Effect of Selenium Supplementation on Serum Amylase, Lactate Dehydrogenase and Alkaline Phosphatase Activities in Rats Exposed to Cadmium Or Lead

Total Page:16

File Type:pdf, Size:1020Kb

Effect of Selenium Supplementation on Serum Amylase, Lactate Dehydrogenase and Alkaline Phosphatase Activities in Rats Exposed to Cadmium Or Lead EFFECT OF SELENIUM SUPPLEMENTATION ON RATS EXPOSED TO CADMIUM OR LEAD Cercetări Agronomice în Moldova Vol. XLVII , No. 4 (160) / 2014 EFFECT OF SELENIUM SUPPLEMENTATION ON SERUM AMYLASE, LACTATE DEHYDROGENASE AND ALKALINE PHOSPHATASE ACTIVITIES IN RATS EXPOSED TO CADMIUM OR LEAD B.G. ŞLENCU1*, C. CIOBANU1, Carmen SOLCAN 2, Alina ANTON2, St. CIOBANU2, Gh. SOLCAN2, Rodica CUCIUREANU1 *E-mail: [email protected] Received June 13, 2014 ABSTRACT. The purpose of the study was Selenium, coadministered with cadmium, to assess the effect of selenium caused a marked increase in serum LDH supplementation on serum amylase, lactate activity, when compared to cadmium alone dehydrogenase (LDH) and alkaline or Control group while practically it had no phosphatase (ALP) activities in rats, during effect on lead induced changes in LDH subacute exposure to toxic doses of activity. Cadmium and lead induced cadmium or lead through the drinking disturbances in serum ALP activity were not water. The experimental groups (n=6) were: influenced by selenium supplementation. Control, Se (Se+4: 0,2 mg/l), Cd (Cd+2: 150 mg/l), Pb (Pb+2: 300 mg/l), Cd+Se (Cd+2: Key words: Rats; Lead; Cadmium; 150 mg/l; Se+4: 0,2 mg/l) and Pb+Se (Pb+2: Selenium; Blood serum enzyme. 300 mg/l; Se+4: 0,2 mg/l). The animals were sacrificed after 56 days. Amylase, LDH and REZUMAT. Efectul suplimentării cu ALP activities were determined from serum. seleniu asupra activităţii amilazei serice, Se and Pb treatments caused an increase in a lactat dehidrogenazei şi a fosfatazei amylase and LDH activities, when alcaline la sobolani, expuşi la cadmiu sau compared to Control group while Cd caused plumb. Scopul acestui studiu a fost de a an increase in amylase activity and a evalua efectul suplimentării cu seleniu decrease in LDH and ALP activities. Cd+Se asupra unor enzime, amilaza, lactat caused a decrease in amylase activity and an dehidrogenaza (LDH) şi fosfataza alcalină increase in LDH activity, when compared to (ALP) la şobolani, în timpul expunerii Cd. Pb+Se caused a decrease in amylase subacute la doze toxice de cadmiu sau activity in comparison to lead. Selenium plumb, prin intermediul apei de bǎut. supplementation alleviated cadmium or lead Loturile experimentale (n=6) au fost: +4 +2 induced changes in serum amylase activity. Martor, Se (Se : 0,2 mg/l), Cd (Cd : 150 1 “Grigore T. Popa” University of Medicine and Pharmacy, School of Pharmacy, Iaşi, Romania 2 “Ion Ionescu de la Brad” University of Agricultural Sciences and Veterinary Medicine, School of Veterinary Medicine, Iaşi, Romania 113 B.G. ŞLENCU et al. mg/l), Pb (Pb+2: 300 mg/l), Cd+Se (Cd+2: of glutathione and sulfhydryl groups, 150 mg/l; Se+4: 0,2 mg/l) şi Pb+Se (Pb+2: +4 resulting in the enhanced production 300 mg/l; Se : 0,2 mg/l). Animalele au fost of various reactive oxygen species sacrificate dupǎ 56 de zile. Amilaza, LDH şi ALP au fost determinate din ser. (ROS) such as superoxide ion, Administrarea de Se sau Pb a determinat o hydrogen peroxide and hydroxyl creştere a amilazei şi LDH, în comparaţie cu radicals (Liu et al., 2009). lotul de control, în timp ce Cd a determinat Lead (Pb) is a toxic metal, which o creştere a amilazei şi o scǎdere a LDH şi can induce various behavioral, ALP. Cd+Se au cauzat o scǎdere a amilazei biochemical, haematological and şi o creştere a LDH, în comparaţie cu Cd. Pb+Se au produs o reducere amilazei, în histological disorders, both in humans comparaţie cu plumbul. Suplimentarea cu and animals (Ciobanu et al., 2012). seleniu a atenuat modificǎrile induse de The most deleterious effects have cadmiu sau plumb asupra amilazei serice. been observed on the haemopoietic, Seleniul, coadministrat cu cadmiul, a cauzat