AGH is a new hemoglobin alpha-chain fragment with antinociceptive activity

Ribeiro, Natalia; Toniolo, Elaine F.; Castro, Leandro M.; Russo, Lilian Cristina; Rioli, Vanessa; Ferro, Emer S.; Dale, Camila S.

doi:10.1016/j.peptides.2013.07.011

Cited by 12 publications

(14 citation statements)

References 72 publications

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“…Noteworthy is that Pep5 derived from G1/S cyclin D2 of the HeLa cell cycle was capable of inducing cell death in vitro and also in vivo when tested in rat C6 glioblastoma [14]. Furthermore, in another recent report peptide AGH, a fragment of the hemoglobin alphachain, inhibited peripheral inflammatory hyperalgesic responses through indirect activation of mμ opioid receptors (MOR), indicating a potential to control inflammatory chronic pain [61].…”

Section: Discussionmentioning

confidence: 99%

Peptidomic analysis of the anterior temporal lobe and corpus callosum from schizophrenia patients

Café-Mendes

Ferro

Torrão

et al. 2017

Journal of Proteomics

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Section: Discussionmentioning

confidence: 99%

Peptidomic analysis of the anterior temporal lobe and corpus callosum from schizophrenia patients

Café-Mendes

Ferro

Torrão

et al. 2017

Journal of Proteomics

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“…Nonetheless, the blood of slaughtered animals is a potential source of bioactive peptides. Indeed, few publications have reported that the blood proteins, especially HB, are potential sources of bioactive peptides . Bovine HB is a protein easily digestible by the human GI digestion process.…”

Section: Discussionmentioning

confidence: 99%

Food peptidomics of in vitro gastrointestinal digestions of partially purified bovine hemoglobin: low‐resolution versus high‐resolution LC‐MS/MS analyses

et al. 2016

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Consumers and governments have become aware how the daily diet may affect the human health. All proteins from both plant and animal origins are potential sources of a wide range of bioactive peptides and the large majority of those display health-promoting effects. In the meat production food chain, the slaughterhouse blood is an inevitable co-product and, today, the blood proteins remain underexploited despite their bioactive potentiality. Through a comparative food peptidomics approach we illustrate the impact of resolving power, accuracy, sensitivity, and acquisition speed of low-resolution (LR)- and high-resolution (HR)-LC-ESI-MS/MS on the obtained peptide mappings and discuss the limitations of MS-based peptidomics. From in vitro gastrointestinal digestions of partially purified bovine hemoglobin, we have established the peptide maps of each hemoglobin chain. LR technique (normal bore C18 LC-LR-ESI-MS/MS) allows us to identify without ambiguity 75 unique peptides while the HR approach (nano bore C18 LC-HR-ESI-MS/MS) unambiguously identify more than 950 unique peptides (post-translational modifications included). Herein, the food peptidomics approach using the most performant separation methods and mass spectrometers with high-resolution capabilities appears as a promising source of information to assess the health potentiality of proteins.

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“…This particular peptide itself is a cleavage product of the hemoglobin alphachain. Subsequent validation showed that this peptide exerts an antinociceptive effect in mice (Ribeiro et al, 2013).…”

Section: Current Status Of Peptidomics In Proteolysis Studiesmentioning

confidence: 99%

“…In-depth analysis using bioinformatics will reveal differentially regulated peptides as well as revealing potential peptide biomarkers and peptide-substrate identification. (Ribeiro et al, 2013) number of the cancer biomarkers identified within the past decade from urine and other biofluids, highlighting their potential as a diagnostic biomarker in ovary, pros tate and bladder cancers (Bauca et al, 2013). In recent months, there have been persistent and intense activities in biomarker research looking for new clinical candidates, which are mainly driven by the urgent need to improve the screening and the early diagnosis of certain neurodegen erative diseases and cancers.…”

Section: Application Of Peptidomics In Biomarkers Discoverymentioning

confidence: 99%

“…For comparison studies, peptide mixtures from peptidase treatment and inactive control can be subse quently tagged with different stable isotopic labels. Using this approach, Ribeiro et al had successfully identified a new endogenous bioactive peptide, AGHLDDLPGALSAL, which possibly represents a novel substrate of thimet oli gopeptidase (Ribeiro et al, 2013). This particular peptide itself is a cleavage product of the hemoglobin alphachain.…”

Section: Current Status Of Peptidomics In Proteolysis Studiesmentioning

confidence: 99%

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The emerging role of the peptidome in biomarker discovery and degradome profiling

Lai

Petrera

Schilling³

2014

Biological Chemistry

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The peptidome represents the array of endogenous peptides that are present in both the intracellular and extracellular space of the body. Peptides are constantly generated in vivo by active synthesis, and by proteolytic processing of larger precursor proteins, often yielding protein fragments that mediate a variety of physiological functions. Given that aberrant proteolysis is a hallmark of various pathological diseases, many studies have now turned to the peptidome. Differential regulation of endogenous peptides may play a role in many pathological conditions. Mass spectrometry (MS) -based investigation of peptides in a system-wide manner is currently facilitating the identification of potential biomarkers. Furthermore, peptidomic approaches have provided major contributions to the identification of protease-substrate relationships; representing one of the major challenges in understanding and therapeutically exploiting protease function in health and disease. As such, degradomic studies looking for cleavage products via peptidomics in particular, have warranted a significant research interest in recent years. Given that substantial studies are accumulating in the field of peptidomics, this review highlights recent advances of MS-based peptidomic strategies in facilitating the identification of potential peptides as novel clinical markers and protease-substrate profiling.

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AGH is a new hemoglobin alpha-chain fragment with antinociceptive activity

Cited by 12 publications

References 72 publications

Peptidomic analysis of the anterior temporal lobe and corpus callosum from schizophrenia patients

Peptidomic analysis of the anterior temporal lobe and corpus callosum from schizophrenia patients

Food peptidomics of in vitro gastrointestinal digestions of partially purified bovine hemoglobin: low‐resolution versus high‐resolution LC‐MS/MS analyses

The emerging role of the peptidome in biomarker discovery and degradome profiling

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