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Acute pancreatitis trypsinogen

The trypsin family of proteases plays a role in acute and chronic pancreatitis, as well as leads to its ultimate destruction [4, 105]. In pancreatitis, active exocrine enzymes are prematurely released inside the pancreatic duct. Various factors can contribute to the development of acute pancreatitis. Trypsinogen, chymotrypsinogen, procarboxypeptidase, and proelastase are inactive proforms of proteolytic enzymes produced by the pancreatic acinar cells. Following secretion these enzymes are activated in a cascade that converts trypsinogen to trypsin in the duodenum and/or small intestine. [Pg.239]

H4. Hedstrom, J., Korvuo, A., Kenkimaki, P., Tikanoja, S., Haapiainen, R., and Kivilaaks, E., Urinary trypsinogen-2 test strip for acute pancreatitis. Lancet 347,729—730 (1996). [Pg.74]

N3. Neoptolemos, J., Kemppainen, E., Mayer, J., Fitzpatric, J., Raraty, M., and Slavin, J., Early prediction of severity in acute pancreatitis by urinary trypsinogen activation peptide A multicentre study. Lancet 255, 1955-1960 (2000). [Pg.77]

T3. Tenner, S., Fernandez-del Castillo, C., Washaw, A., Steinberg, W., Hermon-Taylor, J., and Valenzuela, J. E., Urinary trypsinogen activation peptide (TAP) predicts severity in patients with acute pancreatitis. Int. J. Pancreatol. 21,105-110 (1997). [Pg.80]

When trypsinogens are converted to active TRY, a small peptide is cleaved from the N-terminal region of trypsino-gen (trypsinogen activation peptide or TAP). Determinations of urinary TAP seem to provide useful information on the severity of acute pancreatitis,... [Pg.622]

In healthy individuals, free trypsinogen-1 is the major form found in serum. After an attack of acute pancreatitis, serum TRY-1 rises in parallel with serum AMY activity to peak values ranging from 2 to 400 times the upper reference limit. [Pg.622]

The distribution of the different forms of TRY-1 appears to be related to the type and severity of the acute pancreatitis. Thus in the mildest form of acute pancreatitis, 80% to 99% of the TRY-1 exists as free trypsinogen-1, with smaller proportions existing as bound TRY-1. In the more severe forms, in which mortality ranges from 20% to more than 50%, the proportion of free trypsinogen-1 may be as low as 30% of the total, with appreciable proportions existing as the tti-antitrypsin- and a2-macroglobulin-boimd TRY-l. ... [Pg.622]

As noted above, newly formed TRY is inactivated by complexing with tti-antitrypsin, and assays of this serum complex with TRY-2 have preliminarily shown that this determination can be superior to that of either trypsinogen-2 or AMY in acute pancreatitis. To date, no confirmation of these findings has been published. [Pg.622]

Kemppainen EA, Hedstrb JI, Puolakkainen PA, Sainio VS, Haapiainen RK, Perhoniemi V, et al. Rapid measurement of urinary trypsinogen 2 as a screening test for acute pancreatitis. N Engi J Med 1997 336 1788-93. [Pg.639]

E. A. Kemppainen, J. I. Hedotrom, P. A. Puolakkainen, et al. Rapid Measurement of Urinary Trypsinogen-2 as a screening test for acute pancreatitis. New England Journal of Medicine 336, 1788 (1997),... [Pg.132]

Acute pancreatitis is a result of anatomical changes that arise from two events. The first is the autodigestion of the acinar cells by inappropriate activation of the pancreatic enzymes (especially trypsinogen) within the cell. The second is... [Pg.173]

Hedstrom, J. et al. 1996. Urine trypsinogen-2 as a marker of acute pancreatitis. Clinical Chemistry 42 685-690. [Pg.112]


See other pages where Acute pancreatitis trypsinogen is mentioned: [Pg.74]    [Pg.77]    [Pg.90]    [Pg.622]    [Pg.127]    [Pg.127]    [Pg.1450]    [Pg.259]    [Pg.240]    [Pg.764]   
See also in sourсe #XX -- [ Pg.127 ]




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