α-Amylase is the major form of
amylasefound in humans and other mammals.
Amylase in human physiology
Although found in many tissues, amylase is most prominent in pancreatic juice and
salivawhich each have their own isoformof human α-amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies. In humans, all amylase isoformslink to chromosome1p21 (see AMY1A).
alivary amylase (ptyalin)
Amylase is found in saliva and breaks
starchdown into maltoseand dextrin. This form of amylase is also called ptyalin. It will break large, insoluble starch molecules into soluble starches ( amylodextrin, erythrodextrin, achrodextrin) producing successively smaller starches and ultimately maltose. Ptyalin acts on linear α(1,4) glycosidic linkages, but compound hydrolysisrequires an enzyme which acts on branched products. Salivary amylase is inactivated in the stomachby gastric acid. In gastric juice adjusted to pH 3.3, ptyalin was totally inactivated in 20 minutes at 370C. In contrast, 50% of amylase activity remained after 150 minutes of exposure to gastric juice at pH 4.3. [Fried, M, Abramson, S, Meyer, JH. Passage of salivary amylase through the stomach in humans. Digestive Diseases and Sciences 32:1097-1103 (1987).] Both starch, the substrate for ptyalin, and the product (short chains of glucose) are able to partially protect it against inactivation by gastric acid. Ptyalin added to buffer at pH 3.0 underwent complete inactivation in 120 minutes; however, addition of starch at a 0.1% level resulted in 10% of the activity remaining, and similar addition of starch to a 1.0% level resulted in about 40% of the activity remaining at 120 minutes. [Rosenblum, JL, Irwin, CI, Alpers, DH. Starch and glucose oligosaccharides protect salivary-type amylase activity at acid pH. American Journal of Physiology 254 (Gastrointestinal and Liver Physiology 17):G775-780 (1988).]
Optimum conditions for ptyalin
pH- 5.6–6.9:Human body temperature - 37 degrees Celsius:Presence of certain anions and activators:::Chlorine and bromine- most effective:: Iodine- less effective:: Sulfateand phosphate- least effective
Genetic variation in human ptyalin (salivary amylase)
The salivary amylase gene has undergone duplication during evolution, and DNA hybridization studies indicate that many individuals have multiple tandem repeats of the gene. The number of gene copies correlates with the levels of salivary amylase, as measured by protein blot assays using antibodies to human amylase. Perry and coworkers [Perry, GH, et al. Diet and evolution of human amylase gene copy number variation, Nature Genetics 39:1256-1260 (2007).] reported that gene copy number is associated with apparent evolutionary exposure to high starch diets. For example, a Japanese individual had 14 copies of the amylase gene (one allele with 10 copies, and a second allele with 4 copies). The Japanese diet has traditionally contained large amounts of rice starch. In contrast, a Biaka individual carried six copies (three copies on each allele). The Biaka are rainforest hunter-gatherers who have traditionally consumed a low starch diet. Perry and colleagues speculated that increased copy number of the salivary amylase gene may have enhanced survival coincident to a shift to a starchy diet during human evolution.
Pancreatic α-amylase randomly cleaves the α(1-4) glycosidic linkages of
amyloseto yield dextrin, maltoseor maltotriose. It adopts a double displacement mechanism with retention of anomeric configuration.
Amylase in human pathology
The test for amylase is easier to perform than that for
lipase, making it the primary test used to detect and monitor pancreatitis. Labs will usually measure either pancreatic amylase, or total amylase. If only pancreatic amylase is measured, an increase will not be noted with mumps or other salivary gland trauma.
Unfortunately, because of the small amount present, timing is critical when sampling
bloodfor this measurement. Blood should preferably be taken soon after a bout of pancreatitis pain, otherwise it is excreted rapidly by the kidneys.
Salivary alpha-amylase has been used as a
biomarkerfor stress that does not require a blood draw. [cite journal
last = Noto
first = Yuka
coauthors = Tetsumi Sato, Mihoko Kudo, Kiyoshi Kurata, and Kazuyoshi Hirota
year = 2005
month = December
title = The Relationship Between Salivary Biomarkers and State-Trait Anxiety Inventory Score Under Mental Arithmetic Stress: A Pilot Study.
journal = Anesthesia & Analgesia
volume = 101
issue = 6
pages = 1873–1876
publisher = Lippincott Williams & Wilkins
location = United States
issn = 0003-2999
pmid = 16301277
doi = 10.1213/01.ANE.0000184196.60838.8D
url = http://www.anesthesia-analgesia.org/cgi/content/full/101/6/1873
accessdate = 2008-03-22 ]
Increased plasma levels in humans are found in:
Salivarytrauma (including anaesthetic intubation).
Mumps— due to inflammationof the salivary glands.
Pancreatitis— because of damage to the cells that produce amylase.
Renal failure— due to reduced excretion.
Total amylase readings of over 10X the "upper limit of normal" (ULN) are suggestive of pancreatitis. 5-10x times the ULN may indicate
ileusor duodenal disease or renal failure, and lower elevations are commonly found in salivary gland disease.
* salivary -
AMY1A, AMY1B, AMY1C
* pancreatic -
* [http://macromoleculeinsights.com/alphaamylase.php The alpha-Amylase Protein]
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