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Values of the blood tests pancreatic amylase and lipase

Values of the blood tests pancreatic amylase and lipase


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Anyone know what is considered slightly elevated, moderately elevated and strongly elevated values of pancreatic amylase and lipase?

Many different laboratories in my country divide between these categories for interpretation, but they don't specify which values qualify for each category.

Hope this is the right place for this kind of question.

Thanks in advance.


It is not necessary a fixed value. I think it depends on the doctor that interprets it. For e.g if amylase's normal value is 70, and laboratoy value is 80, i would say it is slightly elevated. A value of 300 is strongly elevated.


Blood tests for acute pancreatitis

The diagnosis of acute pancreatitis requires the presence of at least two of the three diagnostic criteria – characteristic abdominal pain, elevated serum amylase or lipase, and radiological evidence of pancreatitis.

Serum concentrations of amylase and lipase rise within hours of the pancreatic injury. A threshold concentration 2𠄴 times the upper limit of normal is recommended for diagnosis.

Serum lipase is now the preferred test due to its improved sensitivity, particularly in alcohol-induced pancreatitis. Its prolonged elevation creates a wider diagnostic window than amylase.

Neither enzyme is useful in monitoring or predicting the severity of an episode of pancreatitis in adults.

New biomarkers including trypsinogen and elastase have no significant advantage over amylase or lipase.


Values of the blood tests pancreatic amylase and lipase - Biology

@harper7745
Hi Louise
I see your back. Hope your doing ok. I have not been well. I'm scared to have the next blood test because I am having a lot of stomach issue & the neuropathy is killing me. They put me on Gabapentin & they keep increasing it & I do good for a week & then the needles & pins in the legs & feet. It is hard for me to get around. I'm getting discouraged but I keep going. My new grandson is keeping me alive. he is 7 months old & they are coming down for the week end. Glad your back. I'm praying for you.
Take Care
Tigreyes/Genie

Hi Genie
I got back a few days ago. Had a good trip. I am feeling better. So sorry that you aren't. Is your neuropathy from Diabetes? Had appointment with my GI doc. I am on Steroids for 1 more day. Had 2 month RX. Also on Creon, which is pancreatic enzymes to help me digest my food. Guess they are working because I gained 5lbs. with it. Lost 18lb total. Now we just have to wait and see if I stay ok. If I get sick again, or symptoms, I will have to be on Steroids for life. Please don't give up. I know discouragement!! Hopefully your blood work will show something this time that will help. Your grandson needs you. I am praying for you too. Louise

Hi Genie
I got back a few days ago. Had a good trip. I am feeling better. So sorry that you aren't. Is your neuropathy from Diabetes? Had appointment with my GI doc. I am on Steroids for 1 more day. Had 2 month RX. Also on Creon, which is pancreatic enzymes to help me digest my food. Guess they are working because I gained 5lbs. with it. Lost 18lb total. Now we just have to wait and see if I stay ok. If I get sick again, or symptoms, I will have to be on Steroids for life. Please don't give up. I know discouragement!! Hopefully your blood work will show something this time that will help. Your grandson needs you. I am praying for you too. Louise

Hi Louise
Glad your back home & had a nice trip. I am praying for you. I am still not feeling well but am fighting this. My blood pressure is starting to elevate & I am on Losartan 25 low dose but it is on the rise. I am wondering if certain medications can cause it to go up. If it continues I will have to call my Cardiologist. I am not a diabetic & they have no idea why the lipase is going up. In a couple of weeks I go back for the repeat of the test & I hope & pray it has not gone up more. I still think my problem stems from the last surgery I had. The small bowel was injured & I had to have 2 stitches so I don't know if this has anything to do with it. All I know is that I am loaded with adhesions that can not be removed so that might be part of the problem.
Well Louise keep in touch & keep me posted.
Have a good day.
God Bless
Genie


Amylase Blood Test

The pancreas is an organ in the human body that secretes important enzymes and hormones. The enzymes secreted by the pancreas are associated with digestive functions. The hormones associated with the pancreas are glucagon and insulin. Insulin is essential to lower blood sugar levels as it helps the body absorb glucose which is used for energy generation. Glucagon helps to maintain the blood sugar level at an acceptable level so that the individual does not suffer from hypoglycemia. Therefore, the pancreas is very important when it comes to the maintenance of blood sugar levels in the body. The pancreas lies next to the stomach and its outlet connects into the duodenum. This is the first part of the small intestine that leads out of the stomach.

An amylase blood test is a test that is used to determine problems associated with pancreas function. Pancreatitis is a condition where the pancreas is infected or damaged. Symptoms of pancreatitis include severe abdominal pain, nausea and loss of appetite. The amylase blood test is used to determine the state of the pancreas by checking the amylase levels in the blood. The amylase levels may rise or fall depending on the health of the pancreas. Also read more on LFT blood test.