nervous, reproductive and renal o creştere marcantă a activitǎţii serice a systems (Papanikolaou et al., 2005). LDH, în comparaţie cu Cd sau lotul martor, One of the main toxicodynamic însǎ nu a avut nici un efect asupra modificǎrilor produse de plumb asupra mechanisms involved in Pb toxicity is activitǎţii LDH. Tulburǎrile induse de the generation of reactive oxygen cadmiu şi plumb asupra activitǎţii serice a species (ROS) (Ercal et al., 2001). ALP nu au fost influenţate de suplimentarea Amylase (α-amylase) is a cu seleniu. glycoside hydrolase involved in carbohydrate digestion. Lactate Cuvinte cheie: şobolani; plumb; cadmiu; selenium; enzime serice. dehydrogenase is an oxidoreductase with important roles in carbohydrate INTRODUCTION metabolism; in mammals it has five main isoforms. Alkaline phosphatase Selenium (Se) is an essential is a hydrolase involved in microelement with multiple dephosphorylation (Murray et al., physiological roles. It is a component 2003). of several selelenoenzymes with Selenium exerts protective important functions in the body. The effects against cadmium or lead most important selenoenzymes are the toxicity (Reilly, 2006; Newairy et al., glutathione peroxidases, deiodinases 2007; Othman et Missiry, 1998). and thioredoxin reductases (Navarro There is insufficient and/or Alarcon et Cabrera-Vique, 2008; inconclusive data regarding the effects Hatfield et al., 2006). In high doses, of cadmium or lead and the selenium compounds can be toxic concurrent administration of selenium (Reilly, 2006). on serum amylase, lactate Cadmium (Cd) is a toxic metal. dehydrogenase and alkaline It is a potent carcinogen in multiple phosphatase activities. types of tissues. It has been suggested The objective of this study was that Cd toxicity involves the depletion to assess the effect of selenium 114 EFFECT OF SELENIUM SUPPLEMENTATION ON RATS EXPOSED TO CADMIUM OR LEAD supplementation on serum amylase, Selenium (Se+4), cadmium (Cd+2) lactate dehydrogenase and alkaline and lead (Pb+2) were added in the drinking phosphatase activities during subacute water by dissolving sodium selenite exposure to toxic doses of cadmium pentahydrate (Sigma Aldrich), lead or lead through the drinking water, acetate trihydrate (Chemical Company, Romania) and cadmium chloride using a rat experimental model. hemipentahydrate (Chemical Company, Romania). The water dispensers were MATERIALS AND METHODS emptied and refilled everyday and the unconsumed volumes of water were All experimental procedures were measured. conducted according to the The experimental groups were: recommendations set up by 86/609/EEC Control, Se (Se+4: 0,2 mg/l), Cd (Cd+2: directive and other applicable regulations. 150 mg/l), Pb (Pb+2: 300 mg/l), Cd+Se The study protocol was approved by The (Cd+2: 150 mg/l; Se+4: 0,2 mg/l) and Ethics Committee for Research of Pb+Se (Pb+2: 300 mg/l; Se+4: 0,2 mg/l). “Grigore T. Popa” University of Medicine The weight of the animals was and Pharmacy of Iaşi, Romania. measured every 7 days. The experiment A total of 36 male Wistar rats lasted for 56 days. The mean intake of (initial body weight: 250-400 g) were elements reported to body weight (Table randomly divided in six groups (n=6) and 1) was approximated based on the daily each group was kept in a single collective water consumption of each group, the cage, maintained in relative constant cumulative body weights and the environmental conditions (temperature 18 concentration of the elements in the o - 25 C, light/dark cycle: 12 h/12 h) and drinking water. had free access to water and dry feed. Table 1 - Estimation of the mean approximate intake of selenium, cadmium and lead throughout the experiment Se+4 Cd+2 Pb+2 Group (μg/kg b.w.) (mg/kg b.w.) (mg/kg b.w.) Control - - - Se 15,48±0,42 - - Cd - 10,48±0,41 - Pb - - 25,34±0,68 Cd+Se 9,81±0,30 7,36±0,23 - Pb+Se 15,90±0,43 - 23,84±0,64 Values are mean ± standard deviation The animals were narcotized with anticoagulant by cardiac puncture. Serum 100 mg/kg b.w. of ketamine (injectable was obtained by centrifugation, after