Prolyl Endopeptidase: Difference between revisions
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== Function == | == Function == | ||
Although the physiological function of PEPs are not entirely understood there are several proposed functions based on their activity and localization. | |||
PEPs are thought to have a role in the degradation of [http://en.wikipedia.org/wiki/Neuropeptides neuropeptides] due to the high concentration of PEPs in the brain and the fact that PEPs have been shown to degrade several [http://en.wikipedia.org/wiki/Neuropeptides neuropeptides](vasopressin, β-endorphin, thyroliberin). The distribution of PEP in the brain has been found to be similar to that of certain receptors of [http://en.wikipedia.org/wiki/Neuropeptides neuropeptides] which supports PEPs being involved in the degradation of [http://en.wikipedia.org/wiki/Neuropeptides neuropeptide] transmitters. | PEPs are thought to have a role in the degradation of [http://en.wikipedia.org/wiki/Neuropeptides neuropeptides] due to the high concentration of PEPs in the brain and the fact that PEPs have been shown to degrade several [http://en.wikipedia.org/wiki/Neuropeptides neuropeptides](vasopressin, β-endorphin, thyroliberin). The distribution of PEP in the brain has been found to be similar to that of certain receptors of [http://en.wikipedia.org/wiki/Neuropeptides neuropeptides] which supports PEPs being involved in the degradation of [http://en.wikipedia.org/wiki/Neuropeptides neuropeptide] transmitters. | ||
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Prolyl endopeptidases are a promising therapeutic agent due to their ability to degrade the protein rich [http://en.wikipedia.org/wiki/Prolamin prolamins] and inhibit the inflammatory reaction. An early idea for treatment is to orally administer certain microbial PEPs which could directly degrade [http://en.wikipedia.org/wiki/Prolamin prolamins] in the intestine and reduce the auto-immune response. The key for this possibility is to be able to protect the PEPs from being degraded by gastric acids while allowing them to be able to be functional in the small intestine once the acidity is decreased. | Prolyl endopeptidases are a promising therapeutic agent due to their ability to degrade the protein rich [http://en.wikipedia.org/wiki/Prolamin prolamins] and inhibit the inflammatory reaction. An early idea for treatment is to orally administer certain microbial PEPs which could directly degrade [http://en.wikipedia.org/wiki/Prolamin prolamins] in the intestine and reduce the auto-immune response. The key for this possibility is to be able to protect the PEPs from being degraded by gastric acids while allowing them to be able to be functional in the small intestine once the acidity is decreased. | ||
Research by Ehren, Govindarajan, Morón, Minshull, and Khosla | Research by Ehren, Govindarajan, Morón, Minshull, and Khosla has shown the ability to engineer the prolyl endopeptidase of ''Sphingomonas capsulata'' to increase the activity of this PEP under simulated gastric conditions showing the relevance of PEPs as a potential therapeutic agent for [http://en.wikipedia.org/wiki/Coeliac_disease Celiac Disease] [5]. | ||
=== Neurological Disorders === | === Neurological Disorders === | ||
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== References == | == References == | ||
[] Besedin DV, Rudenskaya GN. Proline-Specific Endopeptidases. Russ. J. Bioorg. Chem. 2002 Feb 28; 29(1)1-17. | [] Besedin DV, Rudenskaya GN. Proline-Specific Endopeptidases. Russ. J. Bioorg. Chem. 2002 Feb 28; 29(1)1-17. | ||
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[] Shan L, Marti T, Sollid LM, Gray GM, Khosla C. Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue. Biochem. J. 2008; 383 311-18. | [] Shan L, Marti T, Sollid LM, Gray GM, Khosla C. Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue. Biochem. J. 2008; 383 311-18. | ||
[5] Ehren J, Govindarajan S, Morón B, Minshull J, Khosla C. Protein engineering of improved prolyl endopeptidases for celiac sprue therapy. Protein Eng. Des. Sel. 2008 Oct 4; 21(12)699-707. | |||
