Kinetic study of neuropeptide Y (NPY) proteolysis in blood and identification of NPY3-35: a new peptide generated by plasma kallikrein.

Details

Serval ID
serval:BIB_9B09F50AB826
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Kinetic study of neuropeptide Y (NPY) proteolysis in blood and identification of NPY3-35: a new peptide generated by plasma kallikrein.
Journal
Journal of Biological Chemistry
Author(s)
Abid K., Rochat B., Lassahn P.G., Stöcklin R., Michalet S., Brakch N., Aubert J.F., Vatansever B., Tella P., De Meester I., Grouzmann E.
ISSN
1083-351X[electronic]
Publication state
Published
Issued date
2009
Volume
284
Number
37
Pages
24715-24724
Language
english
Notes
Publication types: Journal Article
Abstract
There is little information on how neuropeptide Y (NPY) proteolysis by peptidases occurs in serum, in part because reliable techniques are lacking to distinguish different NPY immunoreactive forms and also because the factors affecting the expression of these enzymes have been poorly studied. In the present study, LC-MS/MS was used to identify and quantify NPY fragments resulting from peptidolytic cleavage of NPY(1-36) upon incubation with human serum. Kinetic studies indicated that NPY(1-36) is rapidly cleaved in serum into 3 main fragments with the following order of efficacy: NPY(3-36) >> NPY(3-35) > NPY(2-36). Trace amounts of additional NPY forms were identified by accurate mass spectrometry. Specific inhibitors of dipeptidyl peptidase IV, kallikrein, and aminopeptidase P prevented the production of NPY(3-36), NPY(3-35), and NPY(2-36), respectively. Plasma kallikrein at physiological concentrations converted NPY(3-36) into NPY(3-35). Receptor binding assays revealed that NPY(3-35) is unable to bind to NPY Y1, Y2, and Y5 receptors; thus NPY(3-35) may represent the major metabolic clearance product of the Y2/Y5 agonist, NPY(3-36).
Pubmed
Web of science
Open Access
Yes
Create date
07/10/2009 16:26
Last modification date
20/08/2019 16:02
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