solution for veterinary use, administered coagulation. Serum activities of amylase, intraperitoneally) and euthanized at the alkaline phosphatase (ALP) and lactate end of the experiment. Blood was dehydrogenase (LDH) were determined collected in vacutainers without 115 B.G. ŞLENCU et al. using an Accent 200 biochemical analyzer activity, compared to Control group (Cormay, Poland) and specific assay kits. and, respectively, Cd or Pb (Fig. 1). Microsoft Office Excel 2007 with The amount of amylase from Data Analysis add-on was used for serum reflects the balance between statistical processing of experimental the rates of amylase entry and its data. The results are expressed as mean ± standard error of the mean (SEM). A subsequent removal from the blood. paired Student’s t-test was used (p < 0,05 The pancreas and the salivary glands was considered significant). usually account for almost all of the serum amylase, in normal conditions. RESULTS AND DISCUSSION Hyperamylasemia can be the result of an increased rate of entry into the All three Se, Cd and Pb blood or a decreased rate of clearance. treatments produced an increase in Pancreatic lesions or inflammation serum amylase activity, the highest can cause hyperamylasemia. A being observed in the Se group. decreased rate of clearance, due to Selenium supplementation of rats renal impairment, can also cause exposed to cadmium or lead resulted hyperamylasemia (Solcan et al., in a decrease in serum amylase 2005). Figure 1 - Serum amylase activity. Error bars are SEM; ■ = significantly different compared to Control group (p<0,05); □ = significantly different compared to Se (p<0,05); ● = significantly different compared to Cd (p<0,05); ▲ = significantly different compared to Pb (p<0,05) Pancreatitis has many specificity in the diagnosis of ethiopathogenic causes. Intoxication pancreatitis, but is routinely used for with various organic or inorganic this purpose, together with amylase substances can be a cause (Khurana et and other markers (Yadav et al., Barkin, 2001; Reed et Gorelick, 2002).
Recommended publications
  • Characterization of Prebiotics and Their Synergistic Activities with Lactobacillus Probiotics for Β-Glucuronidase Reduction
    ESEARCH ARTICLE R ScienceAsia 45 (2019): 538–546 doi: 10.2306/scienceasia1513-1874.2019.45.538 Characterization of prebiotics and their synergistic activities with Lactobacillus probiotics for β-glucuronidase reduction a, a b a Achara Chaiongkarn ∗, Jirapa Dathong , Wipaporn Phatvej , Premsuda Saman , Chutima Kuanchaa, Lawan Chatanona, Somporn Moonmungmeea a Biodiversity Research Center, Thailand Institute of Scientific and Technological Research, Pathum Thani 12120 Thailand b Expert Center of Innovative Herbal Products, Thailand Institute of Scientific and Technological Research, Pathum Thani 12120 Thailand ∗Corresponding author, e-mail: [email protected] Received 1 Jun 2018 Accepted 28 Oct 2019 ABSTRACT: The role of synbiotics for enriching health and well-being in addition to suppressing disease is gaining interest. Synergistic activities of four candidate prebiotics as exopolysaccharides (EPSs) derived from Lactobacillus fer- mentum TISTR 2514 (EPS-TISTR 2514), Pediococcus acidilactici TISTR 2612 (EPS-TISTR 2612), manno-oligosaccharides and rice syrup-oligosaccharides were characterized and evaluated for decreasing the risk of colorectal cancer (CRC). Results revealed that one or more candidate prebiotics stimulated the growth of Lactobacillus casei DSM 20011, Lactobacillus plantarum DSM 2648, and Lactobacillus rhamnosus DSM 20021 by at least two orders of magnitude higher than positive control (using FOS as carbon source) within 24 h in vitro. Simulated gastrointestinal (pH 1) and α-amylase (pH 7) resistance were tested. Results showed more than 75% remaining after incubation at 37 °C after 6 h for all treatments except rice syrup. L. plantarum DSM 2648 + manno-oligosaccharides (Tr.1), L. plantarum DSM 2648 + EPS-TISTR 2612 (Tr.2), L. rhamnosus DSM 20021 + rice syrup-oligosaccharides (Tr.3), L.
