Hyperhomocysteinemia is strongly associated with cardiovascular diseases. Previous studies have shown that phytoestrogen α-zearalanol can protect cardiovascular system from hyperhomocysteinemia and ameliorate the level of plasma total homocysteine; however, the underlying mechanisms remain to be clarified. The aim of this research is to investigate the possible molecular mechanisms involved in ameliorating the level of plasma homocysteine by α-zearalanol. By the successfully established diet-induced hyperhomocysteinemia rat models, we found that, after α-zearalanol treatment, the activity of cystathionine β-synthase, the key enzyme in homocysteine metabolism, was significantly elevated and level of nitrative stress in liver was significantly reduced. In correlation with this, results also showed a decreased nitration level of cystathionine β-synthase in liver. Together data implied that alleviation of plasma homocysteine level by phytoestrogen α-zearalanol might be related to the reduction of cystathionine β-synthase nitration.
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http://dx.doi.org/10.1155/2014/143192 | DOI Listing |
J Nanobiotechnology
March 2025
Department of Basic Medicine, Wuxi School of Medicine, Jiangnan University, Wuxi, 214122, China.
Background: Aberrant proliferation and inflammation of fibroblast-like synoviocytes (FLSs) significantly contribute to the pathogenesis of rheumatoid arthritis (RA). Deficiency of hydrogen sulfide (HS) is a driving force for the development of RA, and the short half-life of the HS-releasing donor sodium hydrosulfide (NaHS) limits its clinical application in RA therapy. Designing a targeted delivery system with slow-release properties for FLSs could offer novel strategies for treating RA.
View Article and Find Full Text PDFBehav Brain Res
March 2025
Department of Biochemistry, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil; Post Graduation Program of Biochemistry, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil. Electronic address:
Introduction: Classical homocystinuria is a genetic disease caused by partial or total deficiency of cystathionine-β synthase (CβS) enzyme activity, ultimately leading to brain alterations and early atherosclerotic disease. Currently, there is no cure for the disease and the treatments consist in reducing homocysteine levels through diet, however not all patients respond to therapy. Due to its ability to increase neurotrophins production and decrease oxidative stress in the brain, environmental enrichment (EE) has been used with success as an adjuvant non-pharmacological therapy for CNS disorders.
View Article and Find Full Text PDFBr Poult Sci
March 2025
The Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh, Edinburgh, UK.
1. This review is a comprehensive exploration of the author's work in improving skeletal health in laying hens, focusing on the insights from genetics on nutritional, and environmental factors. It discusses the importance of the large number of disciplines that have contributed to the efforts to tackle bone quality in laying hens, particularly the keel bone.
View Article and Find Full Text PDFOrphanet J Rare Dis
March 2025
Travere Therapeutics, San Diego, CA, USA.
Background: Patients with classical homocystinuria (HCU) are unable to metabolize homocysteine and rely on dietary treatment to reduce their risk of complications (e.g., thromboembolism, cognitive impairment).
View Article and Find Full Text PDFJ Microbiol
February 2025
Research Institute of Agriculture and Life Sciences, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul 08826, Republic of Korea.
Pyridoxal 5'-phosphate (PLP)-dependent enzymes participate in various reactions involved in methionine and cysteine metabolism. The representative foodborne pathogen Staphylococcus aureus expresses the PLP-dependent enzyme MccB, which exhibits both cystathionine gamma-lyase (CGL) and cysteine desulfhydrase activities. In this study, we investigated the role of Ser323 in MccB, a conserved residue in many PLP-dependent enzymes in the transsulfuration pathway.
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