Hemopressin: a novel bioactive peptide derived from the alpha1-chain of hemoglobin

Dale, Camila S.; Pagano, Rosana L.; Rioli, Vanessa

doi:10.1590/s0074-02762005000900017

Cited by 33 publications

(27 citation statements)

References 6 publications

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“…This inhibition could also reduce the level of functional angiotensins thereby further lowering the blood pressure. In contrast, hydrolysis of hemopressin by DPP III may potentially contribute to elevation of the same [95]. In addition to their role in regulating blood pressure, angiotensins also bind to their cognate receptors in brain tissues, potently contributing to the cyclicity of reproductive hormones and sexual behaviour, pituitary secretion, neuritic outgrowth, angiogenesis, kidney function, learning and memory.…”

Section: Pathophysiological Implicationsmentioning

confidence: 99%

Dipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter

2011

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Dipeptidyl peptidase III (DPP III), the sole member and representative of the M49 family of metallopeptidases, is a zinc-dependent aminopeptidase. It sequentially hydrolyses dipeptides from the N-terminal of oligopeptides ranging from three to 10 amino acid residues. Although implicated in an array of pathophysiological phenomena, the precise function of this peptidase is still unclear. However, a number of studies advocate its contribution in terminal stages of protein turnover. Altered expression of DPP III which suggests its involvement in primary ovarian carcinoma, oxidative stress (Nrf2 nuclear localization), pain, inflammation and cataractogenesis has recently led to resurgence of interest in delineating the role of the peptidase in these pathophysiological processes. This review article intends to bring forth the latest updates in this arena which may serve as a base for future studies on the peptidase.

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Section: Pathophysiological Implicationsmentioning

confidence: 99%

Dipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter

2011

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“…Dipeptidyl peptidase 3 (DPP3) is a predominantly intracellular ubiquitous zinc‐dependent metallopeptidase that is involved in the metabolism of peptides . DPP3 has been implicated in blood pressure regulation, inflammation, and pain modulation by inactivating bioactive peptides through cleavage, notably angiotensin II, enkephalins, and endorphins . Nevertheless, the biological function of DPP3 is poorly understood .…”

Section: Introductionmentioning

confidence: 99%

Circulating dipeptidyl peptidase 3 is a myocardial depressant factor: dipeptidyl peptidase 3 inhibition rapidly and sustainably improves haemodynamics

Deniau

Rehfeld²,

Santos³

et al. 2019

European J of Heart Fail

115

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Aims Acute heart failure is a high mortality disease and its pathophysiology is not completely understood. Dipeptidyl peptidase 3 (DPP3) is a cytosolic enzyme involved in angiotensin II and enkephalins cleavage. The aim of this study was to investigate the association of circulating DPP3 (cDPP3) levels and mortality in cardiogenic shock patients and to determine the effects of high cDPP3 on organ function in a heart failure (HF) model in mice. Methods and results cDPP3 was measured in 174 patients in cardiogenic shock and high cDPP3 levels were associated with an increased short‐term mortality risk (standardized hazard ratio: 1.4 (1.1–1.8)) and severe organ dysfunction. Additionally, a rapid decrease in cDPP3 in cardiogenic shock patients within 24 h of admission was associated with a favourable outcome. This study showed that injection of DPP3 induced myocardial depression (−10 ± 2% of shortening fraction) and impaired kidney haemodynamics (+0.30 ± 0.02 of renal resistive index) in healthy mice. cDPP3 inhibition by Procizumab, a specific antibody directed against cDPP3, promptly normalized cardiac function and kidney haemodynamics in an acute heart failure mouse model, with a marked reduction in oxidative stress and inflammatory signalling. Conclusion Our study demonstrated cDPP3 is a newly discovered myocardial depressant factor, the levels of which at admission are associated with mortality in severe HF patients. Furthermore, inhibition of cDPP3 by Procizumab improved haemodynamics in a mouse model of HF. Our results suggest that DPP3 could be a new biomarker and biotarget for severe HF.

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“…This family also includes the nine amino acid hemopressin peptide which is antinociceptive, reduces blood pressure, and acts as an inverse agonist at the CB1 receptors (Rioli et al. 2003; Dale et al. 2005a,b; Heimann et al.…”

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confidence: 99%

Hemopressins and other hemoglobin‐derived peptides in mouse brain: comparison between brain, blood, and heart peptidome and regulation in Cpe^fat/fat mice

Gelman

Sironi

Castro

et al. 2010

Journal of Neurochemistry

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J. Neurochem. (2010) 113, 871–880. Abstract Many hemoglobin‐derived peptides are present in mouse brain, and several of these have bioactive properties including the hemopressins, a related series of peptides that bind to cannabinoid CB1 receptors. Although hemoglobin is a major component of red blood cells, it is also present in neurons and glia. To examine whether the hemoglobin‐derived peptides in brain are similar to those present in blood and heart, we used a peptidomics approach involving mass spectrometry. Many hemoglobin‐derived peptides are found only in brain and not in blood, whereas all hemoglobin‐derived peptides found in heart were also seen in blood. Thus, it is likely that the majority of the hemoglobin‐derived peptides detected in brain are produced from brain hemoglobin and not erythrocytes. We also examined if the hemopressins and other major hemoglobin‐derived peptides were regulated in the Cpefat/fat mouse; previously these mice were reported to have elevated levels of several hemoglobin‐derived peptides. Many, but not all of the hemoglobin‐derived peptides were elevated in several brain regions of the Cpefat/fat mouse. Taken together, these findings suggest that the post‐translational processing of alpha and beta hemoglobin into the hemopressins, as well as other peptides, is up‐regulated in some but not all Cpefat/fat mouse brain regions.

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Hemopressin: a novel bioactive peptide derived from the alpha1-chain of hemoglobin

Abstract: Hemopressin (PVNFKFLSH),

Cited by 33 publications

References 6 publications

Dipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter

Dipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter

Circulating dipeptidyl peptidase 3 is a myocardial depressant factor: dipeptidyl peptidase 3 inhibition rapidly and sustainably improves haemodynamics

Hemopressins and other hemoglobin‐derived peptides in mouse brain: comparison between brain, blood, and heart peptidome and regulation in Cpe^fat/fat mice

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Hemopressin: a novel bioactive peptide derived from the alpha1-chain of hemoglobin

Abstract: Hemopressin (PVNFKFLSH),

Cited by 33 publications

References 6 publications

Dipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter

Dipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter

Circulating dipeptidyl peptidase 3 is a myocardial depressant factor: dipeptidyl peptidase 3 inhibition rapidly and sustainably improves haemodynamics

Hemopressins and other hemoglobin‐derived peptides in mouse brain: comparison between brain, blood, and heart peptidome and regulation in Cpefat/fat mice

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Hemopressins and other hemoglobin‐derived peptides in mouse brain: comparison between brain, blood, and heart peptidome and regulation in Cpe^fat/fat mice