Acute pancreatitis is a condition where there is a sudden injury to the pancreas. This may lead to amylase blood test results which show up to 6 times the normal concentration of amylase in the blood. When there is a rapid increase in amylase blood test results, the doctor will suspect acute pancreatitis. Chronic pancreatitis is a condition where there is a long term illness of the pancreas. In such a situation, the amylase blood test results will be moderately elevated for a long period of time. As the pancreas gets further damaged, the amylase blood test level will fall.

The amylase blood test may be conducted alongside a urine amylase test to determine how much of this substance is in the urine. The amylase blood test is a simple procedure as far as the patient is concerned. A needle will be used to collect blood, usually from a vein in the upper forearm. This blood is then sent to a laboratory where it is checked for the level of amylase. The results of the amylase blood test are used to determine the condition of the pancreas. Other supporting symptoms are needed to give a conclusive diagnosis of pancreatitis.


Treating Pancreatitis

Acute pancreatitis usually requires hospitalization, where the patient receives fluids, antibiotics and pain medication through an intravenous drip. The patient will not be allowed to eat, as the digestion of solid food will put too much strain on the pancreas and fasting will allow it to recover. Acute pancreatitis will usually resolve itself within a few days. When leaving the hospital, patients will be advised on how to prevent pancreatitis, usually through a reduction in alcohol consumption, fat intake and smoking cessation. Chronic pancreatitis patients will normally receive treatment for alcohol addiction, but surgery may be required for those presenting with tissue death.


Prevention

Can pancreatitis be prevented?

The best way to prevent pancreatitis is to have a healthy lifestyle. Aim to:

  • Maintain a healthy weight.
  • Get regular exercise.
  • Stop smoking.
  • Avoid alcohol.

These healthy lifestyle choices will also help you avoid gallstones, which cause 40% of acute pancreatitis cases. Your provider may recommend removing your gallbladder if you have painful gallstones multiple times.


Pancreatic Function

B Chronic Pancreatitis

1 Serum Enzymes

Serum amylase and lipase levels may be elevated if acute exacerbations of pancreatitis occur or if chronic pancreatitis is associated with ductal obstruction. However, with complete destruction of acinar tissue and healing by fibrosis, serum enzyme elevations would not be expected.

2 Fecal Examination

When pancreatic insufficiency is under consideration, an examination of feces is important as a preliminary screening test. The gross and microscopic findings of a fecal examination may reflect the failure to digest and absorb fats and proteins as a result of pancreatic enzyme deficiencies. Pancreatic enzyme deficiencies may also be detected by the estimation of enzymes in feces.

Pancreatic enzymes undergo a rapid inactivation as they pass through the intestinal tract. In the rat, diversion of pancreatic juice to the exterior of the body resulted in a rapid disappearance of enzymes from the small intestine, with virtually complete absence after 16 hours. In the rat intestine, pancreatic trypsin has a slower rate of inactivation than lipase ( Pelot and Grossman, 1962 ). In human beings, there is a greater reduction in fecal tryptic activity than chymotryptic activity during intestinal transit. The content of chymotrypsin in the feces gave an excellent indication of the ability of the human pancreas to secrete chymotrypsin. The content of trypsin in the feces, however, less accurately reflected the amount secreted into the duodenum. When the content of trypsin in the feces was high, the pancreatic capacity to secrete trypsin was also high. The converse was not necessarily true, however, since low levels of tryptic activity in the feces were found in subjects whose capacity to secrete trypsin was normal. The content of trypsin in the feces alone cannot, therefore, be used as a reliable index of pancreatic enzyme secretory capacity ( Sale et al., 1974 ).

A Gross and Microscopic Examination.

With severe pancreatic insufficiency the stool is bulky or of a pale yellow or clay color it may be glistening with neutral fat and often has a foul odor. Neutral fat in the feces may be stained with Sudan III or IV stain. The procedure as recommended by Masamune et al. (1977) required a saturated solution of Sudan III in 95% alcohol and a 37% acetic acid solution. Some fecal fat is present in the form of calcium soaps, which do not take the stains for neutral fat unless hydrolyzed with glacial acetic acid. A drop of Sudan III solution and acetic acid was added to small pieces of stool on a glass slide. After mixing, the specimen was heated and covered with a cover slip. The normal number of lipid droplets in human feces was less than 10 per field at a magnification of 100. When the number of fecal fat droplets was greater than normal, fecal fat, as determined chemically, was generally greater than normal. Lorenz (1976) was of the opinion that more than three or four fat droplets per high-power microscope field was indicative of pancreatic insufficiency in animals.

Fecal material may also be stained with Lugol's iodine, which stains starch granules a blue-black color. Excessive amounts of starch granules are compatible with pancreatic insufficiency. Relatively little amylase is required for the digestion of starch thus, the tests for lipid in feces are better qualitative tests of pancreatic insufficiency. When fat, starch granules, or undigested muscle fibers are found in feces, the tests should be repeated at a later time to rule out possible dietary contribution. The results of these simple tests may provide information that can help to establish a diagnosis of pancreatic insufficiency, or they may indicate that other digestion or intestinal absorption tests are justified.

