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Annals of African Medicine 2023Lipase and amylase are the most frequently used biomarker for the diagnosis of pancreatic diseases, especially acute pancreatitis. Lipase has better diagnostic accuracy...
BACKGROUND
Lipase and amylase are the most frequently used biomarker for the diagnosis of pancreatic diseases, especially acute pancreatitis. Lipase has better diagnostic accuracy in comparison to amylase for the analysis of acute pancreatitis. However, lipase assay in random access analyzer is sometimes difficult to perform as it is exposed to different types of samples or reagents which may act as interference.
MATERIALS AND METHODS
In our laboratory, we found the raised values (>500 IU/L) of lipase with normal amylase in some samples. However, the immediate rerun of these samples for lipase only showed normal (<80 IU/L) lipase level. To root out this fallacy, we performed reagent and sample carryover studies.
RESULTS
The cause of the falsely raised value of lipase was revealed by reagent carryover studies. All samples which assayed triglyceride (TGL) followed by lipase immediately after it showed elevated (>500 IU/L) lipase value. This is due to the interference of microbial lipase used in TGL reagents. This was corrected by separating the analysis of lipase and TGL into two different instruments.
CONCLUSION
If interference testing is not done, the laboratories are prone to have an analytical error in reporting and hence lead to diagnostic error. Hence, after analyzer installation, interference testing should be included in the validation protocol.
Topics: Humans; Pancreatitis; Acute Disease; Biomarkers; Lipase; Amylases
PubMed: 36695223
DOI: 10.4103/aam.aam_135_21 -
Journal of Traditional Chinese Medicine... Jun 2024To investigate the effects of (HH) as a free radical scavenger, and an inhibitor of the two enzymes i-e Alpha-amylase (α-amylase) and acetylcholinesterase (AChE).
OBJECTIVE
To investigate the effects of (HH) as a free radical scavenger, and an inhibitor of the two enzymes i-e Alpha-amylase (α-amylase) and acetylcholinesterase (AChE).
METHODS
In this study, HH plant was preliminary analyzed for phytochemical screening and then tested for its antioxidant, anti-α-amylase, and anti-AChE efficiency standard procedures.
RESULTS
Phytochemical analysis shows the existence of different compounds; while Coumarins and quinones were absent. The total phenolic, flavonoid, and tannins content were found to be (78.52 ± 0.69) mg GAE/g, (2.01 ± 0.04) mg RUE/g, and (58.12 ± 0.23) mg TAE/g of plant extract respectively. 28.02% ± 0.02% alkaloid and 2.02% ± 0.05% saponins were present in the HH extract. The HH extract showed the anti-oxidant property with IC50 (50% inhibition) of (151.01 ± 0.13) (HH), (79.01 ± 0.04) (Ascorbic acid) for ferric reducing, (91.48 ± 0.13) (HH), (48.02 ± 0.11) (Ascorbic acid) against Ammonium molybdenum, (156.02 ± 0.31) (HH), (52.38 ± 0.21) (Ascorbic acid) against DPPH, 136.01 ± 0.21 (HH), 52.02± 0.31 (Ascorbic acid) against HO, and 154.12 ± 0.03 (HH), (40.05 ± 0.15) (Ascorbic acid) μg/mL against ABTS respectively. Statistical analysis indicated that HH caused a competitive type of inhibition of α-amylase ( remained constant and Km increases from 10.65 to 84.37%) while Glucophage caused the un-competitive type of inhibition i-e both Km and decreased from 40.49 to 69.15% and 38.86 to 69.61% respectively. The , (inhibition constant); , (dissociation constant), , (Michaelis-Menten constant), and IC50 were found to be 62, 364, 68.1, and 38.08 ± 0.22 for HH and 12, 101.05, 195, 34.01 ± 0.21 for Glucophage. Similarly, HH causes an anon-competitive type of inhibition of AChE i-e Km remains constant while decreases from 60.5% to 74.1%. The calculated , , , and IC50 were found to be 32, 36.2, 0.05, and 18.117 ± 0.018.
