Lipase 

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Lipase is produced by the pancreas, liver, intestine, tongue, stomach, and many other cells. Lipase testing is indicated in acute pancreatitis, as well as in the diagnosis of peritonitis, strangulated or infarcted bowel, and pancreatic cyst. ^[1]

The reference range of lipase is 0-50 U/L, although this is method-dependent. ^[1]

Lipase levels may be increased in the following conditions: ^{[1, 2]}

Acute pancreatitis

Perforated or penetrating peptic ulcer, particularly involving the pancreas

Obstruction of pancreatic duct by stone

Drug-induced spasm of sphincter of Oddi (codeine, morphine, methacholine, cholinergics)

Chronic pancreatitis

Pancreatic pseudocyst

Pancreatic malignancy

Gastric malignancy or perforation

Acute cholecystitis

Small bowel obstruction

Intestinal infarction

Cystic fibrosis

Inflammatory bowel disease

Acute and chronic renal failure

Organ transplantation, particularly associated with a complication (organ rejection, cyclosporine toxicity, cytomegalovirus infection)

Alcoholism

Diabetic ketoacidosis

Intracranial hemorrhage

Lymphoma

Chronic liver disease

Use of certain drugs: Methodological interference (pancreozymin [contains lipase], deoxycholate, glycocholate, taurocholate [prevents inactivation of enzyme], bilirubin [turbidimetric method])

After endoscopic retrograde cholangiopancreatography (ERCP)

Lipase levels are decreased in association with methodological interference (presence of hemoglobin, quinine, heavy metals, calcium ions). ^[1]

Lipase levels are normal in individuals with mumps and in those with macroamylasemia. Values are lower in neonates.

Methodology: Quantitative enzymatic ^[2]

Container: Tiger-top tube (serum-separator tube or plasma-separator tube) ^[2]

Specimen collection method: Routine venipuncture

Processing: Allow the sample to clot completely in the serum tube at room temperature and separate plasma from cells within 2 hours of collection in the laboratory. An adequate sample requires a minimum of 0.2 mL (preferably 2 mL). ^[2] Ambient temperatures and exposure to room air make the sample unacceptable for analysis. Other unacceptable conditions include specimens collected in EDTA, oxalate/fluoride/citrate tubes with glycerol-lubricated stoppers.

Stability: After separation from cells, frozen one year, refrigerated and ambient one week ^[2]

Reported: Within 24 hours

Lipase catalyzes hydrolysis of triglycerides to produce fatty acids and glycerol. Lipase is produced by the pancreas, liver, intestine, tongue, stomach, and many other cells.

Because lipase levels remain elevated longer than amylase and its sensitivity in acute alcoholic pancreatitis is increased, serum lipase may be a more reliable test than serum amylase for the initial diagnosis of acute pancreatitis. ^{[3, 4]}

Certainly, daily measurements of lipase are of no value in the assessment of the patient’s clinical progress or ultimate prognosis. Because of its sensitivity, lipase testing is not very useful in chronic pancreatitis or pancreatic cancer. ^{[3, 4, 5]}

Lipase testing is indicated in acute pancreatitis.

It is also used in the diagnosis of peritonitis, strangulated or infarcted bowel, and pancreatic cyst. ^[1]

Pancreatic inflammation increases enzyme levels.

None of the available tests meet all criteria (establishing the diagnosis accurately, providing early assessment of its severity, identifying the cause) for an ideal laboratory test in the evaluation of a patient with acute pancreatitis. Nevertheless, serum amylase and lipase are considered important tests in the diagnosis of acute pancreatitis.

Easy availability, high sensitivity, and technical simplicity are touted as the advantages of amylase testing, but its greatest disadvantage is its low specificity. Serum lipase is a more reliable diagnostic marker of acute pancreatitis than serum amylase. ^[5] The major benefit of lipase is in patients with delayed presentation, ^{[6, 7]} since its activity remains increased for longer periods (up to 8-14 days), and an increased sensitivity in acute alcoholic pancreatitis. ^{[3, 4]} Nonspecific elevations of lipase levels have been reported in almost as many disorders as amylase.

