Objectives: This work aimed to assess the matrix metalloproteinase inhibitory and related pharmacological actions of 20(R)-ginsenoside Rh2 (20(R)-Rh2) in cultured macrophages and keratinocytes.
Methods: In-vitro anti-inflammatory activity of 20(R)-Rh2 was evaluated by analysing nitric oxide (NO) and prostaglandin E2 (PGE2) contents in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophage cells. Its antioxidant activity was determined by measuring the level of reactive oxygen species (ROS) in the macrophage and keratinocyte cells. Matrix metalloproteinase-9 (MMP-9) and -2 (MMP-2) activity in the culture medium was detected using zymography.
Key Findings: 20(R)-Rh2 was able to suppress NO, PGE2, ROS and pro-matrix metalloproteinase-9 (pro-MMP-9) levels that were enhanced in the LPS-stimulated murine RAW264.7 macrophage cells. 20(R)-Rh2 also exhibited inhibitory effects on the level of ROS and the activity of MMP-9 and -2 in human HaCat keratinocyte cells without stimulant exposure. 20(R)-Rh2 could suppress the gelatinolytic activity of MMP-9 enhanced by tumour necrosis factor-α in the keratinocytes.
Conclusions: 20(R)-Rh2, a minor stereoisomer of ginsenoside Rh2, possesses matrix metalloproteinase inhibitory, anti-inflammatory and antioxidative activity.
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http://dx.doi.org/10.1111/j.2042-7158.2012.01598.x | DOI Listing |
Biogerontology
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Centre for Global Health Research, Saveetha Medical College, Saveetha Institute of Medical and Technical Sciences, Saveetha University, Chennai, India.
Aging is associated with a marked increase in cardiovascular diseases, such as myocardial infarction (MI). Cellular senescence is also a crucial factor in the development of age-related MI. Matrix metalloproteinases (MMPs) interaction with cellular senescence is a critical determinant of MI development and outcomes, most notably in the aged heart.
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January 2025
Department of Parasitology, Chung Shan Medical University, Taichung, 402, Taiwan.
Prostaglandin E2 (PGE-2) is synthesised by cyclooxygenase-2 (COX-2) and microsomal prostaglandin E synthase 1 (mPGES-1). PGE-2 exhibits pro-inflammatory properties in inflammatory conditions. However, there remains limited understanding of the COX-2/mPGES-1/PGE-2 pathway in Angiostrongylus cantonensis-induced meningoencephalitis.
View Article and Find Full Text PDFPhotochem Photobiol
January 2025
Department of Anatomy, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil.
Globally, 537 million people suffer from diabetes mellitus (DM), a condition often associated with sensory disturbances, wound development, and chronic pain, which significantly affects the quality of life and imposes a substantial economic burden. This study evaluated the effects of photobiomodulation (PBM) therapy on nociceptive and sensory changes in diabetic patients to understand pain manifestations and explore PBM's molecular mechanisms on wound healing. Twenty patients with type 2 DM underwent clinical assessments, completed pain and quality of life questionnaires, and had their pain sensitivity evaluated using the quantitative sensory test (QST).
View Article and Find Full Text PDFToxicol Pathol
January 2025
Premier Laboratory, LLC, Longmont, Colorado, USA.
Hematoxylin and eosin (H&E) staining is a suitable approach for detecting substantial structural changes in neural tissues but is less sensitive for identifying subtle alterations to subcellular structures and various chemical constituents, including myelin. Neurohistological methods to better evaluate myelin integrity by light microscopy include acidophilic dyes (eg, eriochrome cyanine R, toluidine blue [used with hard plastic sections]); lipoprotein-binding dyes (eg, Luxol fast blue [LFB], Weil's iron hematoxylin); lipid impregnation with metals (eg, Marchi's, which uses osmium tetroxide for en bloc staining before embedding); and immunohistochemical (IHC) methods to highlight various antigens (eg, myelin basic protein [MBP] and peripheral myelin protein 22 [PMP22]). Some IHC methods reveal enhanced marker expression in damaged myelin (eg, matrix metalloproteinase-9 [MMP9], S100).
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