CONCLUSION
From the current results, it is concluded that HH extract contains bioactive compounds, and could be a good alternative to controlling oxidants, Alzheimer's and Type-II diabetic diseases.
Topics: Antioxidants; alpha-Amylases; Cholinesterase Inhibitors; Acetylcholinesterase; Plant Extracts; Humans; Phytochemicals; Drugs, Chinese Herbal; Enzyme Inhibitors
PubMed: 38767633
DOI: 10.19852/j.cnki.jtcm.2024.03.001 -
FEMS Yeast Research Jan 2023Consolidated bioprocessing (CBP) of starch requires recombinant Saccharomyces cerevisiae strains that produce raw starch-degrading enzymes and ferment the resultant...
Consolidated bioprocessing (CBP) of starch requires recombinant Saccharomyces cerevisiae strains that produce raw starch-degrading enzymes and ferment the resultant sugars to ethanol in a single step. In this study, the native S. cerevisiae COX4 and RPS25A promoter-proximal introns were evaluated for enhanced expression of amylase genes (ateA, temA or temG_Opt) under the control of an S. cerevisiae promoter (ENO1P, TEF1P, TDH3P, or HXT7P). The results showed that different promoters and promoter-intron combinations differentially affected recombinant amylase production: ENO1P-COX4i and TDH3P-RPS25Ai were the best promoters for AteA, followed closely by HXT7P. The latter was also the best promoter for TemA and TemG production, followed closely by TDH3P-RPS25Ai for both these enzymes. Introducing promoter-proximal introns increased amylase activity up to 62% in Y294[ENO-COX-AteA] and Y294[TDH3-RPS-TemA], a significant improvement relative to the intron-less promoters. Strains co-expressing both an α-amylase and glucoamylase genes yielded up to 56 g/L ethanol from 20% w/v raw starch, with a higher carbon conversion observed with strains co-expressing TDH3P-RPS25Ai-temG_Opt than HXT7P-temG_Opt. The study showed that promoter-proximal introns can enhance amylase activity in S. cerevisiae and suggest that these alternative cassettes may also be considered for expression in more efficient ethanol-producing industrial yeast strains for raw starch CBP.
Topics: Saccharomyces cerevisiae; Amylases; Introns; Starch; Ethanol; Fermentation
PubMed: 37891015
DOI: 10.1093/femsyr/foad047 -
Revista Latino-americana de Enfermagem 2021to assess if changes in salivary alpha-amylase activity are associated with anxiety and stress among hospital nursing professionals and whether anxiety and stress are...
OBJECTIVE
to assess if changes in salivary alpha-amylase activity are associated with anxiety and stress among hospital nursing professionals and whether anxiety and stress are associated with sociodemographic, epidemiological, and occupational factors.
METHOD
cross-sectional, quantitative study, carried out with 210 nursing professionals from a hospital. For data collection, we used a questionnaire to characterize workers, Beck's Anxiety Inventory, Lipp's Stress Symptoms Inventory for Adults and samples and saliva samples collected in work shifts. The data were analyzed descriptively and inferentially using the software Statistical Package for the Social Science and GraphPad Prism.
RESULTS
most professionals experienced stress and anxiety. The variables age group, number of children, use of medication and workload were associated with anxiety; age group, smoking and medication use were associated with stress. An increase in the salivary alpha-amylase activity was observed in the middle of the work shift. Professionals who had stress and anxiety had significant changes in alpha-amylase in the night shift.
CONCLUSION
changes in salivary alpha-amylase were associated with anxiety and stress among nursing professionals, indicating that this enzyme can be a possible biomarker of anxiety and stress in workers.
Topics: Adult; Anxiety; Cross-Sectional Studies; Humans; Nurses; Saliva; Salivary alpha-Amylases; Stress, Psychological
PubMed: 34468625
DOI: 10.1590/1518-8345.4859.3468 -
Journal of Cancer Research and... 2023Ectopic production of amylase by tumor cells is known since 1951. Elevated amylase in multiple myeloma (MM) was first described in 1988. It has been postulated that...