    [Show full text]
  • Isolated Co-Lipase Deficiency in Two Brothers
    Gut: first published as 10.1136/gut.23.3.243 on 1 March 1982. Downloaded from Gut, 1982, 23, 243-246 Case reports Isolated co-lipase deficiency in two brothers H HILDEBRAND,* B BORGSTROM, A BEKASSY, C ERLANSON-ALBERTSSON, AND I HELIN From the Department ofPaediatrics and the Department ofPhysiological Chemistry, University ofLund, Sweden SUMMARY Two normally developed Assyrian brothers with isolated pancreatic co-lipase deficiency are described. They presented at the age of 5-6 years with loose stools. They had steatorrhoea, and analysis of exocrine pancreatic enzymes in the small intestine showed co-lipase deficiency, while amylase, chymotrypsin, trypsin, and lipase were normal. Intraduodenal infusion of purified co-lipase improved fat digestion measured by the triolein breath test. Their steatorrhoea diminished on treatment with enteric-coated pancreatic enzymes. The first indication for the existence of a co-factor for activities were assayed titrimetrically`5 using p-tosyl-l- pancreatic lipase was reported in 1963.1 In 1969 a arginine methyl ester (TAME) and N-acetyl-L-tyro- heat-stable co-factor was separated from lipase by gel- sine ethyl ester (ATEE), respectively, as substrates. filtration.2 Pure pancreatic lipase is inhibited by bile Lipase and co-lipase were measured titrimetrically salts in concentrations over their critical micellar con- using tributyrate as substrate.4 Total bile salt concen- centrations.3 The function of the co-factor, called co- trations and the ratio of glycine- to taurine-conjugated lipase, is to restore
    [Show full text]
  • K113436 B. Purpose for Submi
    510(k) SUBSTANTIAL EQUIVALENCE DETERMINATION DECISION SUMMARY ASSAY ONLY TEMPLATE A. 510(k) Number: k113436 B. Purpose for Submission: New device C. Measurand: Alkaline Phosphatase, Amylase, and Lactate Dehydrogenase D. Type of Test: Quantitative, enzymatic activity E. Applicant: Alfa Wassermann Diagnostic Technologies, LLC F. Proprietary and Established Names: ACE Alkaline Phosphatase Reagent Amylase Reagent ACE LDH-L Reagent G. Regulatory Information: Product Classification Regulation Section Panel Code CJE II 862.1050, Alkaline phosphatase 75-Chemistry or isoenzymes test system CIJ II 862.1070, Amylase test system 75-Chemistry CFJ II, exempt, meets 862.1440, Lactate 75-Chemistry limitations of dehydrogenase test system exemption. 21 CFR 862.9 (c) (4) and (9) H. Intended Use: 1. Intended use(s): See indications for use below. 2. Indication(s) for use: The ACE Alkaline Phosphatase Reagent is intended for the quantitative determination of alkaline phosphatase activity in serum using the ACE Axcel Clinical Chemistry System. Measurements of alkaline phosphatase are used in the diagnosis and treatment of liver, bone, parathyroid and intestinal diseases. This test is intended for use in clinical laboratories or physician office laboratories. For in vitro diagnostic use only. The ACE Amylase Reagent is intended for the quantitative determination α-amylase activity in serum using the ACE Axcel Clinical Chemistry System. Amylase measurements are used primarily for the diagnosis and treatment of pancreatitis (inflammation of the pancreas). This test is intended for use in clinical laboratories or physician office laboratories. For in vitro diagnostic use only. The ACE LDH-L Reagent is intended for the quantitative determination of lactate dehydrogenase activity in serum using the ACE Axcel Clinical Chemistry System.