One of the most accurate methods of determining whether there is increased fat in the feces involves the quantitative determination of fecal fat residue. Likewise, fecal nitrogen determination by the macro-Kjeldahl method is one of the more accurate methods of measuring protein digestion. However, these determinations may not differentiate pancreatogenous from intestinal malassimilation and are more suitable for the research laboratory.

B Fecal Trypsin.

Two tests of fecal enzyme activity are suitable for the veterinary clinical laboratory ( Jasper, 1954 ). The procedures are based on the incubation of gelatin with feces and the subsequent detection of proteolysis.

I Tube test.

This procedure utilizes the digestion of a gelatin solution by the test fecal sample and the detection of proteolysis by the failure of the gelatin solution to gel after incubation.

Bring 9 ml of water to 10 ml total volume by adding feces, and mix.

Warm 2 ml of a 7.5% gelatin solution to 37°C, and add 1 ml of 5% sodium bicarbonate and 1 ml of fecal dilution.

Incubate at 37°C for 1 hour (2.5 hours at room temperature).

Refrigerate for 20 minutes. Failure to gel indicates the presence of trypsin in the sample.

Ii Film test.

This procedure utilizes digestion of the gelatin of exposed or unexposed X-ray film.

Bring 9 ml of 5% sodium bicarbonate solution to 10 ml total volume by adding feces, and mix.

Immerse a thin strip of X-ray film in the fecal dilution.

Incubate at 37°C for 1 hour (2.5 hours at room temperature).

Rinse off the film under tap water. A clearing of the submerged portion of the film strip indicates the presence of trypsin in the sample.

Of the two tests, the tube test is recommended as a more accurate procedure for the detection of fecal trypsin. The film test is less sensitive, with approximately 25% of the results being falsely negative. Thus, there is a need to show repeated negative results. If the film test is used, the tube test should be used for the confirmation of samples negative for trypsin. In either test, control samples using diluent only and a normal fecal sample should be run in conjunction with the suspected sample. Davies (1957) found that normal dog fecal material would digest gelatin on X-ray film in dilutions from 1: 20 to 1: 2000. Stools over 1 day old may give false-positive results due to bacterial action.

It should be remembered that the gelatin substrate is not specific for trypsin or chymotrypsin and may be hydrolyzed by proteolytic enzymes produced by intestinal bacteria or proteolytic enzymes of the succus entericus.

3 Pancreatic Chymotrypsin Secretion

The diagnosis of exocrine pancreatic insufficiency has been performed in animals by a procedure involving the oral administration of a chymotrypsin-labile peptide (N-benzoyl-L-tyrosyl) which contains p-aminobenzoic acid (PABA) as a tracer group. In the presence of chymotrypsin the peptide is split, and PABA is liberated. The PABA is absorbed from the gut, undergoes conjugation in the liver, and is excreted in the urine. The amount of PABA in the urine is used as an indirect measure of exocrine pancreatic function. The procedure has been shown to be reliable in detecting surgically induced pancreatic insufficiency in rats, swine, and dogs. Severe hepatic disease or severe renal disease, however, may interfere with the excretion of the PABA ( Imondi et al., 1972 ).

4 Absorption Tests

In veterinary medicine, absorption tests have been concerned primarily with the absorption of fats or vitamins in oil. The tests are based on the principle that dietary fats must be hydrolyzed to fatty acids and glycerol prior to absorption. It should be remembered that, in the presence of reduced ability to assimilate fats, the defect may lie in either a deficiency of pancreatic lipase or an inability of the small bowel to absorb properly digested fats.

A Fat Absorption.

This test is simple to perform, requires a minimum of equipment, and involves only visual comparison of the turbidity of the plasma ( Brobst and Funk, 1972 ). A heparinized blood sample (5 ml) is drawn from the fasted animal and centrifuged. Then 2 ml peanut oil per kilogram body weight are added to a small quantity of food and fed to the dog. A second heparinized blood sample (5 ml) is drawn 2 hours after ingestion of the fat meal, and the sample centrifuged. The turbidities of the pre- and postfeeding samples are compared. Normally, the prefeeding sample has clear plasma, while the postfeeding sample has a creamy or turbid appearance (hyperlipemia). If the plasma samples are equally clear, one can assume that either pancreatic exocrine function is deficient or that the intestine is incapable of proper absorption. The two conditions can be differentiated by repeating the fat meal at a later date, this time supplemented with pancreatic extract as a source of lipase. A cloudy postfeeding sample indicates that absorption from the intestine was normal and that the pancreas was deficient in secretion of lipase. Enteritis may render the test unreliable because of false-negative results.

B Labeled Fat Absorption.

Measuring intestinal absorption of radioiodine-labeled triolein and radioiodine-labeled oleic acid has proved to be valuable in the differential diagnosis of pancreatic steatorrhea and intestinal malabsorption in dogs ( Kaneko et al., 1965 ). Kallfelz et al. (1968) demonstrated that in normal dogs approximately 13% of the oleic acid and 11% of the triolein was absorbed. In a dog with pancreatic fibrosis, the absorption of oleic acid was normal but that of triolein was less than 1%, indicating defective hydrolysis.


