http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
A Review on Renal Toxicity Profile of Common Abusive Drugs
Singh, Varun Parkash,Singh, Nirmal,Jaggi, Amteshwar Singh The Korean Society of Pharmacology 2013 The Korean Journal of Physiology & Pharmacology Vol.17 No.4
Drug abuse has become a major social problem of the modern world and majority of these abusive drugs or their metabolites are excreted through the kidneys and, thus, the renal complications of these drugs are very common. Morphine, heroin, cocaine, nicotine and alcohol are the most commonly abused drugs, and their use is associated with various types of renal toxicity. The renal complications include a wide range of glomerular, interstitial and vascular diseases leading to acute or chronic renal failure. The present review discusses the renal toxicity profile and possible mechanisms of commonly abused drugs including morphine, heroin, cocaine, nicotine, caffeine and alcohol.
A Review on Renal Toxicity Profile of Common Abusive Drugs
Varun Parkash Singh,Nirmal Singh,Amteshwar Singh Jaggi 대한약리학회 2013 The Korean Journal of Physiology & Pharmacology Vol.17 No.4
Drug abuse has become a major social problem of the modern world and majority of these abusive drugs or their metabolites are excreted through the kidneys and, thus, the renal complications of these drugs are very common. Morphine, heroin, cocaine, nicotine and alcohol are the most commonly abused drugs, and their use is associated with various types of renal toxicity. The renal complications include a wide range of glomerular, interstitial and vascular diseases leading to acute or chronic renal failure. The present review discusses the renal toxicity profile and possible mechanisms of commonly abused drugs including morphine, heroin, cocaine, nicotine, caffeine and alcohol.
Advanced Glycation End Products and Diabetic Complications
Varun Parkash Singh,Anjana Bali,Nirmal Singh,Amteshwar Singh Jaggi 대한약리학회 2014 The Korean Journal of Physiology & Pharmacology Vol.18 No.1
During long standing hyperglycaemic state in diabetes mellitus, glucose forms covalent adducts withthe plasma proteins through a non-enzymatic process known as glycation. Protein glycation andformation of advanced glycation end products (AGEs) play an important role in the pathogenesis ofdiabetic complications like retinopathy, nephropathy, neuropathy, cardiomyopathy along with someother diseases such as rheumatoid arthritis, osteoporosis and aging. Glycation of proteins interfereswith their normal functions by disrupting molecular conformation, altering enzymatic activity, andinterfering with receptor functioning. AGEs form intra- and extracellular cross linking not only withproteins, but with some other endogenous key molecules including lipids and nucleic acids to contributein the development of diabetic complications. Recent studies suggest that AGEs interact with plasmamembrane localized receptors for AGEs (RAGE) to alter intracellular signaling, gene expression, releaseof pro-inflammatory molecules and free radicals. The present review discusses the glycation of plasmaproteins such as albumin, fibrinogen, globulins and collagen to form different types of AGEs. Furthermore,the role of AGEs in the pathogenesis of diabetic complications including retinopathy, cataract,neuropathy, nephropathy and cardiomyopathy is also discussed.
Advanced Glycation End Products and Diabetic Complications
Singh, Varun Parkash,Bali, Anjana,Singh, Nirmal,Jaggi, Amteshwar Singh The Korean Society of Pharmacology 2014 The Korean Journal of Physiology & Pharmacology Vol.18 No.1
During long standing hyperglycaemic state in diabetes mellitus, glucose forms covalent adducts with the plasma proteins through a non-enzymatic process known as glycation. Protein glycation and formation of advanced glycation end products (AGEs) play an important role in the pathogenesis of diabetic complications like retinopathy, nephropathy, neuropathy, cardiomyopathy along with some other diseases such as rheumatoid arthritis, osteoporosis and aging. Glycation of proteins interferes with their normal functions by disrupting molecular conformation, altering enzymatic activity, and interfering with receptor functioning. AGEs form intra- and extracellular cross linking not only with proteins, but with some other endogenous key molecules including lipids and nucleic acids to contribute in the development of diabetic complications. Recent studies suggest that AGEs interact with plasma membrane localized receptors for AGEs (RAGE) to alter intracellular signaling, gene expression, release of pro-inflammatory molecules and free radicals. The present review discusses the glycation of plasma proteins such as albumin, fibrinogen, globulins and collagen to form different types of AGEs. Furthermore, the role of AGEs in the pathogenesis of diabetic complications including retinopathy, cataract, neuropathy, nephropathy and cardiomyopathy is also discussed.