BACKGROUND
Ectopic production of amylase by tumor cells is known since 1951. Elevated amylase in multiple myeloma (MM) was first described in 1988. It has been postulated that translocation of chromosome 1, where amylase gene is situated, is responsible for ectopic production from the malignant plasma cells. Anecdotal reports have shown hyperamylasemia in MM to be associated with extensive bone disease, rapid progression, and shorter survival. Serum amylase estimation is a ubiquitous test. This prospective study was conducted to ascertain the degree of elevated amylase, its clinical utility, and implications in MM patients.
MATERIALS AND METHODS
In an 18-month period, all consenting patients with newly diagnosed or relapsed MM were tested for serum amylase levels. The study excluded patients with elevated lipase, abnormal creatinine clearance, and evidence of intestinal obstruction or perforation. Patients with amylase value >100 U/L were designated to have "elevated amylase level" for the purpose of this study.
RESULTS
We enrolled 58 patients with MM, of which 29.3% (n = 17) were found to have elevated serum amylase levels. The median age of patients with elevated amylase was 65 years. The male-to-female ratio was 1.9:1. There was no statistical association between age, gender, type of heavy chain class, light chain, or high-risk cytogenetics. Among patients with the International Staging System (ISS), Stages I, II, and III, 20.8% (n = 5), 31.3% (n = 5), and 41.2% (n = 7) were noted to have elevated amylase levels. A statistically significant association was noted between the presence of extramedullary disease (EMD) and elevated amylase level (P = 0.028). Higher mortality (29.4% versus 17%) and shorter mean survival of (30.2 ± 3.3 months versus 51.7 + 4.9 months) were recorded in patients with elevated amylase levels in comparison to those with normal levels.
CONCLUSIONS
Elevated serum amylase level in MM is indicative of advanced ISS stage, the presence of EMD, higher risk of mortality, and shorter survival. Serum amylase can be used as a cost-effective tool in myeloma management.
Topics: Humans; Male; Female; Aged; Multiple Myeloma; Prognosis; Prospective Studies; Amylases; Plasma Cells
PubMed: 37787288
DOI: 10.4103/jcrt.jcrt_2143_21 -
Aging Cell Aug 2021Recent studies indicate a crucial role for neuronal glycogen storage and degradation in memory formation. We have previously identified alpha-amylase (α-amylase), a...
Recent studies indicate a crucial role for neuronal glycogen storage and degradation in memory formation. We have previously identified alpha-amylase (α-amylase), a glycogen degradation enzyme, located within synaptic-like structures in CA1 pyramidal neurons and shown that individuals with a high copy number variation of α-amylase perform better on the episodic memory test. We reported that neuronal α-amylase was absent in patients with Alzheimer's disease (AD) and that this loss corresponded to increased AD pathology. In the current study, we verified these findings in a larger patient cohort and determined a similar reduction in α-amylase immunoreactivity in the molecular layer of hippocampus in AD patients. Next, we demonstrated reduced α-amylase concentrations in oligomer amyloid beta 42 (Aβ ) stimulated SH-SY5Y cells and neurons derived from human-induced pluripotent stem cells (hiPSC) with PSEN1 mutation. Reduction of α-amylase production and activity, induced by siRNA and α-amylase inhibitor Tendamistat, respectively, was further shown to enhance glycogen load in SH-SY5Y cells. Both oligomer Aβ stimulated SH-SY5Y cells and hiPSC neurons with PSEN1 mutation showed, however, reduced load of glycogen. Finally, we demonstrate the presence of α-amylase within synapses of isolated primary neurons and show that inhibition of α-amylase activity with Tendamistat alters neuronal activity measured by calcium imaging. In view of these findings, we hypothesize that α-amylase has a glycogen degrading function within synapses, potentially important in memory formation. Hence, a loss of α-amylase, which can be induced by Aβ pathology, may in part underlie the disrupted memory formation seen in AD patients.