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Values of the blood tests pancreatic amylase and lipase - Biology

Catalase

Hydrogen peroxide (H2O2) is a common by-product of metabolic reactions. In high concentration it is toxic therefore, its accumulation in cells would be harmful. Most tissues, however, contain the enzyme catalase, which catalyzes the breakdown of peroxide to water and oxygen as follows: The reaction is extremely rapid. The action of the enzyme can be demonstrated easily by the evolution of oxygen in the form of gas bubbles when an extract of a tissue containing the enzyme is added to a dilute solution of hydrogen peroxide. We will use homogenized (ground-up) chicken or beef liver as a source of catalase. Catalase

  • Catalase - general information Classrooms of 21st century
  • Catalase - An Extraordinary Enzyme
  • Heat denature enzyme
  • Structure of Catalase image and graph
  • Links -

Amylase

    Amylase References:
    • Amylase - Independent study by Amy Caruana (Student at Kean Univ)
    • Amylase - results from U. North Dakota
    • Enzymes amylase, temp, pH, substrate concentration
    • Benedicts test for reducing sugar - image of result
    • Amylase How does it work?
    • Amylase - starch hydrolysis
    • Salivary amylase - pH
    Pepsin is a protease that begins digestion of proteins, breaking them into peptides and amino acids. Pepsinogen, is secreted by gastric glands of the stomach into the stomach. There, in the acid environment of the stomach, pepsinogen is converted into pepsin.

    Although both pepsin and trypsin are proteases, they require quite different conditions of acidity and alkalinity for their action.

      Pepsin References:
      • Pepsin -
      • Pepsin - molecule of the month
      • pH optimum -
      • Pepsin - mentions pH optimum
      Trypsin is a protease secreted into the small intestine by the pancreas. As pepsin, trypsin digests proteins into peptides and amino acids and is made and secreted in an inactive form, trypsinogen.

      Although both pepsin and trypsin are proteases, they require quite different conditions of acidity and alkalinity for their action.

        Trypsin References:
        • Trypsin Encyclopedia description
        • Illustration search for trypsin within this large file
        • Images Google search engine

        An Analogy

        Suppose you are interested in purchasing a Pizza store and wish to investigate how productive the store is without the present owner knowing because, you fear the owner will raise the price. So, instead of going into the store and watching what happens and asking to examine the books that record expenses and profits, you decide to watch the store from outside.

        You observe how often trucks arrive with pizza dough, pizza toppings (cheese, pepporoni, etc.), and other supplies. You also observe how often workers leave the store to deliver pizzas to customers.

        In this analogy, the pizza supplies are the reactants and the boxed pizzas that are delivered to customers are the end products. The workers within the store that shape the dough, add the toppings and place the pizzas in ovens and finally in boxes are the equivalent of the enzymes.

        Although we don't actually see the workers doing their job, we can infer that if the store is using large quantities of reactants (dough and toppings) and / or making large numbers of end products (pizzas) that the workers (enzymes) must be very active.


