Roberto Motterlini

ORCID: 0000-0003-2684-2612
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About
Contact & Profiles
Research Areas
  • Heme Oxygenase-1 and Carbon Monoxide
  • Hemoglobin structure and function
  • Neonatal Health and Biochemistry
  • Eicosanoids and Hypertension Pharmacology
  • Cannabis and Cannabinoid Research
  • Neuroscience of respiration and sleep
  • Thermal Regulation in Medicine
  • X-ray Diffraction in Crystallography
  • Cardiac Arrest and Resuscitation
  • Crystallization and Solubility Studies
  • Alcohol Consumption and Health Effects
  • Nitric Oxide and Endothelin Effects
  • Genomics, phytochemicals, and oxidative stress
  • Adipose Tissue and Metabolism
  • Organ Transplantation Techniques and Outcomes
  • Cancer, Hypoxia, and Metabolism
  • High Altitude and Hypoxia
  • Optimism, Hope, and Well-being
  • Mitochondrial Function and Pathology
  • Hemoglobinopathies and Related Disorders
  • Traumatic Brain Injury and Neurovascular Disturbances
  • Biomarkers in Disease Mechanisms
  • Autophagy in Disease and Therapy
  • Intracerebral and Subarachnoid Hemorrhage Research
  • Metabolism and Genetic Disorders

Inserm
2016-2025

Institut Mondor de Recherche Biomédicale
2016-2025

Université Paris-Est Créteil
2016-2025

Paris-Est Sup
2012-2023

Beth Israel Deaconess Medical Center
2006-2016

Zero to Three
2014

Assistance Publique – Hôpitaux de Paris
2013

Italian Institute of Technology
2008-2012

Hamamatsu University School of Medicine
2012

Jagiellonian University
2012

The transcription factor Nrf2, which normally exists in an inactive state as a consequence of binding to cytoskeleton-associated protein Keap1, can be activated by redox-dependent stimuli. Alteration the Nrf2-Keap1 interaction enables Nrf2 translocate nucleus, bind antioxidant-responsive element (ARE) and initiate genes coding for detoxifying enzymes cytoprotective proteins. This response is also triggered class electrophilic compounds including polyphenols plant-derived constituents....

10.1042/bj20021619 article EN Biochemical Journal 2003-04-25

Carbon monoxide (CO) is generated in living organisms during the degradation of heme by enzyme oxygenase, which exists constitutive (HO-2 and HO-3) inducible (HO-1) isoforms. gas known to dilate blood vessels a manner similar nitric oxide has been recently shown possess antiinflammatory antiapoptotic properties. We report that series transition metal carbonyls, termed here carbon monoxide-releasing molecules (CO-RMs), liberate CO elicit direct biological activities. Specifically,...

10.1161/hh0202.104530 article EN Circulation Research 2002-02-08

Carbon monoxide, which is generated in mammals during the degradation of heme by enzyme oxygenase, an important signaling mediator. Transition metal carbonyls have been recently shown to function as carbon monoxide-releasing molecules (CO-RMs) and elicit distinct pharmacological activities biological systems. In present study, we report that a water-soluble form CO-RM promotes cardioprotection vitro vivo. Specifically, found tricarbonylchloro(glycinato)ruthenium(II) (CORM-3) stable water at...

10.1161/01.res.0000084381.86567.08 article EN Circulation Research 2003-07-08

The enzyme heme oxygenase‐1 (HO‐1) is a cytoprotective and anti‐inflammatory protein that degrades to produce biliverdin/bilirubin, ferrous iron carbon monoxide (CO). properties of HO‐1 are related inhibition adhesion molecule expression reduction oxidative stress, while exogenous CO gas treatment decreases the production inflammatory mediators such as cytokines nitric oxide (NO). CO‐releasing molecules (CO‐RMs) novel group substances identified by our capable modulating physiological...

10.1038/sj.bjp.0706241 article EN British Journal of Pharmacology 2005-05-09

Carbon monoxide (CO) is emerging as an important and versatile mediator of physiological processes to the extent that treatment animals with exogenous CO gas has beneficial effects in a range vascular- inflammatory-related disease models. The recent discovery certain transition metal carbonyls function CO-releasing molecules (CO-RMs) biological systems highlighted potential exploiting this similar classes compounds stratagem deliver for therapeutic purposes. Here we describe biochemical...

10.1096/fj.04-2169fje article EN The FASEB Journal 2004-11-19

Mesenchymal stem cells (MSCs) protect tissues against cell death induced by ischemia/reperfusion insults. This therapeutic effect seems to be controlled physiological cues released the local microenvironment following injury. Recent lines of evidence indicate that MSC can communicate with their through bidirectional exchanges mitochondria. In particular, in vitro and vivo studies report MSCs rescue injured delivery own However, role mitochondria conveyed from somatic remains unknown. By...

10.1038/cdd.2017.51 article EN cc-by-nc-nd Cell Death and Differentiation 2017-05-19

Carbon monoxide (CO) is continuously produced in mammalian cells during the degradation of heme. It a stable gaseous molecule that reacts selectively with transition metals specific redox state, and these characteristics restrict interaction CO defined biological targets transduce its signaling activity. Because high affinity for ferrous heme, can be grouped into heme-containing proteins, representing large variety sensors enzymes series diverse function cell organism. Despite this notion,...

