High impact information on PNLIPRP2

• Despite their similar amino acid sequences, PTL, PLRP1, and PLRP2 differ in important kinetic properties [1].
• PTL and PLRP2 differ in substrate specificity, bile acid inhibition, colipase requirement, and interfacial activation [1].
• This suggests that the two novel proteins also exist in other species and that some of the sequences reported to be pancreatic lipase might more likely be the orthologues of hPLRP1 or hPLRP2 in those species [2].
• Each protein has a globular amino-terminal (N-terminal) domain, which contains the catalytic site for PTL and PLRP2, and a beta-sandwich carboxyl-terminal (C-terminal) domain, which includes the predominant colipase-binding site for PTL [3].
• Pancreatic triglyceride lipase (PTL) and the homologous pancreatic lipase related protein 2 (PLRP2) provide a unique opportunity to understand the molecular mechanism of lipolysis [4].

Anatomical context of PNLIPRP2

• The pancreas expresses several members of the lipase gene family including pancreatic triglyceride lipase (PTL) and two homologous proteins, pancreatic lipase-related proteins 1 and 2 (PLRP1 and PLRP2) [1].
• Additionally, intestinal enterocytes, paneth cells and cultured cytotoxic T-cells express mRNA encoding pancreatic lipase related protein 2 [5].
• Thus, pancreatic lipase related protein 2 is a lipase that participates in the cytotoxic activity of T-cells and plays a critical role in the digestion of breast milk fats [5].
• Characterization of pancreatic lipase-related protein 2 isolated from human pancreatic juice [6].

Associations of PNLIPRP2 with chemical compounds

• PS-PLA(1), mPA-PLA(1)alpha and mPA-PLA(1)beta exhibit only PLA(1) activity, while HL, EL and PLRP2 show triacylglycerol-hydrolyzing activity in addition to PLA(1) activity [7].

Enzymatic interactions of PNLIPRP2

• PLRP2 hydrolyzed RP solubilized in micelles but less efficiently than PL (0.023+/-0.005 mumol/min/mg) [8].

Other interactions of PNLIPRP2

• Both PL and PLRP2 hydrolyzed RP solubilized in a vesicle rich-solution, and a synergic phenomenon between the two lipases was enlighten [8].
• Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity [2].

Analytical, diagnostic and therapeutic context of PNLIPRP2

• Western blotting analysis showed that these antibodies did not react with classical human pancreatic lipase (HPL) or human pancreatic lipase-related protein 1 (HPLRP1) but cross-reacted with native rat PLRP2 (RPLRP2), as well as with recombinant rat and guinea-pig PLRP2 (GPLRP2) [6].

References