Topics: Alzheimer Disease; Amyloid beta-Peptides; Animals; Glycogenolysis; Humans; Male; Mice; alpha-Amylases
PubMed: 34261192
DOI: 10.1111/acel.13433 -
Ulusal Travma Ve Acil Cerrahi Dergisi =... Dec 2022Acute pancreatitis (AP) is inflammation of pancreas in which pancreas enzymatic activity is increased. Parasym-pathetic innervation of pancreas plays an important role...
BACKGROUND
Acute pancreatitis (AP) is inflammation of pancreas in which pancreas enzymatic activity is increased. Parasym-pathetic innervation of pancreas plays an important role in several functions of pancreas. Botulinum toxin (BTx) might be a tool to suppress the pancreas activity in AP.
METHODS
In the preliminary experimental study, BTx (15U/kg) was administered directly and intraductal ways. After 10 days, blood amylase, lipase, trypsinogen, insulin, and glucagon levels were compared and no significant difference was seen between groups. Intraductal BTx administration is preferred for experimental AP model in rats; control, AP, intraductal BTx, and AP with Intraductal BTx (AP+BTx). AP was created by intraperitoneal injection of cerulean 20 µg/kg/injection (5 times). After 24 h, serum amylase, lipase, IL-6, IL-1β, TNF-α, and IL-10 were measured and pancreas tissue was evaluated for inflammation and necrosis.
RESULTS
Mean serum amylase, lipase IL-6, IL-1β, and TNF-α levels of the AP group were significantly higher compared to the other groups (p<0.05). However, there was no significant difference between the amylase and lipase levels of control, BTx, and AP+BTx groups. Serum insulin and glucagon levels in AP group were significantly higher than control and BTx groups (p<0.05). However, there is no significant difference between the insulin and glucagon levels of AP and AP+BTx groups. in pathological evaluation. In AP+ BTx group, there is less amount of centrilobular necrosis and there is mild inflammation and hyperplasia of pancreatic duct epithelium.
CONCLUSION
Administration of intraductal BTx suppressed the AP without making significant suppression in endogenous activity of pancreas.
Topics: Animals; Rats; Pancreatitis; Tumor Necrosis Factor-alpha; Acute Disease; Glucagon; Interleukin-6; Inflammation; Amylases; Necrosis; Lipase; Botulinum Toxins; Insulins
PubMed: 36453789
DOI: 10.14744/tjtes.2021.90140 -
Frontiers in Bioscience (Landmark... Oct 2023Tobacco use by youth is ever-demanding, and it is increasingly distributed not only in India but also globally. Saliva is a complex oral bio-fluid, freely available,... (Observational Study)
Observational Study
BACKGROUND
Tobacco use by youth is ever-demanding, and it is increasingly distributed not only in India but also globally. Saliva is a complex oral bio-fluid, freely available, performing absolute tasks for maintaining oral health and homeostasis. It contains a plethora of significant constituents such as proline-rich proteins (PRPs), immunoglobulins, IgA, enzymes lysozyme, lactoferrin, peroxidases, amylase, etc. The basic ecological balance of the oral cavity is stabilized via salivary clearance by reduced aggregation and adherence of microorganisms by direct microbial activity. This balance of oral activity is also done by indirect mechanisms by immunological as well as non-immunological means and also by effectively regulating salivary pH flow rate. This institutional observational study was planned to assess and compare salivary parameters (pH, salivary flow rate), total proteins, α-amylase, calcium, phosphate, and IgA, of unstimulated whole saliva of both tobacco abusers and tobacco non-users.
METHODS
The Study consisted of 270 participants (Tobacco habit) group, n = 135 and Control (Healthy) group, n = 135 and were in the age range of 20-50 years. They were assessed for oral health status, followed by the analysis of salivary pH, flow rate, total proteins, amylase, calcium, phosphates, and IgA of unstimulated whole saliva.
RESULTS
Comparative evaluation of salivary parameters among groups found that varying tobacco abusers had increased salivary amylase, protein levels, and phosphate whereas decreased salivary pH, flow rate, IgA, and in the whole unstimulated saliva samples than those of non-tobacco users. This difference among groups was statistically significant. ( < 0.05), and calcium levels were not altered significantly.