        Conflicts of interest

        Author(s), yearHospital, country Type of studyPatients in series and patients with raised lipase levels, nNormal range of lipaseNormal range of amylasePeak amylase level (non-pancreatitis), mean (range)Peak lipase level (non-pancreatitis), mean (range)Imaging (CT ± others)Presence of abdominal pain/tenderness
        Akaza., 2007 71 Fukuoka, Osaka, Sapporo, Tsukuba and Tokyo, Japan Prospective non-randomized open label study 129 73 had ↑ lipase w/o pancreatitis 8 had levels ϥ × ULN, and 32 had levels Ϣ𠄵 × ULN NRNRNRNRNR0/73 patients with ↑ lipase
        Argiris., 1999 38 New York, USA Prospective observational study 86 26 had ↑ lipase w/o pancreatitis Number with lipase levels ≥ 3 × ULN NR 10� U/l25� U/l117 (range 17�)56 (range 9�)No US or CT features of pancreatitis in 6 patients with ↑ lipase 1 patient had mild pancreatic duct dilatation and ‘minimal pancreatic enlargement’ imaging not performed in others due to no clinical suspicion5/86 patients with ↑ lipase (epigastric discomfort or dyspepsia) (pancreatitis was not suspected)
        Ashley & Lauwers, 2002 60 Boston, USA Case report 1 Had lipase level ≥ 3 × ULN NRNR421614No CT, US or MRI features of pancreatitisNil
        Asvesta., 1988 34 Thessaloniki, Greece Case𠄼ontrol study 168 72 had ↑ lipase At least 10 had lipase levels ≥ 3 × ULN 0� U/lNRNR366 (79 in controls)NR0/168 patients with ↑ lipase
        Bokemeyer, 2002 40 Minden, Germany Prospective observational study 136 19 had ↑ lipase w/o pancreatitis (11 had CD, 8 had UC) 6 had lipase levels Ϣ × ULN w/o pancreatitis 0� U/l28� U/lNR (1 patient had levels > 2 × ULN)NRNo US features of pancreatitis in all 19 patients with ↑ lipase0/19 patients with ↑ lipase
        Brooks., 2009 59 Cleveland, USA Case report 1 Had lipase level ≥ 3 × ULN 12� U/l0� U/l12412664No CT features of pancreatitisYes (epigastric pain)
        Carroccio., 2006 41 Palermo, Italy Prospective observational study 202 (90 adults, 112 children) 19 adults and 21 children had ↑ lipase w/o pancreatitis No patient had lipase levels ≥ 3 × ULN (peak was 2.5 × ULN) 20� IU/l (adults) variable for children10� IU/l (adults) variable for children240 (median) (adults) 1.4 × ULN (median) (children)432 (median) (adults) 1.3 × ULN (median) (children)No US features of pancreatitis in all 202 patients10/90 adults and 9/112 children (‘recurrent abdominal pain’)
        Catton & Lobo, 2010 58 Nottingham, UK Case report 1 Had lipase level ≥ 3 × ULN 23� IU/l30� IU/l3804398No CT features of pancreatitisYes (epigastric pain)
        Chase., 1996 43 Chattanooga, USA Retrospective case series 306 208 had non-pancreatic abdominal pain 26/208 had ↑ lipase 4 had lipase levels ≥ 3 × ULN 5� U/l30� U/lN/A d (maximum 385)N/A d (maximum 3685)NR26/26 patients with ↑ lipase
        Chen., 1996 49 Taipei, Taiwan Retrospective case series 84 22 had ↑ lipase w/o pancreatitis 4 had levels ≥ 3 × ULN w/o pancreatitis 𼆐 U/l𼆀 IU/l127 ± 17 (haemodialysis patients) 192.1 ± 24.5 (no dialysis)206 ± 35 (haemodialysis patients) 146.1 ± 18.4 (no dialysis)No US features of pancreatitis in all 22 patients with ↑ lipase0/22 patients with ↑ lipase
        Denz., 2007 25 Berlin, Mannheim and Karlsruhe, Germany Prospective observational study 66 52 had ↑ lipase 38 had lipase levels ≥ 3 × ULN 𼅐 U/lNRNRNRCT showed features of pancreatitis in 7/20 patients in which it was done No CT features of pancreatitis in 13 patients with lipase ≥ 3 × ULN bb NR
        Diani., 1998 17 Pavia and Varese, Italy Retrospective case series 4 All 4 had ↑ lipase w/o pancreatitis 3 had lipase levels ≥ 3 × ULN w/o pancreatitis 8� U/lNRWithin normal limits (all patients)197 (patient 1) 120 (patient 2) 351 (patient 3) 412 (patient 4)No US features negative of pancreatitis in all patients no CT features of pancreatitis in at least 2 patientsNR
        Duerksen., 2000 39 Winnipeg, Canada Case report 1 Had lipase level ≥ 3 × ULN 𼆐 IU/l𼄠 IU/l3502000No CT or US features of pancreatitisNil
        Frank & Gottlieb, 1999 14 Landshut, Germany Indianapolis, USA Retrospective case series 25 All 25 had ↑ lipase All 25 had lipase levels ≥ 3 × ULN 40� U/l25� U/lN/A d N/A d NR19/25 patients with ↑ lipase
        Gomez., 2012 2 Nottingham, UK Retrospective cohort study 2979 18 had lipase levels ≥ 3 × ULN w/o pancreatitis i 0� U/l0� U/lNRNRNo CT features of pancreatitis in all 18 patients18/18 patients (acute abdominal pain)
