch granules such as potato, corn and barley raw starch granules, indicating that the raw-starch-digesting amylase is active in E. coli. Furthermore, this amylase crossreacted with the rabbit antiserum raised against the raw potato-digesting alpha-amylase of B. circulans F-2. From these results it was concluded that the cloned amylase is the same amylase protein as B. circulans F-2 amylase, which has a potent raw-starch digestibility. Thus, this paper is to our knowledge the first describing the molecular cloning of raw-starch-digesting alpha-amylase from Bacillus species and its successful expression in E. coli.

Bacillus↗
PubMed1995

Cholinergic regulation of amylase gene expression in the rat parotid gland. Inhibition by two distinct post-transcriptional mechanisms.

Stimulation of the beta-adrenergic or cholinergic muscarinic receptors are the principal mechanisms by which parotid salivary secretion is regulated in vivo. In this study we have examined the effects of cholinergic stimulation on amylase gene expression in dispersed rat parotid cells. [3H]Leucine incorporation into amylase and total protein was inhibited by carbamylcholine. Within 5 min of its addition, 10 microM carbamylcholine induced a 50-60% reduction in the rate of amylase synthesis which was sustained for more than 2 h. Blockade of the muscarinic receptor with atropine 8 min after addition of 10 microM carbamylcholine reversed the carbamylcholine-induced inhibition of amylase synthesis. When cells were exposed to carbamylcholine for 2 h before addition of atropine, there was only a slight reversal of inhibition. Carbamylcholine had no significant effect on the rate of total RNA synthesis but caused a progressive loss of amylase mRNA. After 2 h, amylase mRNA in cells treated with 10 microM carbamylcholine was 46% of control levels. Actinomycin D (5 micrograms/ml) lowered amylase mRNA by 8%; cycloheximide and phorbol 12-myristate 13-acetate had no effect. Isoprenaline (isoproterenol; at a concentration of 10 microM), which is an inducer of amylase gene transcription, elevated the amylase mRNA content by 30% after 2h. The calcium ionophore A23187 mimicked the effect of carbamylcholine by inhibiting [3H]leucine incorporation into amylase and lowering amylase mRNA content. The results suggest that acute stimulation of the muscarinic cholinergic receptor inhibits amylase biosynthesis in parotid cells not only by rapid attenuation of translation but also by causing a gradual loss of amylase mRNA, apparently by a Ca(2+)-dependent destabilization of the mRNA.

Amylases↗
PubMed1991

Molecular cloning and expression in Escherichia coli of cDNA encoding the subunit of sweet potato beta-amylase.

Tuberous roots of the sweet potato are unusually rich in beta-amylase, and the beta-amylase polypeptides account for about 5% of the total soluble protein of the organ. Unlike beta-amylases from other origins, the sweet potato beta-amylase is a tetramer of identical subunits, and it also bears starch phosphorylase-inhibitor activity. A cDNA for the subunit of sweet potato beta-amylase was obtained by immunological screening of an expression cDNA library constructed by the vector-primer and linker method using a plasmid vector containing tac-SP6 promoters. The SP6 transcript of a 2,000 base-pair-long cDNA insert directed the synthesis in vitro of a precursor to the subunit of beta-amylase which was identical in size with the mature subunit, and the beta-amylase mRNA detected by Northern blot hybridization was identical in size with the SP6 transcript of the cDNA insert. The cDNA insert contained 1,494 base pairs of an open reading frame which codes for the 499-amino-acid-long precursor to the subunit of beta-amylase. An amino acid sequence identical to the N-terminal amino acid sequence of the mature subunit appeared immediately after the initiator methionine of the precursor, indicating that the subunit of beta-amylase is synthesized as a mature form. Comparison of the amino acid sequences of subunits of sweet potato beta-amylase and seed beta-amylases from barley and soybean indicated that these enzymes share about 68% amino acid identities among each other. Escherichia coli cells harboring the cDNA clone produced the mature-sized subunit of the beta-amylase, and the soluble extract exhibited amylolytic activity which migrated to the same position as the beta-amylase purified from the sweet potato in non-denaturing polyacrylamide gel containing soluble starch indicating that oligomerization of the subunit occurred properly in E. coli cells.

Amino Acid Sequence↗
PubMed1991

Serum amylase determination in the emergency department evaluation of abdominal pain.