10.1152/ajpcell.00360.2016 article EN AJP Cell Physiology 2017-01-12

Macrophages adopt different phenotypes in response to microenvironmental changes, which can be principally classified into inflammatory and anti-inflammatory states. Inflammatory activation of macrophages has been linked with metabolic reprogramming from oxidative phosphorylation aerobic glycolysis. In contrast mouse macrophages, little information is available on the link between metabolism inflammation human macrophages. current report it demonstrated that lipopolysaccharide...

10.1016/j.redox.2019.101147 article EN cc-by-nc-nd Redox Biology 2019-02-20

Bilirubin is a potent antioxidant generated intracellularly during the degradation of heme by enzyme oxygenase. The purpose this study was to determine role increased cardiac bilirubin in protection against postischemic myocardial dysfunction. Rat hearts were isolated and perfused according Langendorff technique evaluate recovery function after 30 min global ischemia 60 reperfusion. We found that upregulation inducible isoform oxygenase (HO-1) treatment animals with hemin 24 h before...

10.1152/ajpheart.2000.278.2.h643 article EN AJP Heart and Circulatory Physiology 2000-02-01

We investigated the effect of nitric oxide (NO) on induction stress protein heme oxygenase and its protective role in vascular endothelial cells exposed to hydrogen peroxide. Treatment porcine aortic for 6 h with NO-releasing compounds (0.1-1 mM) sodium nitroprusside (SNP), S-nitroso-N-acetylpenicillamine (SNAP), 3-morpholinosydnonimine (SIN-1) resulted a concentration-dependent increase activity. At 1 mM, activity was augmented 8.5-fold SNP, 5.8-fold SNAP, 5.7-fold SIN-1 over control value....

10.1152/ajpheart.1996.270.1.h107 article EN AJP Heart and Circulatory Physiology 1996-01-01

Heme oxygenase-1 (HO-1) is a redox-sensitive inducible protein that provides efficient cytoprotection against oxidative stress. Curcumin, polyphenolic natural compound possesses anti-tumor and anti-inflammatory properties, has been reported recently to induce potently HO-1 expression in vascular endothelial cells (<i>Free Rad Biol Med</i><b>28:</b>1303–1312, 2000). Here, we extend our previous findings by showing caffeic acid phenethyl ester (CAPE), another plant-derived phenolic agent,...

10.1124/mol.61.3.554 article EN Molecular Pharmacology 2002-03-01

The inducible isoform of haem oxygenase (HO-1) has been proposed as an effective system to counteract oxidant-induced cell injury. In several circumstances, this cytoprotective effect attributed increased generation the antioxidant bilirubin during degradation by HO-1. However, a direct implication for HO-1-derived in protection against oxidative stress remains be established. present study, we examined dynamics HO-1 expression and production after stimulation vascular smooth-muscle cells...

10.1042/bj3480615 article EN Biochemical Journal 2000-06-07

Thiols are very important antioxidants that protect cells against oxidative insults. Recently, a different and new physiological role has been defined for these compounds because of their involvement in nitric oxide (NO) binding transport biological systems. In view characteristics, we examined the effect thiols NO on expression inducible form heme oxygenase (HO-1), stress protein degrades to carbon monoxide biliverdin. Cultured bovine aortic endothelial exposed donors sodium nitroprusside...

10.1074/jbc.272.29.18411 article EN cc-by Journal of Biological Chemistry 1997-07-01

Carbon monoxide (CO), one of the end products heme catabolism by oxygenase, possesses antihypertensive and vasodilatory characteristics. We have recently discovered that certain transition metal carbonyls are capable releasing CO in biological fluids modulate physiological functions via delivery CO. Because initial compounds identified were not water soluble, we synthesized new CO‐releasing molecules chemically modified to allow solubility water. The aim this study was assess vasoactive...

10.1038/sj.bjp.0705825 article EN British Journal of Pharmacology 2004-06-01

Abstract —The enzyme heme oxygenase, which exists in inducible (HO-1) and constitutive (HO-2) isoforms, catalyzes the degradation of to biliverdin CO mammalian tissues. has been implicated control vascular tone a manner similar that for NO. In present study, we investigated contribution oxygenase/CO pathway modulation acute hypertensive responses vivo induced by (1) ααHb, chemically modified hemoglobin known scavenge NO, (2) N G -nitro- l -arginine methyl ester (L-NAME), competitive NOS...

10.1161/01.res.83.5.568 article EN Circulation Research 1998-09-07

The stress protein heme oxygenase-1 (HO-1) is induced in endothelial cells exposed to nitric oxide (NO)-releasing agents, and this process finely modulated by thiols (Foresti, R., Clark, J. E., Green, C. J., Motterlini R. (1997) <i>J. Biol. Chem.</i> 272, 18411–18417). Here, we report that up-regulation of HO-1 aortic severe hypoxic conditions (<i>p</i>O<sub>2</sub> ≤ 2 mm Hg) preceded increased inducible NO synthase activity. This effect accompanied oxidation intracellular glutathione...

10.1074/jbc.275.18.13613 article EN cc-by Journal of Biological Chemistry 2000-05-01

It is now established that NO a messenger molecule in mammals despite its high toxicity. As NO(+) and CO are isoelectronic, it should not be unexpected could also have role as messenger. produced naturally humans at rate of between 3 6 cm(3) per day, this increased markedly by certain inflammatory states pathological conditions associated with red blood cell hemolysis. Over the last 10 years, interest biological effects has greatly increased, medical literature does major signaling mammals....

10.1002/anie.200301634 article EN Angewandte Chemie International Edition 2003-08-13
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