        Goto., 2000 51 Akita and Matsumoto, Japan Case report 1 Had lipase level ≥ 3 × ULN 29� IU/l115� IU/l6253338No US features of pancreatitisNil
        Gottlieb., 1996 24 Indianapolis, USA Prospective case series 231 Number with ↑ lipase NR 193 patients did not have pancreatitis 40� U/l25� U/l200 ± 13 (cf. 657 ± 104 for pancreatitis patients)2444 ± 288 (cf. 9879 ± 1480 for pancreatitis patients)NR70/193 patients w/o pancreatitis had abdominal pain
        Gullo, 1996 18 Bologna, Italy Prospective case series 18 All 18 had ↑ lipase At least 6 had lipase levels ≥ 3 × ULN 24� IU/l0� IU/lNR (range 1.4𠄴.1 × ULN)NR (range 1.5𠄷.7 × ULN)No CT or US (൲) features of pancreatitis in all patients0/18 patients
        Gullo, 2000 19 Bologna, Italy Prospective observational study 102 j 19 had ↑ lipase w/o pancreatitis 7 had lipase levels ≥ 3 × ULN w/o pancreatitis 24� IU/l0� IU/lNR (range 1.3𠄵.2 × ULN)NR (range 1.6� × ULN)No US features of pancreatitis in all 19 patients with ↑ lipase0/19 patients with ↑ lipase
        Gullo., 2006 20 Bologna, Italy Prospective observational study 18 w 16 had ↑ lipase w/o pancreatitis 7 had lipase levels ≥ 3 × ULN w/o pancreatitis 13� IU/l13� IU/l (pancreatic isoamylase)NR (range 𢏀.8𠄳.9 × ULN) (pancreatic isoamylase)NR (range 𢏀.8𠄶.4 × ULN)No US, CT or MRI features of pancreatitis in all patients0/18 patients
        Gullo, 2007 21 Bologna, Italy Prospective observational study 42 w 38 had ↑ lipase w/o pancreatitis 30 had lipase levels ≥ 3 × ULN w/o pancreatitis at some point during study 13� IU/l28� IU/lNR255 (mean of peak levels in each patient over 5 days)No US or CT features of pancreatitis in all patients No MRI features of pancreatitis in 36 patients0/42 patients
        Gumaste., 1993 4 New York, USA Prospective cohort study 170 (95 w/o pancreatitis + 75 with pancreatitis) 10 had ↑ lipase w/o pancreatitis 1 had lipase levels ≥ 3 × ULN w/o pancreatitis 31� U/l?40� U/lN/A d N/A d NR f 95/95 patients w/o pancreatitis (acute abdominal pain)
        Haddad., 2004 29 Indianapolis, USA Prospective cohort study 50 20 had ↑ lipase w/o pancreatitis 7 had lipase levels ≥ 3 × ULN w/o pancreatitis 15� U/l (vitros) 5� U/l (colorimetric)25� U/l (vitros) 25� U/l (Catachem)162 ± 152 in DKA patients with ↑ lipase or amylase (cf. 38 ± 10 for DKA patients with normal enzymes)404 ± 385 in DKA patients with ↑ lipase or amylase (cf. 46 ± 27 for DKA patients with normal enzymes)CT features of pancreatitis in 1 patient (performed in 3 patients with lipase ≥ 3 × ULN)36/50 x patients (abdominal pain and/or vomiting)
        Heikius., 1999 42 Oulu, Finland Prospective observational study 237 aa 16 had ↑ lipase w/o pancreatitis No patient had lipase levels ≥ 3 × ULN (peak was 2.9 × ULN) 𼅠 U/l70� U/l176 (range 1.1𠄱.9 × ULN)66 (range 1.1𠄲.9 × ULN)US showed increased/patchy echogenicity of the pancreas in 6/38 patients with ↑ lipase or amylaseNR
        Justice., 1994 66 Savannah, USA Prospective case series 38 (37 w/o pancreatitis + 1 with pancreatitis) 24 had ↑ lipase w/o pancreatitis Number with lipase levels ≥ 3 × ULN NR 23� U/l30� U/l140 ± 109712 ± 614No CT features of pancreatitis in the 3 patients it was performed inNR
        Keating & Lowe, 2002 52 St Louis, USA Case report 1 Had lipase level ≥ 3 × ULN 20� U/l15� U/l1143 (range 119� over 2 months)1139 (range 694� over 2 months)No CT or US (൲) features of pancreatitis g Yes (lower abdominal cramps)
        Klassen., 1996 63 Baltimore, USA Prospective case series 69 (68 w/o pancreatitis + 1 with pancreatitis) Number with ↑ lipase NR 23� IU/l30� U/l341 ± 401548 ± 222NRNR
        Klimstra., 1992 61 New Haven and Washington, USA Retrospective case series 28 4 had ↑ lipase At least 1 had lipase levels ≥ 3 × ULN 0𠄱 Teitz unitsNRNRNR (maximum 20 Teitz units)NRNR
        Lando., 2012 35 Alexandria and Washington, USA Retrospective cohort study 90 31 had ↑ lipase w/o pancreatitis Number with lipase levels ≥ 3 × ULN NR h �� U/l (ULN) h NRNR (maximum was 100 U/l above normal)NR (maximum 453)No imaging done (patients asymptomatic)0/90 patients
        Lee., 2010 67 Taipei, Taiwan Case𠄼ontrol study 89 43 had ↑ lipase or amylase (exact number with ↑ lipase NR) � U/l� U/lNR t NR t See footnote y Difficult to assess/NR v
