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Int. J. Mol. Sci. 2014, 15(9), 16787-16799; doi:10.3390/ijms150916787

Metabolism of Cryptic Peptides Derived from Neuropeptide FF Precursors: The Involvement of Insulin-Degrading Enzyme

1
Department of Chemical Sciences, University of Catania, Viale Andrea Doria 6, 95125 Catania, Italy
2
Department of Biochemistry and Neurobiology, AGH University of Science and Technology, Mickiewicza 30, 30-059 Krakow, Poland
3
Centre for Polymer and Carbon Materials, Polish Academy of Sciences, Sklodowskiej-Curie 34, 41-819 Zabrze, Poland
*
Author to whom correspondence should be addressed.
Received: 5 June 2014 / Revised: 3 September 2014 / Accepted: 9 September 2014 / Published: 22 September 2014
(This article belongs to the Collection Proteins and Protein-Ligand Interactions)
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Abstract

The term “cryptome” refers to the subset of cryptic peptides with bioactivities that are often unpredictable and very different from the parent protein. These cryptic peptides are generated by proteolytic cleavage of proteases, whose identification in vivo can be very challenging. In this work, we show that insulin-degrading enzyme (IDE) is able to degrade specific amino acid sequences present in the neuropeptide pro-NPFFA (NPFF precursor), generating some cryptic peptides that are also observed after incubation with rat brain cortex homogenate. The reported experimental findings support the increasingly accredited hypothesis, according to which, due to its wide substrate selectivity, IDE is involved in a wide variety of physiopathological processes. View Full-Text
Keywords: IDE; neuropeptide; metalloprotease; cryptome; mass spectrometry; surface plasmon resonance IDE; neuropeptide; metalloprotease; cryptome; mass spectrometry; surface plasmon resonance
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Grasso, G.; Mielczarek, P.; Niedziolka, M.; Silberring, J. Metabolism of Cryptic Peptides Derived from Neuropeptide FF Precursors: The Involvement of Insulin-Degrading Enzyme. Int. J. Mol. Sci. 2014, 15, 16787-16799.

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