Although lipase is mostly found in the pancreas, serum levels may also increase in association with other intra-abdominal pathologies or renal insufficiency. Most studies have reported specificities above 95%, with sensitivities varying between 55% and 100% at a cutoff activity of 600 IU/L. ^[4] However, a normal serum lipase level does not exclude acute pancreatitis, particularly recurrent disease, when the clinical features are compatible with the diagnosis.

The level of lipase cannot be used to determine disease severity or to predict outcome. ^[8] Simultaneous estimation of lipase with amylase does not improve the accuracy. ^[4]

Pancreatic panniculitis presents with tender, ill-defined, red-brown nodules in the lower limbs that may ulcerate and drain an oily substance. It usually precedes pancreatic disease, particularly pancreatitis and pancreatic carcinoma. Therapy should be directed at the underlying pancreatic disease. ^[9]

Williamson MA, Snyder LM, Wallach JB. Wallach’s interpretation of diagnostic tests. 9th ed. Philadelphia: Wolters Kluwer/Lippincott Williams & Wilkins Health; 2011.

Laboratories A. National Reference Laboratories. [cited 2012 August 28, 2012]. [Full Text].

Gomella LG HS. Laboratory Diagnosis: Chemistry, Immunology, Serology. Gomella LG HS, editor. Clinician’s Pocket Reference: The Scut Monkey. 11 ed. New York: McGraw-Hill; 2007.

Smotkin J, Tenner S. Laboratory diagnostic tests in acute pancreatitis. Journal of clinical gastroenterology. 2002. 34(4):459-62. Epub 2002/03/22.

Yadav D, Agarwal N, Pitchumoni CS. A critical evaluation of laboratory tests in acute pancreatitis. Am J Gastroenterol. 2002. 97(6):1309-18. Epub 2002/07/04.

Al-Bahrani AZ, Ammori BJ. Clinical laboratory assessment of acute pancreatitis. Clin Chim Acta. 2005. 362(1-2):26-48. Epub 2005/07/19.

Sternby B, O’Brien JF, Zinsmeister AR, et al. What is the best biochemical test to diagnose acute pancreatitis? A prospective clinical study. Mayo Clin Proc. 1996. 71(12):1138-44. Epub 1996/12/01.

Tietz NW, Shuey DF. Lipase in serum–the elusive enzyme: an overview. Clin Chem. 1993. 39(5):746-56. Epub 1993/05/01.

Atilla R OC. Pancreatitis and Cholecystitis. Tintinalli JE SJ, Cline DM, Ma OJ, Cydulka RK, Meckler GD, editor. Tintinalli’s Emergency Medicine: A Comprehensive Study Guide. 7th ed. New York: McGraw-Hill; 2011.

Garcia-Romero D, Vanaclocha F. Pancreatic panniculitis. Dermatol Clin. 2008. 26(4):465-70, vi. Epub 2008/09/17.

Bishnu Prasad Devkota, MD, MHI, FRCS(Edin), FRCS(Glasg), FACP Professor of Medicine, St Louis University School of Medicine

Bishnu Prasad Devkota, MD, MHI, FRCS(Edin), FRCS(Glasg), FACP is a member of the following medical societies: American College of Physicians, American Medical Informatics Association, Royal College of Physicians and Surgeons of Glasgow, Healthcare Information and Management Systems Society, Royal College of Surgeons of Edinburgh

Disclosure: Nothing to disclose.

Eric B Staros, MD Associate Professor of Pathology, St Louis University School of Medicine; Director of Clinical Laboratories, Director of Cytopathology, Department of Pathology, St Louis University Hospital

Eric B Staros, MD is a member of the following medical societies: American Medical Association, American Society for Clinical Pathology, College of American Pathologists, Association for Molecular Pathology

Disclosure: Nothing to disclose.

Lipase 

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