        Liu., 2001 68 Chicago, USA Case𠄼ontrol study 75 11 had ↑ lipase and amylase levels Number with lipase levels ≥ 3 × ULN NR 0� U/l0� U/l402474US done in 3/11 patients with ↑ lipase, US + CT done in 3/11 patients nil imaging in 5 patients – no US or CT features of pancreatitis in these patients0/11 patients with ↑ lipase k
        Lobo., 2007 36 Nottingham, UK Prospective cohort study 44 (20 controls + 24 patients with SOD) At least 17 controls and 23 SOD patients had ↑ lipase levels Exact number with lipase levels ≥ 3 × ULN NR 23� U/l30� U/l𢏇 × ULN (in controls, post-provocation with morphine and prostigmine)� × ULN (median – in controls, post-provocation with morphine and prostigmine) levels increased up to 50 × ULN in SOD patients (exact values NR)NR0/20 controls (post-provocation) 20/24 SOD patients (post-provocation)
        Lott., 1986 11 Columbus, USA Case𠄼ontrol study 156 Up to 39 patients had lipase levels ≥ 3 × ULN w/o pancreatitis e Variable e Variable e N/A d N/A d NRNR
        Lott & Lu, 1991 8 Columbus, USA Case𠄼ontrol study100 Exact number with ↑ lipase NR At least 6 patients had lipase ≥ 3 × ULN w/o pancreatitis𼈀 U/l𼅀 U/lN/A d N/A d NRNR
        Malloy., 2012 28 San Diego, USA Case𠄼ontrol study1869 119 type 2 DM patients and 29 obese non-DM patients had ↑ lipase w/o pancreatitis 13 type 2 DM patients and 2 obese non-DM patients had lipase levels ≥ 3 × ULN w/o pancreatitis s 0� U/l13� IU/l (pancreatic amylase)28 ± 20 (type 2 DM, screening), 27 ± 16 (type 2 DM, baseline) 26 ± 10 (obese, screening), 26 ± 10 (obese, baseline)42 ± 29 (type 2 DM, screening), 43 ± 33 (type 2 DM, baseline) 33 ± 26 (obese, screening), 33 ± 14 (obese, baseline)NR0/119 patients with ↑ lipase
        Manjuck., 2005 26 NY, USA Prospective cohort study245 99 had ↑ lipase (11/99 had pancreatitis) Number with lipase levels ≥ 3 × ULN NR23� U/lNR140 (cf. 389 for patients with image-proven pancreatitis) b 900 (cf. 2231 for patients with image-proven pancreatitis) b US features of pancreatitis present in 2 patients CT features of pancreatitis present in a further 9 patients a Difficult to assess c
        Masoero., 1996 50 Torino, Italy Prospective cohort study212 (63 with CRF, 98 on HD, 28 on CAPD, 23 with renal transplants) 118 had ↑ lipase levels 13 had lipase levels ≥ 3 × ULN (10 HD, 1 CAPD, 2 CRF)23� U/l0� U/l390 ± 336 in HD patients 280 ± 128 in CRF patients 255 ± 109 in CAPD patients 209 ± 93 in RT patients 148 ± 64 in controls389 ± 347 in HD patients 292 ± 211 in CRF patients 259 ± 177 in CAPD patients 175 ± 77 in RT patients 122 ± 62 in controlsUS done in 40 patients with particularly high pancreatic enzyme levels – no US features of pancreatitis in these patients0/212 patients
        Matos., 2009 62 Indianapolis and Nashville, USA Mannheim and Dresden, Germany Retrospective case series17 4 had ↑ lipase levels w/o pancreatitis Number with lipase ≥ 3 × ULN NRNRNRNRNR (maximum 4151)NR10/17 had abdominal pain (unclear if same as those patients with ↑ lipase)
        Mitura & Romanczuk, 2009 64 Siedlce, Poland Case report1 Had lipase level ≥ 3 × ULN13� IU/l28� IU/l21133184No US features of pancreatitis (CT not done)Yes (para-umbilical pain)
        Nair., 2000 30 New York, USA Prospective case series100 20 had ↑ lipase w/o pancreatitis 17 had lipase levels ≥ 3 × ULN of these, 9 did not have pancreatitis0� IU/l0� IU/lNRNRCT done in the 17 patients with lipase levels ≥ 3 × ULN – 8/17 had CT features of pancreatitis27/100 patients (number with ↑ lipase and abdominal pain NR)
        Nsien., 1992 31 Washington, USA Retrospective case series3 All 3 had lipase levels ≥ 3 × ULN23� IU/l20� IU/l497No CT features of pancreatitis in any patient0/3 patients l
        Okumura., 1998 53 Otsu, Japan Case report1 Had lipase level ≥ 3 × ULN5� IU/l25� IU/l731730No CT or US features of pancreatitisYes (NB lipase measured during Crohn's disease relapse)
        Pezzilli., 1997 69 Bologna, Italy Prospective cohort study88 6 had ↑ lipase 1 had lipase levels ≥ 3 × ULN24� IU/l0� IU/lNR (range 22�)NR (range 5�)No US features of pancreatitis in all 6 patients with ↑ lipase0/6 patients with ↑ lipase
        Quiros., 2008 32 Davis, Aurora and Stanford, USA Prospective cohort study67 21 had ↑ lipase w/o pancreatitis 14 of these had abdo pain, and 7 did not) Number with lipase ≥ 3 × ULN NR 13� U/l30� U/l136 ± 29594 ± 163No imaging was done42/67 patients (upon presentation) 14/21 patients with ↑ lipase