    [Show full text]
  • Extrapancreatic Sources of Lipase
    Clinical Chemistry Byline David Parry, PhD, FCACB St. Boniface General Hospital James Dalton, PhD, FCACB Health Sciences Centre Extrapancreatic Sources of Lipase Reports now abound in the literature indicating that serum lipase is more specific and sensitive than amylase for detecting acute pancreatitis in patients presenting with acute abdominal pain (1-7). Amylase has been the mainstay biochemical test for the investigation of acute pancreatitis for many years, whereas lipase has not been widely used primarily because, until recently, reliable lipase assays were not suitable for rapid turnaround of results. Now, reliable and rapid lipase results are available at HSC, St. Boniface General Hospital, Seven Oaks General Hospital and Grace General Hospital. It is generally well appreciated that increases in serum amylase are seen not only in pancreatic disorders, but also in a number of non-pancreatic abdominal and non-abdominal diseases (1). With increased use of lipase, it has become increasingly recognized that lipase too can be elevated in clinical conditions that do not involve the pancreas. Even though the superiority of lipase over amylase for investigating acute pancreatitis has been shown repeatedly in recent literature (2-5), it is important to be aware that there are a number of clinical conditions that can give rise to elevated nonpancreatic lipase: 1) A recent study (2) has shown that some patients presenting with acute abdominal pain have elevations in serum lipase that are due to extrapancreatic disease processes. The sources of elevated lipase were attributed to a number of intra-abdominal anatomic locations other than the pancreas, including the biliary tract, esophagus, stomach, duodenum and small intestine.
    [Show full text]
  • Diagnostic Value of Serum Enzymes-A Review on Laboratory Investigations
    Review Article ISSN 2250-0480 VOL 5/ ISSUE 4/OCT 2015 DIAGNOSTIC VALUE OF SERUM ENZYMES-A REVIEW ON LABORATORY INVESTIGATIONS. 1VIDYA SAGAR, M.SC., 2DR. VANDANA BERRY, MD AND DR.ROHIT J. CHAUDHARY, MD 1Vice Principal, Institute of Allied Health Sciences, Christian Medical College, Ludhiana 2Professor & Ex-Head of Microbiology Christian Medical College, Ludhiana 3Assistant Professor Department of Biochemistry Christian Medical College, Ludhiana ABSTRACT Enzymes are produced intracellularly, and released into the plasma and body fluids, where their activities can be measured by their abilities to accelerate the particular chemical reactions they catalyze. But different serum enzymes are raised when different tissues are damaged. So serum enzyme determination can be used both to detect cellular damage and to suggest its location in situ. Some of the biochemical markers such as alanine aminotransferase, aspartate aminotransferase, alkaline phasphatase, gamma glutamyl transferase, nucleotidase, ceruloplasmin, alpha fetoprotein, amylase, lipase, creatine phosphokinase and lactate dehydrogenase are mentioned to evaluate diseases of liver, pancreas, skeletal muscle, bone, etc. Such enzyme test may assist the physician in diagnosis and treatment. KEYWORDS: Liver Function tests, Serum Amylase, Lipase, CPK and LDH. INTRODUCTION mitochondrial AST is seen in extensive tissue necrosis during myocardial infarction and also in chronic Liver diseases like liver tissue degeneration DIAGNOSTIC SERUM ENZYME and necrosis². But lesser amounts are found in Enzymes are very helpful in the diagnosis of brain, pancreas and lung. Although GPT is plentiful cardiac, hepatic, pancreatic, muscular, skeltal and in the liver and occurs only in the small amount in malignant disorders. Serum for all enzyme tests the other tissues.
