Combination of snap freezing, differential pH two-dimensional reverse-phase high-performance liquid chromatography, and iTRAQ technology for the peptidomic analysis of the effect of prolyl oligopeptidase inhibition in the rat brain

Tenorio-Laranga, Jofre; Valero, M. Luz; Männistö, Pekka T.; Pino, Manuel M. Sánchez del; Garcı́a-Horsman, J. Arturo

doi:10.1016/j.ab.2009.06.019

Cited by 24 publications

(46 citation statements)

References 53 publications

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“…The identification of endogenous Prep substrates is a major part of the effort to elucidate Prep-regulated pathways related to cognition (9,23,28,35). These studies integrate pharmacological inhibition of Prep with postmortem measurements of peptide levels in the central nervous system.…”

Section: Peptidomics Of Prep In the Central Nervous Systemmentioning

confidence: 99%

“…2). Since these initial efforts, similar approaches have been used to study other peptidases as well (23)(24)(25)(26)(27)(28)31,32). Fig.…”

Section: Introductionmentioning

confidence: 99%

“…In such experiments, known endogenous peptides and, importantly, previously unidentified peptides, including posttranslationally modified versions of known peptides, can be measured (29). Recently, peptidomics has been applied to identify peptidase-regulated peptides, including substrates, by quantifying changes in the tissue peptidome as a function of peptidase activity (23)(24)(25)27,28,31,32) (Fig. 2).…”

Section: Introductionmentioning

confidence: 99%

“…For example, in vitro assays with recombinant enzyme cannot account for protein-protein interactions or spatial localization that can promote or prevent interactions between peptidases and candidate substrates (22). To overcome these challenges, recent studies have begun to look at the direct impact of peptidase activity on the peptides in cells and tissues through the application of mass spectrometry (MS)-based peptidomics (23)(24)(25)(26)(27)(28). In these experiments, changes in the peptide profile as a function of peptidase activity can reveal substrates, products, and pathways regulated by a peptidase in vivo.…”

Section: Introductionmentioning

confidence: 99%

“…In the analysis of prolyl peptidases, pharmacology (23,28) and genetics (23,24) have both been employed to inactivate the enzymes. The benefit of genetic knockouts is that they are highly specific, effectively remove all enzyme activity, and can be used to target any peptidase without needing any specific reagents.…”

Section: Introductionmentioning

confidence: 99%

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Peptidomics of the Prolyl Peptidases

Lone

Nolte

Tinoco

et al. 2010

AAPS J

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Abstract. The prolyl peptidases are a family of enzymes characterized by a biochemical preference for cleaving proline-containing peptides. The members of this enzyme family include prolyl endopeptidase, prolyl endopeptidase-like, dipeptidyl peptidase 4 (DPP4), DPP7, DPP8, DPP9, and fibroblast activation protein. DPP4 is the best studied member of the family, due to its role in physiological glucose tolerance, exerted through the regulation of the insulinotropic peptide glucagon-like peptide-1. While other members of the prolyl peptidase family have also been implicated in various (patho)physiological processes, the underlying peptides and pathways regulated by these enzymes are less clear. The identification of endogenous substrates of the prolyl peptidases is an important step in elucidating the molecular mechanisms of these enzymes. Here, we highlight the utility of liquid chromatography-mass spectrometry-based peptidomics to enable the discovery of endogenous prolyl peptidase substrates directly from tissues, and demonstrate the utility of this information in understanding the biochemical and physiological functions of the prolyl peptidases.

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Section: Peptidomics Of Prep In the Central Nervous Systemmentioning

confidence: 99%

“…2). Since these initial efforts, similar approaches have been used to study other peptidases as well (23)(24)(25)(26)(27)(28)31,32). Fig.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Peptidomics of the Prolyl Peptidases

Lone

Nolte

Tinoco

et al. 2010

AAPS J

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Targeted modification of wheat grain protein to reduce the content of celiac causing epitopes

Osorio

Wen

Gemini

et al. 2012

Funct Integr Genomics

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The prolamin peptides in wheat gluten and in the homologous storage proteins of barley and rye cause painful chronic erasure of microvilli of the small intestine epithelium in celiac patients. If untreated, it can lead to chronic diarrhea, abdominal distension, osteoporosis, weight-loss due to malabsorption of nutrients, and anemia. In addition to congenital cases, life-long exposure to gluten proteins in bread and pasta can also induce development of celiac sprue in adults. To date, the only effective treatment is life-long strict abstinence from the staple food grains. Complete exclusion of dietary gluten is, however, difficult due to use of wheat in many foods, incomplete labeling and social constraints. Thus, finding alternative therapies for this most common foodborne disease remained an active area of research, which has led to many suggestions in last few years. The pros and cons associated with these therapies were reviewed in the present communication. As different celiac patients are immunogenic to different members of the undigestible proline/glutamine rich peptides of ~149 gliadins and low molecular weight glutenin subunits as well as the six high molecular weight glutenin subunits, an exhaustive digestion of the immunogenic peptides in the stomach, duodenum, jejunum, and ileum of celiacs is required. In view of the above, we evaluated the capacity of cereal grains to synthesize and store the enzymes prolyl endopeptidase from Flavobacterium meningosepticum and the barley cysteine endoprotease B2, which in combination are capable of detoxifying immunogenic gluten peptides in a novel treatment of celiac disease.

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Stability comparison between sample preparation procedures for mass spectrometry-based targeted or shotgun peptidomic analysis

Beaudry¹

2010

Analytical Biochemistry

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Combination of snap freezing, differential pH two-dimensional reverse-phase high-performance liquid chromatography, and iTRAQ technology for the peptidomic analysis of the effect of prolyl oligopeptidase inhibition in the rat brain

Cited by 24 publications

References 53 publications

Peptidomics of the Prolyl Peptidases

Peptidomics of the Prolyl Peptidases

Targeted modification of wheat grain protein to reduce the content of celiac causing epitopes

Stability comparison between sample preparation procedures for mass spectrometry-based targeted or shotgun peptidomic analysis

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