Refine your search
Collections
Year
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z All
Choudhury, Shatabdi
- Protective role of Borreria hispida against Galactosamine Induced Diabetic Cataract
Abstract Views :146 |
PDF Views:0
Authors
M. Sumithra
1,
Shatabdi Choudhury
1,
L. S. Dhivya
1,
M. Nithiyanand
1,
Jimson Zachariah
1,
Sharmila
1
Affiliations
1 Dept of Pharmacology, SRM College of Pharmacy, Kasttankulathur, Kancheepuram District, Tamilnadu, IN
1 Dept of Pharmacology, SRM College of Pharmacy, Kasttankulathur, Kancheepuram District, Tamilnadu, IN
Source
Research Journal of Pharmacy and Technology, Vol 12, No 3 (2019), Pagination: 1235-1238Abstract
Cataract is the major cause of blindness all over the world, nearly 42% of visual impairment occurs due to diabetic associated complications in the eye. Borreria hispida, belonging to Rubiaceae family was used to treat eye infections by folklore system of medicine in India. This study was aimed to create scientific evidence for the anti-cataract activity of hydroalcoholic leaf extract of Borreria hispida (HAEBH) in diabetes induced cataract using goat lens. Cataract was induced using galactosamine in goat eyes lens. In this study, isolated goat lenses were suspended in bovine serum albumin. Totally sixteen lenses were selected, each group containing four lenses - normal control (distilled water treated lens), galactosamine treated lens, 1mg/ml of the hydroalcoholic extract of Borreria hispida leaves extract treated lens (HAEBH) and finally 1mg/ml of standard drug atropine treated lens. The opacification of lens were monitored in all the sixteen lenses. Among these, the anticataract activity of Borreria hispida was strengthened by the reduction in the deposition of proteins which is involved in the opacification of lens compared to galactosamine treated lens. The extract shown effective anticataract effect similar to that of standard group. The hydroalcoholic extract of Borreria hispida possess anticataract activity may be due to inhibition of Aldose Reductase enzyme involved in the polyol pathway which has a prime role in developing diabetes induced cataract. Further studies has to be carried out to isolate the prominent biomolecule responsible to control diabetes associated cataract.Keywords
Borreria hispida, Galactosamine, Aldose Reductase, Polyol Pathway.References
- D.K. Patel, S.K. Prasad, R Kumar, S Hemalatha . Asia Pac J Trop Disease, (2011); 323-9.
- Deepak G Langade, G Rao, RC Girme, PS Patki, PM Bulakh In vitro prevention by ACE inhibitors of cataract induced by glucose. Indian J of Pharmacol. 2006 :8(2): 107-110
- Eye Diseases Prevalence Research Group Prevalence of cataract and pseudophakia/aphakia among adults in the United States. Arch Ophthalmol. (2004;)122:487–494.
- GV Sampath Kumar, VVL Sri Vidya, Ch. Sandhya. Hepatoprotective Activity of Borreria hispida Roots Against Carbon Tetrachloride induced hepatotoxicity in Albino Wister Rats. Int J of Bio and Pharm Res (2013); 4(12) 1277-1282
- R Dhevi, V. Elango. Invitro Antioxidant activity and HPTLC Fringer printing of seeds of Spermacoce hispida linn. IJPPR (2015); 7-3-23a, 7-3-23b, 7-3-23c.
- K Chandrashekhar, Vinayak Meti., Shishir Mishra. Pharmacological Activities of Spermacoce hispidalinn: A review, IJRAP 4(1), Jan- Feb 2013.
- Farnsworth NR 1988. Screening plants for new medicines. In: Biodiversity, EO Wilson and FM Peter (eds), National Aca Press, Washington D.C., pp. 83—97.
- A G Chandorkar , M V Albal, PM Bulakh , MP Muley . Lens Organ Culture. Indian Journal of Ophthalmology,1981: 29(3): PP 151-152
- Lowry, A. Rosebrough, A. Farr , R. Randall J Biol Chem, 1951; 193:265 13. Srikanth Merugu , B Veeresh , Deepa Rekulapally . T Swetha. Study Of In Vitro Anticataract Activity Of Tamarindus indica Linn On Isolated Goat Lenses. Int Jl of Pharm (2012); 2(4) 758-763.
