The Insertion/Deletion Polymorphism of the Angiotensin Converting Enzyme (ACE) in Parkinson’s Disease

Parkinson’s disease (PDI is a neurodegenerative disorder of unknown etiology. Both genetic and environmental factors are thought to be implicated to some extent. The ACE gene insertion/deletion (I/D) polymorphism has been associated with common neurodegenerative disorders that share similar clinical and neuropathological features with PD (Alzheimer’s disease). In this study we set out to examine the role of the ACE gene insertion/deletion (I/D) polymorphism in Parkinson’s disease (PD)

The Insertion/Deletion Polymorphism of the Angiotensin Converting Enzyme (ACE) in Parkinson’s Disease

Parkinson’s disease (PDI is a neurodegenerative disorder of unknown etiology. Both genetic and environmental factors are thought to be implicated to some extent. The ACE gene insertion/deletion (I/D) polymorphism has been associated with common neurodegenerative disorders that share similar clinical and neuropathological features with PD (Alzheimer’s disease). In this study we set out to examine the role of the ACE gene insertion/deletion (I/D) polymorphism in Parkinson’s disease (PD)

The role of H2S bioavailability in endothelial dysfunction

This is the author accepted manuscript. The final version is available from the publisher via the DOI in this record.Endothelial dysfunction (EDF) reflects pathophysiological changes in the phenotype and functions of endothelial cells that result from and/or contribute to a plethora of cardiovascular diseases. We review the role of hydrogen sulfide (H2S) in the pathogenesis of EDF, one of the fastest advancing research topics. Conventionally treated as an environment pollutant, H2S is also produced in endothelial cells and participates in the fine regulation of endothelial integrity and functions. Disturbed H2S bioavailability has been suggested to be a novel indicator of EDF progress and prognosis. EDF manifests in different forms in multiple pathologies, but therapeutics aimed at remedying altered H2S bioavailability may benefit all.This work has been supported by a Discovery Grant from Natural Sciences and Engineering Research council of Canada to RW. CS has been supported by the American Diabetes Association, the National Institutes of Health of USA and the Shriners Hospitals for Children. FI has been supported by the National Institutes of Health of USA. MW has been supported by the Medical Research Council of UK. AA has been supported by programme grants from British Heart Foundation (RG/09/001/25940), Medical Research Council (G0700288), Royal Society and European Union. AP has been supported through an Aristeia grant (1436) that is co-financed by the European Union (ESF) and Greek national funds through the Operational Program “Education and Lifelong Learning”. MW and AP are supported by the COST Action BM1005 (ENOG: European network on gasotransmitters)

Haem oxygenase in GtoPdb v.2023.1

Haem oxygenase (heme,hydrogen-donor:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating)), E.C. 1.14.99.3, converts heme into biliverdin and carbon monoxide, utilizing NADPH as cofactor

Haem oxygenase (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

Haem oxygenase (heme,hydrogen-donor:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating)), E.C. 1.14.99.3, converts heme into biliverdin and carbon monoxide, utilizing NADPH as cofactor