We hypothesized that selective ordering of serum amylase in the emergency department (ED) is justified because (a) most patients with elevated amylase can be prospectively identified by characteristic clinical findings, and (b) the diagnosis of pancreatitis is usually predominantly based on clinical findings, since amylase is known to be neither sensitive nor specific for pancreatitis. The study population included 133 consecutive patients with a chief complaint of abdominal pain who had amylase drawn over a 2-week period at a university hospital ED. Patients with known major trauma were excluded. Emergency department and hospital charts were reviewed for selected clinical variables. The first part of our hypothesis was evaluated by comparing clinical characteristics of cases (elevated amylase) and controls; the second part was tested by comparing clinical findings and amylase in cases (patients diagnosed as having pancreatitis) and controls. We found that 17 patients with and 116 without elevated amylase were similar with regard to all clinical variables, and that no combination of findings could be used to predict elevated amylase. Amylase level was not predictive of an ultimate diagnosis of pancreatitis, which was, however, strongly related to classical clinical findings. Pancreatitis risk factors, epigastric pain and tenderness, radiation of pain to the back, and nausea and vomiting were each statistically more common in patients diagnosed as having pancreatitis (regardless of amylase) than in patients in whom pancreatitis was excluded despite elevated amylase; all patients diagnosed with pancreatitis had at least two of these. Thus, selective ordering of amylase on the basis of clinical characteristics fails to identify a large proportion of patients with elevated amylase.(ABSTRACT TRUNCATED AT 250 WORDS)

Abdominal Pain↗
PubMed1981

Study of the possible enteropancreatic circulation of pancreatic amylase in the dog.

The possible existence of an enteropancreatic circulation of amylase was investigated in the dog. Endogenous amylase concentration in pancreatic venous blood was consistently greater than that in arterial blood, indicating a net flux of amylase from the pancreas to blood. Less than 0.02% of the metabolic clearance of 125I-amylase was accounted for by 125I-amylase in pancreatic secretions, indicating a minimal flux of amylase from the blood to pancreatic secretions. The venous-arterial amylase concentration across gut segments containing large quantities of amylase was not significantly different from 1.00, indicating absorption of less than 0.2% of the luminal amylase per hour. No 125I-amylase was detectable in serum after endoscopic instillation of labeled enzyme into the duodenum. These studies demonstrate negligible intestinal absorption of amylase and negligible pancreatic extraction of amylase, indicating negligible enteropancreatic circulation of pancreatic amylase in the dog.

Amylases↗
PubMed1984

Inhibitory action of thyrotropin-releasing hormone on serum amylase activity and its mechanism.

The effect of im administration of 500 micrograms TRH on serum amylase activity was studied in 34 normal women, 6 women with primary hypothyroidism, 1 woman with anorexia nervosa, 6 women with hyperthyroidism due to Graves' disease, and 5 women with renal failure on chronic hemodialysis. Serum amylase activity decreased significantly in 31 of 34 normal subjects 60 to 120 min after administration of TRH. However, amylase isoenzymes were not significantly affected after administration of TRH, suggesting that TRH equally affects pancreatic and salivary amylase activity. TRH was also effective in patients on chronic hemodialysis, indicating that TRH does not reduce serum amylase activity by increasing urinary excretion of amylase. Since TRH reduced serum amylase activity in hyperthyroid patients in whom TRH failed to stimulate TSH secretion, TRH does not reduce serum amylase activity through increased secretion of TSH. The action of TRH was not mediated by serum thyroid hormone levels since TRH was similarly effective in patients with hypothyroidism or hyperthyroidism. TRH did not inhibit or interfere with amylase determination when added in vitro to heparinized blood. Perfusion of the dog pancreas with TRH reduced amylase activity in pancreatic juice and pancreatic venous blood. The magnitude of the decrease was related to the dose of TRH used. Since decrease in amylase activity of the pancreatic juice preceded that in pancreatic venous blood, TRH probably directly acts on the pancreas to reduce amylase secretion. As a result, serum amylase activity decreased after administration of TRH.

Amylases↗
PubMed1987

Mechanism of glucocorticoid-induced increase in pancreatic amylase gene transcription.

