Serum pancreatic phospholipase A2 and prophospholipase A2 in acute pancreatitis and after endoscopic retrograde pancreatography

1993 ◽  
Vol 28 (5) ◽  
pp. 679-686 ◽  
Author(s):  
Kazuko Yamamoto ◽  
Yasuhisa Shinomura ◽  
Hiromasa Tojo ◽  
Mitsuhiro Okamoto ◽  
Sciichiro Tarui
Keyword(s):  
Acute Pancreatitis ◽  
Phospholipase A2 ◽  
Endoscopic Retrograde Pancreatography ◽  
Endoscopic Retrograde ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2

Pancreatic phospholipase A2 in cerulein-induced acute pancreatitis in the rat

1993 ◽  
Vol 14 (3) ◽  
pp. 261-267
Author(s):  
Antti J. Hietaranta ◽  
Heikki J. Aho ◽  
Timo J. Nevalainen
Keyword(s):  
Acute Pancreatitis ◽  
Phospholipase A2 ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2

Immunoreactive pancreatic phospholipase A2 and catalytically active phospholipases A2 in serum from patients with acute pancreatitis.

1988 ◽  
Vol 34 (6) ◽  
pp. 1052-1054 ◽  
Author(s):  
J U Eskola ◽  
T J Nevalainen ◽  
P Kortesuo
Keyword(s):  
Acute Pancreatitis ◽  
Catalytic Activity ◽  
Phospholipase A2 ◽  
Pla2 Activity ◽  
Serum Samples ◽  
Phospholipases A2 ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2 ◽  
Before And After ◽  
Pla2 Enzyme

Abstract Measuring the content of immunoreactive pancreatic phospholipase A2 (PLA2; EC 3.1.1.4) and the catalytic activity of PLA2 in serum samples from five patients with acute pancreatitis, we found no correlation between these two measurements overall. To test the specificity of the method for catalytic PLA2, we measured PLA2 activity in serum samples before and after immunoadsorption with an antiserum to human pancreatic PLA2. The results suggest the presence of at least two immunologically distinct PLA2 enzyme proteins in sera from these patients. One of the enzymes is pancreatic in origin and may exist in active, inactive, or inhibited form. The activity profile of the second PLA2 enzyme in serum during acute pancreatitis differs from that for other common pancreatic enzymes. In the present experiment, the catalytic activity was not removed by treatment with the anti-human pancreatic PLA2 antiserum. The source of this second PLA2 activity is unknown. Some samples contained increased activities of both PLA2 forms.

Severe acute pancreatitis is related to increased early urinary levels of the activation peptide of pancreatic phospholipase A2

Pancreatology ◽  
2002 ◽  
Vol 2 (6) ◽  
pp. 535-542 ◽  
Author(s):  
Jens M. Mayer ◽  
Michael Raraty ◽  
John Slavin ◽  
Esko Kemppainen ◽  
John Fitzpatrick ◽  
...  
Keyword(s):  
Acute Pancreatitis ◽  
Phospholipase A2 ◽  
Severe Acute Pancreatitis ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2 ◽  
Urinary Levels ◽  
Activation Peptide

Molecular Characterization of Murine Pancreatic Phospholipase A2

2001 ◽  
Vol 20 (3) ◽  
pp. 149-157 ◽  
Author(s):  
Asim K. Mandal ◽  
Zhongjian Zhang ◽  
Janice Y. Chou ◽  
Drazen Zimonjic ◽  
Catherine L. Keck ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Molecular Characterization ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2

Contiguous Binding of Decylsulfate on the Interface-Binding Surface of Pancreatic Phospholipase A2

Biochemistry ◽  
2008 ◽  
Vol 47 (9) ◽  
pp. 2899-2907 ◽  
Author(s):  
Shi Bai ◽  
Mahendra K. Jain ◽  
Otto G. Berg
Keyword(s):  
Phospholipase A2 ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2 ◽  
Binding Surface

Genetic analysis of pancreatic phospholipase A2 (PLA2G1B) in patients with chronic pancreatitis

Pancreatology ◽  
2022 ◽  
Author(s):  
Maren Ewers ◽  
Denise Epple ◽  
Peter Bugert ◽  
Jonas Rosendahl ◽  
Heiko Witt
Keyword(s):  
Chronic Pancreatitis ◽  
Genetic Analysis ◽  
Phospholipase A2 ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2
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