    [Show full text]
  • Inflammatory Mediators in Human Acute Pancreatitis
    546 Gut 2000;47:546–552 Inflammatory mediators in human acute pancreatitis: clinical and pathophysiological Gut: first published as 10.1136/gut.47.4.546 on 1 October 2000. Downloaded from implications J Mayer, B Rau, F Gansauge, H G Beger Abstract sources during the course of the disease.1 Background—The time course and rela- Studies on AP have demonstrated that these tionship between circulating and local mediators are produced in a variety of tissues in cytokine concentrations, pancreatic in- a predictable sequence, initiated by local flammation, and organ dysfunction in release of proinflammatory mediators such as acute pancreatitis are largely unknown. interleukin (IL)-1â, IL-6, and IL-8, which Patients and methods—In a prospective induce a systemic inflammatory response clinical study, we measured the pro- reflected by increased levels of soluble inter- inflammatory cytokines interleukin (IL)- leukin 2 receptor (sIL-2R), neopterin, or 1â, IL-6 and IL-8, the anti-inflammatory tumour necrosis factor á (TNF-á). This results cytokine IL-10, interleukin 1â receptor in inflammatory infiltration of distant organs antagonist (IL-1RA), and the soluble IL-2 with multiorgan failure and death.1 receptor (sIL-2R), and correlated our The systemic inflammatory response is kept findings with organ and systemic compli- at bay by local and systemic release of anti- cations in acute pancreatitis. In 51 pa- inflammatory mediators such as interleukin 1â tients with acute pancreatitis admitted receptor antagonist (IL-1RA) and IL-10 which within 72 hours after the onset of symp- were shown to reduce the severity of pancreatitis 2–5 toms, these parameters were measured and pancreatitis associated organ failure.
    [Show full text]
  • IDH1R132H Mutation Inhibits the Proliferation and Glycolysis of Glioma Cells by Regulating the HIF- 1Α/LDHA Pathway
    IDH1R132H Mutation Inhibits the Proliferation and Glycolysis of Glioma Cells by Regulating the HIF- 1α/LDHA Pathway Hailong Li PLAGH: Chinese PLA General Hospital Shuwei Wang Chinese PLA General Hospital Yonggang Wang ( [email protected] ) Beijing Tiantan Hospital https://orcid.org/0000-0002-8412-9244 Research Keywords: cell metabolism, glycolysis, isocitrate dehydrogenase, signal pathway, tumorgenesis Posted Date: March 15th, 2021 DOI: https://doi.org/10.21203/rs.3.rs-299422/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/19 Abstract Background: This study aims to explore the role and underlying mechanism of the IDH1R132H in the growth, migration, and glycolysis of glioma cells. Methods: The alternation of IDH1, HIF-1α, and LDHA genes in 283 LGG sample (TCGA LGG database) was analyzed on cBioportal. The expression of these three genes in glioma tissues with IDH1R132H mutation or IDH1 wild type (IDH1-WT) and normal brain tissues was also assessed using immunohistochemistry assay. In addition, U521 glioma cells were transfected with IDH1-WT or IDH1R132H to explore the role of IDH1 in the proliferation and migration of glioma cells in vitro. Cell growth curve, Transwell mitigation assay, and assessment of glucose consumption and lactate production were conducted to evaluate the proliferation, migration, and glycolysis of glioma cells. Results: The expression of HIF-1α and LDHA in IDH1R132H mutant was signicantly lower than that in glioma cells with wild type IDH1 (P<0.05). IDH1R132H inhibited the proliferation and glycolysis of U521 glioma cells. Conclusion: The IDH1 mutation IDH1R132H plays an important role in the occurrence and development of glioma through inhibiting the expression of HIF-1α and glycolysis.
