|
|
||||||||
Clinical Chemistry, Vol 40, 1761-1765, Copyright © 1994 by American Association for Clinical Chemistry
J Hedstrom, J Leinonen, V Sainio and UH Stenman
Department of Clinical Chemistry, Helsinki University Central Hospital, Finland.
We developed a sensitive time-resolved immunofluorometric assay (IFMA) for trypsin-2 complexed with alpha 1-antitrypsin (AAT). We used a trypsin-2-specific monoclonal antibody on the solid phase and a europium-labeled polyclonal antibody to AAT as tracer. The detection limit is 0.05 microgram/L and the range of linearity extends to 100 micrograms/L. We compared the clinical utility of the trypsin-2-AAT assay with that of free trypsinogen-2 and amylase in serum by studying 120 healthy subjects, 29 patients with acute pancreatitis, 11 with extrahepatic biliary obstruction, and 34 with acute abdominal disorders of extrapancreatic origin. In patients with acute pancreatitis the median concentration of trypsin-2-AAT in serum was 59-fold that in healthy controls, 42-fold that in patients with biliary obstruction, and 33-fold that in patients with acute abdominal disorders of extrapancreatic origin. These differences are greater than those for trypsinogen-2 (19-, 20-, and 28-fold, respectively) and amylase (5.4-, 6.5-, and 5.4-fold, respectively). Compared with the assays of free trypsinogen-2 and amylase, our assay of trypsin-2-AAT improved the clinical specificity for acute pancreatitis by eliminating false- positive results in our control groups. Increased concentrations of trypsin-2-AAT and trypsinogen-2 were also observed in patients with chronic renal failure undergoing dialysis.
The following articles in journals at HighWire Press have cited this article:
![]() |
M. Stenman, M. Ainola, L. Valmu, A. Bjartell, G. Ma, U.-H. Stenman, T. Sorsa, R. Luukkainen, and Y. T. Konttinen Trypsin-2 Degrades Human Type II Collagen and Is Expressed and Activated in Mesenchymally Transformed Rheumatoid Arthritis Synovitis Tissue Am. J. Pathol., October 1, 2005; 167(4): 1119 - 1124. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Paju, J. Vartiainen, C. Haglund, O. Itkonen, K. von Boguslawski, A. Leminen, T. Wahlstrom, and U.-H. Stenman Expression of Trypsinogen-1, Trypsinogen-2, and Tumor-Associated Trypsin Inhibitor in Ovarian Cancer: Prognostic Study on Tissue and Serum Clin. Cancer Res., July 15, 2004; 10(14): 4761 - 4768. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. M. Andersen, J. Hedstrom, E. Kemppainen, P. Finne, and P. Puolakkainen The Ratio of Trypsin-2-{{alpha}}1-Antitrypsin to Trypsinogen-1 Discriminates Biliary and Alcohol-induced Acute Pancreatitis Clin. Chem., February 1, 2001; 47(2): 231 - 236. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Hedstrom, C. Haglund, E. Kemppainen, M. Leinimaa, J. Leinonen, and U.-H. Stenman Time-resolved Immunofluorometric Assay of Trypsin-1 Complexed with {alpha}1-Antitrypsin in Serum: Increased Immunoreactivity in Patients with Biliary Tract Cancer Clin. Chem., October 1, 1999; 45(10): 1768 - 1773. [Abstract] [Full Text] [PDF] |
||||
![]() |
A BORGSTROM, K OHLSSON, E KEMPPAINEN, J HEDSTROM, and U-H STENMAN Do trypsin 2-alpha -1-antitrypsin complexes occur naturally in the circulation? • Reply Gut, December 1, 1998; 43(6): 861 - 862. [Full Text] [PDF] |
||||
![]() |
E Kemppainen, J Hedstrom, P Puolakkainen, J Halttunen, V Sainio, R Haapiainen, E Kivilaakso, and U-H Stenman Increased serum trypsinogen 2 and trypsin 2-alpha 1 antitrypsin complex values identify endoscopic retrograde cholangiopancreatography induced pancreatitis with high accuracy Gut, November 1, 1997; 41(5): 690 - 695. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Hedstrom, V. Sainio, E. Kemppainen, R. Haapiainen, E. Kivilaakso, T. Schroder, J. Leinonen, and U.-H. Stenman Serum complex of trypsin 2 and (alpha)(sub 1) antitrypsin as diagnostic and prognostic marker of acute pancreatitis: clinical study in consecutive patients BMJ, August 10, 1996; 313(7053): 333 - 337. [Abstract] [Full Text] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |