ArticleBiochemistry2011
A peptidomics strategy to elucidate the proteolytic pathways that inactivate peptide hormones.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- An expanded role for dipeptidyl peptidase 4 in cell regulation.Current opinion in hematology · 2020Review
- A Chemical Strategy for Protease Substrate Profiling.Cell chemical biology · 2019Article
- Pharmacology, physiology, and mechanisms of action of dipeptidyl peptidase-4 inhibitors.Endocrine reviews · 2014Review
- Quantitation of endogenous peptides using mass spectrometry based methods.Current opinion in chemical biology · 2013Review
- Analysis of the proteolysis of bioactive peptides using a peptidomics approach.Nature protocols · 2013Article
- Peptidomics methods for the identification of peptidase-substrate interactions.Current opinion in chemical biology · 2013Review
- Proteolysis controls endogenous substance P levels.PloS one · 2013Article
- Profiling protease activities by dynamic proteomics workflows.Proteomics · 2012Review
- Investigating endogenous peptides and peptidases using peptidomics.Biochemistry · 2011Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Proteolysis plays a key role in regulating the levels and activity of peptide hormones. Characterization of the proteolytic pathways that cleave peptide hormones is of basic interest and can, in some cases, spur the development of novel therapeutics. The lack, however, of an efficient approach to identify endogenous fragments of peptide hormones has hindered the elucidation of these proteolytic pathways. Here, we apply a mass spectrometry (MS) based peptidomics approach to characterize the intestinal fragments of peptide histidine isoleucine (PHI), a hormone that promotes glucose-stimulated insulin secretion (GSIS). Our approach reveals a proteolytic pathway in the intestine that truncates PHI at its C-terminus to produce a PHI fragment that is inactive in a GSIS assay, a result that provides a potential mechanism of PHI regulation in vivo. Differences between these in vivo peptidomics studies and in vitro lysate experiments, which showed N- and C-terminal processing of PHI, underscore the effectiveness of this approach to discover physiologically relevant proteolytic pathways. Moreover, integrating this peptidomics approach with bioassays (i.e., GSIS) provides a general strategy to reveal proteolytic pathways that may regulate the activity of peptide hormones.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.