    [Show full text]
  • 21 CFR Ch. I (4–1–10 Edition) § 862.1440
    § 862.1440 21 CFR Ch. I (4–1–10 Edition) intended to identify ketones in urine Lactic acid measurements that evalu- and other body fluids. Identification of ate the acid-base status are used in the ketones is used in the diagnosis and diagnosis and treatment of lactic aci- treatment of acidosis (a condition dosis (abnormally high acidity of the characterized by abnormally high acid- blood). ity of body fluids) or ketosis (a condi- (b) Classification. Class I (general con- tion characterized by increased produc- trols). The device is exempt from the tion of ketone bodies such as acetone) premarket notification procedures in and for monitoring patients on subpart E of part 807 of this chapter ketogenic diets and patients with dia- subject to § 862.9. betes. (b) Classification. Class I (general con- [52 FR 16122, May 1, 1987, as amended at 65 trols). The device is exempt from the FR 2307, Jan. 14, 2000] premarket notification procedures in § 862.1455 Lecithin/sphingomyelin subpart E of part 807 of this chapter ratio in amniotic fluid test system. subject to § 862.9. (a) Identification. A lecithin/ [52 FR 16122, May 1, 1987, as amended at 65 sphingomyelin ratio in amniotic fluid FR 2307, Jan. 14, 2000] test system is a device intended to § 862.1440 Lactate dehydrogenase test measure the lecithin/sphingomyelin system. ratio in amniotic fluid. Lecithin and sphingomyelin are phospholipids (fats (a) Identification. A lactate dehydro- or fat-like substances containing phos- genase test system is a device intended phorus). Measurements of the lecithin/ to measure the activity of the enzyme sphingomyelin ratio in amniotic fluid lactate dehydrogenase in serum.
    [Show full text]
  • Observation and Identification of Lactate Dehydrogenase Anomaly in a Postburn Patient Postgrad Med J: First Published As on 5 August 2004
    481 ORIGINAL ARTICLE Observation and identification of lactate dehydrogenase anomaly in a postburn patient Postgrad Med J: first published as on 5 August 2004. Downloaded from Z-J Liu, Y Zhang, X-B Zhang, X Yang ............................................................................................................................... Postgrad Med J 2004;80:481–483. doi: 10.1136/pgmj.2003.015420 See end of article for authors’ affiliations Objective: Lactate dehydrogenase (LDH) anomaly is one of the macroenzymes. Macroenzymes are ....................... enzymes in serum that have formed high molecular mass complexes, either by self polymerisation or by Correspondence to: association with other serum components. The aim of this study was to identify the properties of LDH Professor Ze-Jun Liu, anomaly and observe the changes from admission to discharge in a postburn patient with LDH anomaly in Department of Laboratory Medicine, Southwest his serum. Hospital, Third Military Methods: LDH isoenzymes of the serum were electrophoretically fractionated with terylene cellulose Medical University, acetate supporting media; LDH anomaly was identified by counter immunoelectrophoresis. Chongqing 400038 Peoples’ Republic of Results: An abnormal LDH-4 band and an extra band on the cathode of LDH-5 were observed in the China; a65424208@ serum of this patient and were found to be part of an LDH-IgG complex. As his symptoms improved, the online.cq.cn patient’s LDH anomaly gradually disappeared. The appearance and disappearance of the anomaly seemed to be related to the progression of the patient’s burns. Submitted 26 September 2003 Conclusion: In clinical practice, it is important to keep in mind the possibility of an LDH anomaly in patients Accepted 30 October 2003 when the LDH level is abnormally high or does not seem to be related to the clinical state.
    [Show full text]
  • D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance (NAD Binding/Lactate Dehydrogenase/X-Ray Crystallography)
    Proc. Nat. Acad. Sci. USA Vol. 70, No. 11, pp. 3052-3054, November 1973 D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance (NAD binding/lactate dehydrogenase/x-ray crystallography) MANFRED BUEHNER*, GEOFFREY C. FORD, DINO MORAS, KENNETH W. OLSEN, AND MICHAEL G. ROSSMANNt Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907 Communicated by Dr. William N. Lipscomb, July 6, 1973 ABSTRACT A 3.0-A resolution electron density map orientation of the mutually perpendicular molecular 2-fold of lobster glyceraldehyde-3-phosphate dehydrogenase axes within the unit cell had been established by Rossmann (EC 1.2.1.12) was computed. The essentially single iso- morphous replacement map was very substantially im- et al. (11) using the rotation function (12). This knowledge, proved by averaging subunits. NAD binds in an open con- along with the accurate data obtained from an Optronics formation at sites close to subunit interfaces. The coen- Film Scanner (13), enabled us to solve the difference Patter- zyme binding portion of the enzyme has almost the same son function of the K2HgI4 heavy-atom derivative for its fold as the corresponding portion of lactate dehydro- major set of four sites. This in turn genase (EC 1.1.1.27). The presence of this structure in the permitted determination of five enzymes, analyzed so far, that use nucleotide co- the other heavy-atom sites in all derivatives by difference enzymes might indicate a fundamental primordial struc- Fourier methods, to give three chemically independent sites tural element. per polypeptide chain. The 3.0-A electron density map, which was essentially D-Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) phased by single isomorphous replacement (14), was re- catalyzes the NAD-mediated oxidative phosphorylation of oriented by means of a skew plane program (15) so that the its substrate to D-1,3-diphosphoglyceric acid.
