Development of a Specific Assay for Pancreatic Lipase Activity for Diagnostic Purposes

  • Georges Férard
  • Jean Marc Lessinger
  • Panteleimon Arzoglou
  • Atanase Visvikis
  • Wolfgang Junge
Chapter
Part of the NATO ASI Series book series (NSSA, volume 266)

Abstract

Determination of pancreatic lipase (E.C. 3.1.1.3) in serum is frequently required for diagnosing pancreatitis for at least two reasons. First, an increase in levels of pancreatic enzymes in blood or in urine is a part of the definition of acute pancreatitis [1]. Among the pancreatic enzymes, serum lipase activity is presently considered as the most efficient marker of this disease as shown in many comparative studies. As an example, data from 15 comparative studies published since 1985 indicate that the mean values of sensitivity of serum amylase, pancreatic isoamylase and lipase activity for the diagnosis of acute pancreatitis are 0.88 0.85 and 0.91 and those of specificity are 0.74 0.81 and 0.88, respectively. Second, several assays recently developed are easy to perform in an automated manner. Our goal is to analyze the characteristics of contemporary methods for lipase assay and to compare the results obtained by these methods for plasma samples from patients suffering from acute pancreatitis. The interassay agreement will be discussed and some recommendations will be formulated to improve the specificity and the accuracy of lipase assays for diagnostic use.

Keywords

Acute Pancreatitis Bile Salt Lipase Activity Pancreatic Lipase Hepatic Lipase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Sarles H., Adler G., Dani R., Frey C., Gullo L., Harada H., Martin E., Norohna M., and Scuro L.A., Classifications of pancreatitis and definition of pancreatic diseases. Digestion 43: 1989; 234 - 236.PubMedCrossRefGoogle Scholar
  2. 2.
    Ziegenhorn J., Neumann U., Knitsch K.W., and Zwez W., Determination of serum lipase. Clin. Chem. 25: 1979; 1067.Google Scholar
  3. 3.
    Mauck J.C., Weaver M.S., and Stanton C., Development of a Kodak Ektachem clinical chemistry slide for serum lipase. Clin. Chem. 30: 1984; 1058 - 1059.Google Scholar
  4. 4.
    Imamura S., and Misaki H, An enzymatic method using 1,2-diglyceride for pancreatic lipase test in serum. Clin. Chem. 35: 1989; 1126.Google Scholar
  5. 5.
    Imamura S., and Misaki H (1984) A sensitive method for assay of lipase activity by coupling with 3-oxydation enzymes of fatty acid, in: Selected Topics in Clinical Enzymology, vol 12 pp. 73-77, Goldberg D.M., Werner M., eds, Walter de Gruyter, Berlin-New York.Google Scholar
  6. 6.
    Rick W., Kinetischer Test zur Bestinunung der Serumlipaseaktivität. Z Klin. Chem. Klin. Biochem. 7: 1969; 530 - 539.Google Scholar
  7. 7.
    Tietz N.W., and Repique E.V., Proposed standard method for measuring lipase activity in serum by a continuous sampling technique. Clin. Chem. 19: 1973; 1268 - 1275.PubMedGoogle Scholar
  8. 8.
    Lessinger J.M., Arzoglou P.L., and Férard G., Evidence for multiple forms of pancreatic lipase in human plasma. Adv. Clin. Enzymol. 3: 1986; 139 - 150.Google Scholar
  9. 9.
    Lott J.A., and Lu C.L., Lipase isoforms and amylase isoenzymes: Assays and application in the diagnosis of acute pancreatitis. Clin. Chem. 37: 1991; 361 - 368.PubMedGoogle Scholar
  10. 10.
    Clavien P.A., Burgan S., and Moossa A.R., Serum enzymes and other laboratory tests in acute pancreatitis. Br. J. Surg. 76: 1989; 1234 - 1243.PubMedCrossRefGoogle Scholar
  11. 11.
    Lessinger J.M.,Tavridou A., Arzoglou P.L., and Férard G., Interest of using a purified, stable and commutable preparation of human pancreatic lipase in indirect assays. Anal. Lett. 25: 1992; 1453¬1468.Google Scholar
  12. 12.
    Tavridou A., Avranas A., and Arzoglou P.L., A mathematical approach to lipolysis based on the interrelationship of physicochemical and biochemical data. Bioch. Biophys. Res. Comms 186: 1992; 746 - 752.CrossRefGoogle Scholar
  13. 13.
    Junge W., Leybold K., and Philipp B., Identification of a non-specific carboxylesterase in human pancreas using vinyl 8-phenyloctanoate as a substrate. Clin. Chico. Acta 94: 1979; 109 - 114.CrossRefGoogle Scholar
  14. 14.
    Demanet C., Goedhuys W., Haentjens M., Huyghens L., Blaton V., and Gorus F., Two automated fully enzymatic assays for lipase activity in serum compared: positive interference from post-heparin lipase activity. Clin. Chem. 38: 1992; 288 - 292.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Georges Férard
    • 1
  • Jean Marc Lessinger
    • 1
  • Panteleimon Arzoglou
    • 2
  • Atanase Visvikis
    • 3
  • Wolfgang Junge
    • 4
  1. 1.Laboratoire de Biochimie appliquée, Faculté de PharmacieUniversité Louis Pasteur de StrasbourgIllkirchFrance
  2. 2.Laboratory of Biochemistry, Department of ChemistryUniversity of ThessalonikiThessalonikiGreece
  3. 3.Centre du MédicamentNancyFrance
  4. 4.Friedrich-Ebert KrankenhausNeumunsterGermany

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