View source for Trypsin

[[File:Aktivační kaskáda pankreatu.jpg|thumb|Activation cascade of panreatic enzymes in CZ]]
'''Trypsin''' (in the form of [[trypsinogen]]), like other pancreatic enzymes, is produced by [[acinous cells of the pancreas]] in the inactive form so called proenzyme and is secreted into the duodenum via the pancreatic duct.It is an enzyme that hydrolytically cleaves proteins just like pepsin. It differs from pepsin by its optimal pH for its function, ie it is active in the alkaline environment of the duodenum. Activation of pancreatic enzymes takes place in an activation cascade that is initiated by intestinal [[enterokinase]].Trypsin passes partially into the bloodstream, where it can be meassured by doctors using immunological methods (RIA). 

Usually trypsin is meassured together with trypsinogen and trypsin complex with α1-proteinase inhibitor ([[α1-antitrypsin]]), depending on the detection methodology used. '''Physiological values range from 100 to 400 µg / l''', which depend on the type of detection method used. In acute pancreatitis we show a several-fold increase (up to 20,000 µg / l), a slight increase is in [[cholelithiasis]]. Decreased values indicate [[chronic pancreatitis]], [[Cystic Fibrosis|cystic fibrosis]]. Decreased and elevated trypsin levels can be seen in [[Pancreatic Cancer|pancreatic cancer]]. 

<noinclude>
==Links==

*se svolením autora převzato z KOCNA, Petr. ''GastroLab : MiniEncyklopedie laboratorních metod v gastroenterologii'' [online]. ©2002. Poslední revize 2011-01-08, [cit. 2011-03-04]. <http://www1.lf1.cuni.cz/~kocna/glab/glency1.htm>.
*https://www.wikiskripta.eu/w/Trypsin

===Source===

* HERNÁNDEZ, CA, et al. Determination of plasma trypsin-like activity in healthy subjects, patients with mild to moderate alcoholic chronic pancreatitis, and patients with nonjaundice pancreatic cancer. ''Dig Dis Sci. ''2005, vol. 50, no. 11, s. 2165-9, ISSN 0163-2116 (Print), 1573-2568 (Electronic). PMID: 16240234.

* LEMPINEN, M, et al. Sequential changes in pancreatic markers in acute pancreatitis. ''Scand J Gastroenterol. ''2003, vol. 38, no. 6, s. 666-75, ISSN 0036-5521 (Print), 1502-7708 (Electronic). PMID: 12825877.

* HEDSTRÖM, J, et al. A comparison of serum trypsinogen-2 and trypsin-2-alpha1-antitrypsin complex with lipase and amylase in the diagnosis and assessment of severity in the early phase of acute pancreatitis. ''Am J Gastroenterol. ''2001, vol. 96, no. 2, s. 424-30, ISSN 0002-9270 (Print), 1572-0241 (Electronic). PMID: 11232685.

* MUNOZ, A, et al. Diagnosis and management of acute pancreatitis. ''Am Fam Physician. ''2000, vol. 62, no. 1, s. 164-74, ISSN 0002-838X (Print), 1532-0650 (Electronic). PMID: 10905786.

* KEMPPAINEN, E, et al. Time course profile of serum trypsinogen-2 and trypsin-2-alpha1-antitrypsin in patients with acute pancreatitis. ''Scand J Gastroenterol. ''2000, vol. 35, no. 11, s. 1216-20, ISSN 0036-5521 (Print), 1502-7708 (Electronic). PMID: 11145296.

* OJIMA, H, et al. Significance of the measurement of serum trypsin in patients surgically treated for gastric cancer. ''Hepatogastroenterology. ''2000, vol. 47, no. 36, s. 1773-6, ISSN 0172-6390. PMID: 11149054.</noinclude>
[[Category:Gastroenterology]]
[[Category:Biochemistry]]
[[Category:Physiology]]
[[Category:Internal Medicine]]
{{editorcheck}}