    [Show full text]
  • Pancreatic Amylase and Lipase Plasma Concentrations Are
    Diabetes Care Volume 38, May 2015 e71 Pancreatic Amylase and Lipase Plasma David P. Sonne,1 Tina Vilsbøll,1 and Filip K. Knop1,2 Concentrations Are Unaffected by Increments in Endogenous GLP-1 Levels Following Liquid Meal Tests Diabetes Care 2015;38:e71–e72 | DOI: 10.2337/dc14-2751 Recent findings have suggested that amylase and lipase in plasma following patients with type 2 diabetes (P , incretin-based therapies promote pan- the ingestion of oral glucose and three 0.05), whereas lipase concentrations creatic inflammation and possibly cell isocaloric and isovolemic liquid mealsd were similar. Neither of the enzymes proliferation within the endocrine and all of which exerted normal endogenous increased following nutrient ingestion, exocrine pancreas (1). However, these GLP-1 secretion (4)din patients with suggesting that postprandial elevations studies have been met with substan- type 2 diabetes and matched control of endogenous GLP-1 (two- to three- tive criticism based on technical and subjects. fold) cannot trigger enzyme release methodical issues (2). Nevertheless, Detailed description of the experimen- from the human pancreas, at least not incretin-based therapies seem to result tal procedures and subjects was provided acutely. in small increases (within normal range) previously (4). In short, pancreas-specific These results suggest that the obser- in plasma concentrations of amylase amylase and lipase concentrations were vation of elevated plasma amylase and andlipaseinpatientsreceivingthese measured in plasma from 15 patients lipase
    [Show full text]
  • (PB) Is a Major Drug in the Treatment of Canine, Feline and Human Epilepsy and Can Significantly Reduce the Severity of Seizures
    ACTA VET. BRNO 2002, 71: 309–312 Phenobarbital Effects on Brain and Liver Tissues Enzyme Activity in Balb/C Mice E. YAZAR 1*, O. DEMIR2, M. ELMAS1, A. L. BAS1, B. TRAS1 1Department of Pharmacology and Toxicology, Faculty of Veterinary Medicine, University of Selcuk, Konya, Turkey 2Department of Neurology, Faculty of Medicine, University of Selcuk, Konya, Turkey Received October 8, 2001 Accepted June 19, 2002 Abstract Yazar, E., O. Demir, M. Elmas, A. L. Bas, B. Tras: Phenobarbital Effects on Brain and Liver Tissues Enzyme Activity in Balb/C Mice. Acta Vet. Brno 71, 2002: 309-312. The purpose of the present study was to investigate the effect of phenobarbital on some brain and liver tissue enzyme activities in Balb/C mice. Forty male Balb/C mice were used. Ten mice served as a control group, and thirty mice were administered with phenobarbital (80 mg·kg-1 body mass, single oral dose). Brain and liver samples were taken at 6, 12 and 24 h after drug administration. Brain and liver tissues alkaline phosphatase, aspartate aminotransferase, gamma glutamyl transferase and amylase activities were measured by auto- analyzer. Phenobarbital did not affect gamma glutamyl transferase and amylase activities in the brain and liver, and alkaline phosphatase and aspartate aminotransferase activities in the liver. However, statistically significant (p < 0.05) increases of alkaline phosphatase and aspartate aminotransferase activities were observed in the brain. In general, after phenobarbital administration, serum alkaline phosphatase and aspartate aminotransferase activities increase and these increases are believed to be derived from the liver. These result suggest that brain may contribute to increased activities of these enzymes in serum in Balb/C mice.
    [Show full text]