        Rosti., 2009 72 Bergamo, Bologna, Brescia, Catania, Catanzaro, Naples, Rome, Turin and Udine, Italy Prospective case series73 21 had ↑ lipase w/o pancreatitis 3 had lipase levels > 5 × ULN w/o pancreatitisNRNRNRNRNR0/21 patients with ↑ lipase
        Ryan., 1994 27 Iowa, USA Prospective cohort study100 17 had ↑ lipase (5 of these had clinical pancreatitis) Number with lipase ≥ 3 × ULN NR𼆐 U/l𼅰 U/l544 ± 112 in patients w/o pancreatitis (but raised enzymes) cf. 725 ± 202 in patients with clinical pancreatitis716 ± 150 in patients w/o pancreatitis (but raised enzymes) cf. 882 ± 349 in patients with clinical pancreatitisNo CT features of pancreatitis in the 17 patients with ↑ lipase US features of pancreatitis in 1/17 patients with ↑ lipase y 5/17 patients with ↑ lipase z
        Semakula., 1996 70 Bonheiden, Brussels, Ghent and Liege, Belgium Stockholm, Sweden Prospective cohort study307 Numbers with ↑ lipase NR)0𠄹 years: 17� U/l 10� years: 30� U/l 20� years: 46� U/l15� U/l47 ± 21 (range NR)88 (range 12𠄴,177)NRNR
        Sinha., 2010 65 London and Southend-on-Sea, UK Case report1 Had lipase level ≥ 3 × ULN5� IU/l25� IU/l11211700No CT features of pancreatitisYes (epigastric, then generalized)
        Smith., 2005 15 Sydney, Australia Case𠄼ontrol study1880 427 had ↑ lipase w/o pancreatitis r 62 had lipase levels ≥ 3 × ULN w/o pancreatitis𼆐 U/l27� U/l𼄀 (median)190� (median)NRNR
        Sutton., 2009 5 Nottingham, UK Case𠄼ontrol study1520 Number with ↑ lipase NR 41 had lipase levels ≥ 3 × ULN w/o pancreatitis𼌀 IU/l𼄐 IU/lNRNRNRNR
        Taes., 2000 54 Ghent, Belgium Columbus, USA Case report1 Had lipase level ≥ 3 × ULN23� U/l30� U/l3764No CT features of pancreatitis (ERCP showed minimal dilation of choledochus and Wirsung duct)Yes (patient initially admitted with chronic constipation and progressive abdominal distension with lipase of 575)
        Testoni., 2009 22 Milan, Italy Prospective cohort study25 11 had ↑ lipase Number with levels ≥ 3 × ULN NR0� IU/l13� IU/l (pancreatic amylase)NR (range 76�)NR (range 65�)0/25 had US, CT or MRCP features of pancreatitis 2/25 had MRCP features of chronic pancreatitis 8/25 had MRCP-S features of chronic pancreatitis0/25 patients
        Vantyghem., 1999 33 Lille, France Prospective cohort study164 (52 had DKA, 90 had poorly-controlled DM, 22 had well-controlled DM, 27 were controls) 31 had ↑ lipase w/o pancreatitis (19/52 patients with DKA had ↑ lipase m ) Number with lipase levels ≥ 3 × ULN NR0� IU/l0� IU/l194 ± 270 (in DKA group)348 ± 690 (in DKA group)NR n NR o
        Wen., 2005 57 Taipei, Taiwan Prospective case series37 12 had ↑ lipase w/o pancreatitis 5 had levels ≥ 3 × ULN w/o pancreatitis𼄠 U/l𼄀 U/lNR (although no child had levels ≥ 3 × ULN)NR0/37 had US features of pancreatitis 18/31 patients with BA underwent MRI and did not have any features of pancreatitis0/37 patients q
        Yoffe., 2003 37 Houston, USA Case𠄼ontrol study103 26 had ↑ lipase w/o pancreatitis Number with lipase levels 𢙓 × ULN NR114� U/l25� U/l82 ± 30 (cf. 75 ± 45 for controls)253 ± 72 (cf. 210 ± 42 for controls)NR p 0/103 patients
        Yuki., 1999 55 Izumo, Japan Case report1 Had lipase level ≥ 3 × ULN0� IU/l50� IU/lPeak NR (but > ULN)888No US or CT features of pancreatitisNil
        Zachee., 1985 16 Antwerp, Belgium Prospective case series40 26 had ↑ lipase levels (3 of these patients had pancreatitis) Number with lipase levels ≥ 3 × ULN NRNRNR4.6 ± 3.1 × ULN (w/o pancreatitis)3.5 ± 3.9 × ULN (w/o pancreatitis)NR0/37 patients w/o pancreatitis
        Zaman., 1994 56 Leuven, Belgium Case report1 Had lipase level ≥ 3 × ULN23� U/l30� U/l11042600NRNR

        AAA, abdominal aortic aneurysm CAPD, continuous ambulatory peritoneal dialysis CD, Crohn's disease CR, case report CRF, chronic renal failure CT, computed tomography DKA, diabetic ketoacidosis DM, diabetes mellitus HD, haemodialysis ICH, intracranial haemorrhage MRCP, magnetic resonance cholangiopancreatography MRCP-S, secretin-enhanced MRCP MRI, magnetic resonance imaging NR, not recorded SAH, subarachnoid haemorrhage SOD, sphincter of Oddi dysfunction UC, ulcerative colitis ULN, upper limit of normal US, ultrasonography w/o, without.