High expression in adult horse of PLRP2 displaying a low phospholipase activity.
Abstract: The physiological role of the two lipase-related proteins, PLRP1 and PLRP2, still remains obscure although some propositions have been made concerning PLRP2. In this paper, we report the presence of high amounts of PLRP2 in adult horse pancreas whereas no PLRP1 could be detected. As well, a non-parallel expression of PLRP2 and PLRP1 is observed in adult cat and dog, since no PLRP2 could be detected in these two species. In adult ox, neither PLRP2 nor PLRP1 could be found. These findings are in favor of a different regulation of the expression of the genes encoding pancreatic lipase and the related proteins according to the species. The cDNA encoding horse PLRP2 has been cloned and the protein expressed in insect cells. Both native and recombinant PLRP2 display the same catalytic properties. They possess a moderate lipase activity, inhibited by bile salts and not restored by colipase. Interestingly, they differ from PLRP2 from other species by their very low phospholipase activity indicating that PLRP2 could not be considered as a general phospholipase as previously postulated. This work highlights the variability of the properties of PLRP2 and rises the question of the physiological function of this protein in adult according to the species.
Publication Date: 2002-03-21 PubMed ID: 11904221DOI: 10.1016/s0167-4838(01)00309-0Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article discusses the study conducted on two lipase-related proteins, PLRP1 and PLRP2, present in various animal species including horses, cats, and dogs. The study evaluates their levels of expression, the regulatory differences across species and their functions, especially concerning the phospholipase activity of PLRP2.
Research Purpose and Methodology
- The main purpose of this research was to understand the physiological role of two lipase-related proteins, PLRP1 and PLRP2, whose functions are not well established.
- The researchers analysed the presence and expression of these proteins in the pancreas of various animal species like horses, cats, dogs and ox.
- The method involved cloning the cDNA encoding horse PLRP2 and expressing the protein in insect cells.
Findings and Observations
- High amounts of PLRP2 were found in the pancreas of adult horses, while no PLRP1 could be detected.
- In adult cats and dogs, PLRP2 was absent while the presence of PLRP1 was noted, indicating a non-parallel expression of these two proteins in these species.
- In the case of adult ox, neither PLRP2 nor PLRP1 could be found.
- These findings suggest different regulations of the genes encoding pancreatic lipase and the related proteins across different species.
Properties of PLRP2
- Both native and recombinant PLRP2 showed the same catalytic properties and displayed moderate lipase activity.
- This activity was inhibited by bile salts and was not restored by colipase.
- The PLRP2 from horses showed very low phospholipase activity, differing from the PLRP2 of other species. This contradicts the previous notion of considering PLRP2 as a general phospholipase.
Conclusion
- This research emphasized the variability of the properties of PLRP2 and raised questions about its physiological function in adults according to different species.
- Further research is needed to fully understand the biological role and significance of PLRP2 in different animals.
Cite This Article
APA
Jayne S, Kerfelec B, Foglizzo E, Chapus C, Crenon I.
(2002).
High expression in adult horse of PLRP2 displaying a low phospholipase activity.
Biochim Biophys Acta, 1594(2), 255-265.
https://doi.org/10.1016/s0167-4838(01)00309-0 Publication
Researcher Affiliations
- INSERM - U476 Nutrition humaine et lipides, 18 Avenue Mozart, 13009 Marseille, France.
MeSH Terms
- Amino Acid Sequence
- Animals
- Base Sequence
- Cell Line
- Cloning, Molecular
- DNA, Complementary / biosynthesis
- Gene Library
- Horses / metabolism
- Insecta
- Kinetics
- Lipase / biosynthesis
- Lipase / genetics
- Molecular Sequence Data
- Pancreas / metabolism
- Phospholipases / metabolism
- Recombinant Proteins / metabolism
- Species Specificity
Citations
This article has been cited 7 times.- Zhu G, Fang Q, Zhu F, Huang D, Yang C. Structure and Function of Pancreatic Lipase-Related Protein 2 and Its Relationship With Pathological States. Front Genet 2021;12:693538.
- Hecker N, Sharma V, Hiller M. Convergent gene losses illuminate metabolic and physiological changes in herbivores and carnivores. Proc Natl Acad Sci U S A 2019 Feb 19;116(8):3036-3041.
- Xiao X, Lowe ME. The β5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2). J Biol Chem 2015 Nov 27;290(48):28847-56.
- Xiao X, Ross LE, Sevilla WA, Wang Y, Lowe ME. Porcine pancreatic lipase related protein 2 has high triglyceride lipase activity in the absence of colipase. Biochim Biophys Acta 2013 Sep;1831(9):1435-41.
- Fieker A, Philpott J, Armand M. Enzyme replacement therapy for pancreatic insufficiency: present and future. Clin Exp Gastroenterol 2011;4:55-73.
- Schreiber R, Taschler U, Preiss-Landl K, Wongsiriroj N, Zimmermann R, Lass A. Retinyl ester hydrolases and their roles in vitamin A homeostasis. Biochim Biophys Acta 2012 Jan;1821(1):113-23.
- Person MD, Shen J, Traner A, Hensley SC, Lo HH, Abbruzzese JL, Li D. Protein fragment domains identified using 2D gel electrophoresis/MALDI-TOF. J Biomol Tech 2006 Apr;17(2):145-56.
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