To determine the mechanism(s) responsible for glucocorticoid-induced increases in amylase content in pancreatic acinar AR42J cells, we examined the effects of dexamethasone on amylase protein biosynthesis, steady-state mRNA levels, and gene transcription. Dexamethasone treatment led to a dose-dependent increase in amylase synthesis which was one-half maximal at 2 nM and maximal at 100 nM where a 6-fold increase was achieved. This dexamethasone-induced increase in amylase synthesis was detectable after 12 h, one-half maximal after 19 h, and approached maximal after 72 h. Dexamethasone treatment also increased amylase mRNA levels in a time- and dose-dependent manner in parallel with the changes in amylase synthesis. Nuclear RNA transcript elongation (run-on) assays indicated that amylase gene transcription was also increased in a time- and dose-dependent manner. Glucocorticoid enhancement of amylase gene transcription occurred relatively slowly, with a 6-fold increase occurring after 48 h of treatment with 100 nM dexamethasone. Thus, the effects of glucocorticoids on pancreatic amylase gene transcription fully accounted for the increased levels of amylase mRNA, synthesis, and content. However, due to the slow time course of dexamethasone induction of amylase gene expression we evaluated the possibility of glucocorticoid induction of a regulatory protein. We found that inclusion of cycloheximide or puromycin during dexamethasone treatment blocked the induction of amylase mRNA. These data suggest that the glucocorticoid-induced increase in amylase gene transcription requires induction of an unidentified regulatory protein(s).

Amylases↗
PubMed1987

Structural organization of the alpha-amylase gene locus in Drosophila melanogaster and Drosophila miranda.

Chromosomal sites belonging to the alpha-amylase gene family have been identified in D. melanogaster and D. miranda and in the sibling species of miranda, pseudoobscura, and persimilis. Two sites occur in chromosome 2 of melanogaster; one contains the Amy gene locus (54A) and the other an amylase "pseudogene" (53CD). Two sites of homology exist at 73A and 78C and perhaps another at 81BC in chromosome 3 of pseudoobscura and persimilis and in the homologous regions of the X2 chromosome in miranda. The active Amy locus is apparently at 73A. The structural organization of cloned sequences from this multigene family in melanogaster and miranda is under analysis, with emphasis on the functional Amy gene region. Electrophoretic variants of amylase have served as invaluable tools in these studies. For melanogaster, their use as genetic markers enabled us to positively identify our lambda Dm65 clone of the Amy locus and to show that it contains two functional copies of the structural gene for alpha-amylase. Amylase isozymes are now being used in P element-mediated transformation experiments aimed at defining regulatory elements for the temporal and spatial control of amylase expression during development and in response to dietary glucose. In miranda, electrophoretic variants of amylase were useful in assigning the Amy locus to chromosome X2, and they continue to serve as essential markers in our study of the evolution of dosage compensation for amylase expression in males of this species. Restriction maps of the Amy locus in 7 strains of D. melanogaster indicate that despite the worldwide origins of the chromosome samples, all contain a duplication of the amylase structural gene at this locus regardless of whether they produce two alpha-amylase isozymes, a single variant, or none. We have aligned these maps with the genetic and cytological maps of chromosome 2R in melanogaster and assigned alleles for different amylase isozymes to either the proximal or distal Amy gene copy in a number of strains. Restriction site polymorphism is relatively limited at the Amy locus, but some strain-specific rearrangements exist. The locus of two strains with reduced amylase activity, Amy1 (CA 1) and Amy "null", contain anomalies--an insertion in the former and an inversion in the latter. Causal relationships are being sought between the level of amylase expression in these strains and the position of their respective anomalies.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1994

alpha-Amylase in resectable lung cancer.

Biochemical analysis and immunohistochemical techniques support the theory that hyperamylasaemia in lung cancer is due to amylase production in carcinoma cells. The vast majority of amylase-producing carcinomas are adenocarcinomas with amylase isoenzyme similar to the salivary type. This prospective study assesses alpha-amylase expression in resectable lung cancer. Seventy four patients with resectable lung cancer were studied. Amylase activity in tumour tissue was analysed and isoamylase identification performed. Immunohistochemical analysis was performed using a polyclonal rabbit antibody against human salivary amylase. Hyperamylasaemia occurred in 13 out of 70 patients. Increased amylase activity in tumour tissue was found in 10 out of 52 cases, of which only two were associated with hyperamylasaemia. With the exception of one large cell carcinoma and one squamous cell carcinoma, the tumours were adenocarcinomas. Immunohistochemical analysis revealed amylase expression in seven adenocarcinomas and two adenosquamous carcinomas. In conclusion, immunohistochemical amylase expression was restricted to carcinomas with adenomatous differentiation. Biochemical analysis confirmed amylase production in 5 of 7 cases examined, the tissue amylase isoenzymes being of salivary type. However, hyperamylasaemia and a slightly increased amylase activity in tumour tissue may be caused by factors other than amylase-producing carcinoma cells.

Adenocarcinoma, Papillary↗