Pancreatic Lipase (PNLIP) ELISA Kits

Human Pancreatic Lipase (PNLIP) interaction partners

1. Serum lipase subtype analysis cannot replace the standard lipase measurement for the diagnosis of acute pancreatitis, but the test demonstrated adequate sensitivity for use in triage or as an add-on test for serum lipase elevation.

2. Presence of methionine at position 221 in the PNLIP protein sequence causes protein misfolding and aggregation.

3. All these findings support the use of YLLIP2 in enzyme replacement therapy for the treatment of pancreatic exocrine insufficiency, a pathological situation in which an acidification of intestinal contents occurs.

4. In patients with intraductal papillary mucinous neoplasm without a history of pancreatitis, serum pancreatic lipase and amylase outside normal range are associated with risk of malignancy.

5. a novel mutation in the PNLIP gene in two brothers with congenital pancreatic lipase deficiency

6. Low PNLIP expression is associated with pancreatic cancer.

7. Triacylglycerol lipase and alpha-amylase are highly over-expressed in pancreatic cyst fluids in patients with mucinous pancreatic neoplasms.

8. Combination of two mutations with a promising one at the entrance of the catalytic cavity (K80E) negatively affected the lipase activity at neutral pH but not that at acidic pH.

9. the amplitude of the lid opening measured in solution or in a frozen solution in the presence of amphiphiles

10. Review. The structure and function of the pancreatic lipase C2 domains, based on the recent 3D structures and improved sequence alignments are reviewed.

11. analysis of human pancreatic lipase from pancreatic juice (BCR693) and a recombinant form (BCR694)

12. examination of tryptophan changes in pancreatic lipase

13. a specific method of measuring classical pancreatic lipase in human serum

14. analysis of a lid hydrophobicity pattern in pancreatic lipase

15. pancreatic lipase-colipase interactions in the presence of bile salt micelles are mediated by Val-407 and Ile-408 of PL

16. Electron paramagnetic resonance spectroscopy along with site-directed spin labeling was used to monitor the conformational changes in the human PL lid in solution to assess the effects of partners of the lipase, i.e. colipase and bile salts.

17. Introducing a negative charge close to the catalytic histidine induced a shift of the pH optimum toward acidic values but strongly reduced the lipase activity.

18. The disulfide bridge between the hinges of the lid kept the secondary structure of the lid intact, whereas the HPL was completely unfolded.

19. Trp-107 and Trp-253 contribute to the change in steady state fluorescence that is triggered by mixed micelles of inhibitor and bile salt.

Mouse (Murine) Pancreatic Lipase (PNLIP) interaction partners

1. the ability to degrade unfolded protein decreases in the aging pancreas, and this leads to reduction of pancreatic lipase activity and a decrease in lipid absorption

2. pancreatic triglyceride lipase has a critical role in dietary cholesterol absorption and a minimal role in dietary fat absorption in mice

3. PTL and CEL serve complementary functions, working together to mediate the absorption of a major portion of dietary fat and fat-soluble vitamin esters

Pig (Porcine) Pancreatic Lipase (PNLIP) interaction partners

1. Only the double mutant at higher temperature showed lid opening movement suggesting the essential role of the three residues in holding the lid in closed conformation. The lid opening dynamics was faster in octanol than water suggesting that non-polar solvents favor open conformation of the lid.

2. PPL in closed conformation is stable in water and the open conformation is driven towards closed state. The lid follows a swirling trajectory during the closure. Conformational state of the lid regulates the activity and substrate specificity of PPL. Hence, it is essential to understand the lid dynamics and the role of specific amino acid residues involved.