CONCLUSIONS
This study concludes that salivary parameters are altered in tobacco abusers when compared to those of non-abusers, and it was more significant in smokeless tobacco abusers than in any other form of tobacco abuse.
Topics: Adolescent; Humans; Young Adult; Adult; Middle Aged; Calcium; Salivary Proteins and Peptides; Immunoglobulin A; Amylases; Phosphates
PubMed: 37919053
DOI: 10.31083/j.fbl2810263 -
Food Research International (Ottawa,... Jul 2022The relation between contamination by trichothecenes, DON (Deoxyvalenol) and 15-ADON (15-acetil-deoxyvalenol), and enzymes, protease, β-amylase and α-amylase, in the...
The relation between contamination by trichothecenes, DON (Deoxyvalenol) and 15-ADON (15-acetil-deoxyvalenol), and enzymes, protease, β-amylase and α-amylase, in the mashing step was studied. Malted barley was subject to mashing at three temperature ramps, which resulted in enzyme extracts. Enzyme activity of the extract was evaluated in a model solution with DON and 15-ADON. Results indicated that activities of protease and β-amylase are changed by trichothecenes. Reduction in 15-ADON concentration was 100% when the initial concentration was 0.23 µg mL and 74, 72 and 92% when it was 0.85 µg mL, under activities of protease, β-amylase and α-amylase, respectively. On the other hand, DON concentration increased 45 and 30% under protease and β-amylase activities, respectively. Malt contamination by DON and 15-ADON can affect enzyme activity and modify the process yield, which may cause economic losses.
Topics: Mycotoxins; Peptide Hydrolases; Trichothecenes; alpha-Amylases; beta-Amylase
PubMed: 35761607
DOI: 10.1016/j.foodres.2022.111317 -
International Journal of Molecular... Jul 2022PLG-007 is a developmental therapeutic compound that has been clinically shown to reduce the magnitude of postprandial glucose excursions and has the potential to be an...
PLG-007 is a developmental therapeutic compound that has been clinically shown to reduce the magnitude of postprandial glucose excursions and has the potential to be an adjunct treatment for diabetes and inflammatory-related diseases. The present investigation is aimed at understanding the molecular mechanism of action of PLG-007 and its galactomannan (GM) components GMα and GMβ (in a 1:4 mass ratio, respectively) on enzyme (i.e., α-amylase, maltase, and lactase) hydrolysis of glucose polymers using colorimetric assays and C HSQC NMR spectroscopy. The starch-iodine colorimetric assay indicated that GMα strongly inhibits α-amylase activity (~16-fold more potent than GMβ) and thus is the primary active component in PLG-007. C HSQC experiments, used to follow the α-amylase-mediated hydrolysis of starch and amylopectin, further demonstrate the α-amylase inhibitory effect of GMα via α-amylase-mediated hydrolysis of starch and amylopectin. Maltohexaose (MT6) was used to circumvent the relative kinetic complexity of starch/amylopectin degradation in Michaelis-Menten analyses. The V, K, and K parameters were determined using peak volume integrals from C HSQC NMR spectra. In the presence of PLG-007 with α-amylase and MT6, the increase in K from 7.5 ± 0.6 × 10 M (control) to 21 ± 1.4 × 10 M, with no significant change in V, indicates that PLG-007 is a competitive inhibitor of α-amylase. Using K values, K was estimated to be 2.1 ± 0.9 × 10 M; however, the microscopic K value of GMα is expected to be larger as the binding stoichiometry is likely to be greater than 1:1. Colorimetric assays also demonstrated that GMα is a competitive inhibitor of the enzymes maltase and lactase. Overall, this study provides insight as to how PLG-007 (GMα) is likely to function in vivo.
Topics: Amylopectin; Galactose; Glucose; Hydrolysis; Lactase; Mannans; Starch; alpha-Amylases; alpha-Glucosidases
PubMed: 35887087
DOI: 10.3390/ijms23147739