- Srikanth Merugu, B. Veeresh , Deepa Rekulapally . T Swetha. Study Of In Vitro Anticataract Activity of Tamarindus indica Linn On Isolated Goat Lenses. Int J of Phar 1951; 193:265 13.
- Lowry OH, Rosebrough NJ, Farr LA, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193: 265–275.
- P. Thenmozhi., T.V. Poonguzhali., B. Janarthanam. Phytochemical Screening And Antioxidant Activity Of Borreria hispida L.- An anticancer plant. Int J of Modern Trends in Eng and Res: 2016:3(2): PP
- Khan SS, Chaghtai SA, Oommachan M. Medicinal plants of Rubiaceae of Bhopal - An Ethnobotanical study. J Scient Res (Bhopal) 1984; 6:37–9.
- Purushothaman KK, Kalyani K. Isolation of isorhamnetin from Borreria hispida Linn. J Res Indian Med Yoga Homeop. 1979; 14:131–2.
- Kaviarasan K, Kalaiarasi P, Pugalendi V. Antioxidant efficacy of flavonoid-rich fraction from Spermacoce hispida in hyperlipidemic rats. J Appl Biomed. 2008;6: 165–76.
- J. H. Kinoshita. A thirty year journey in the polyol pathway, Exp. Eye Res. 50 (1990); 567–573.
- Alzheimer’s Disease Pathophysiology and its Implications
Abstract Views :173 |
PDF Views:0
Authors
Affiliations
1 Department of Pharmacology, SRM College of Pharmacy, SRMIST, Chennai-603203, IN
2 Department of Pharmacology, SRM College of Pharmacy, SRMIST Kattankulathur, Chennai 603203, IN
1 Department of Pharmacology, SRM College of Pharmacy, SRMIST, Chennai-603203, IN
2 Department of Pharmacology, SRM College of Pharmacy, SRMIST Kattankulathur, Chennai 603203, IN
Source
Research Journal of Pharmacy and Technology, Vol 12, No 4 (2019), Pagination: 2045-2048Abstract
Alzheimer’s disease (AD) is a destructive neurodegenerative disorder characterized by progressive memory defeat and impairment in behavior. Accordingly, although there is presently no “cure” for Alzheimer’s disease. A large number of potential therapeutic interventions have emerged that are designed to correct loss of presynaptic cholinergic function. A few of these compounds have confirmed in delaying the deterioration of symptoms of Alzheimer’s disease, a valuable treatment target considering the progressive nature of the disease. This review summarizes the main underlying neurobiological mechanisms in AD, including the theory with emphasis on amyloid peptide, cholinergic hypothesis, the role of tau protein, and the involvement of oxidative stress in Alzheimer. We also shed light on the inflammatory process involved in the progression of Alzheimer along with its recent advances in the treatment.Keywords
Alzheimer, Amyloid Peptide, Tau Protein, Inflammatory Process, Treatment.References
- Anand R, Gill KD, Malhdi AA. Therapeutics of Alzheimer’s disease: past, present and future. Neuropharmacology 2014; 76:27-50.
- Selkoe DJ. Normal and abnormal biology of the beta-Amyloid Precursor Protein. Annu Rev Neurosci 1994; 17:489–517.
- Anderson JP, Chen Y, Kim KS, Robakis NK. An alternative secretasecleavage produces soluble Alzheimer amyloid precursor protein containing a potentially amyloidogenic sequence. J Neurochem 1992; 59:2328–31.
- Blasko I, et al. Costimulatory Effects of Interferon-g and Interleukin-1b or Tumor Necrosis Factor a on the Synthesis of Ab1-40 and Ab1-42 by Human Astrocytes. Neurobiol Dis 2000; 7:682–9.
- Murphy MP, LeVine H. Alzheimer’s disease and the b-Amyloid peptide. J Alzheimer’s Dis 2010; 19:311.
- Alonso AC, Grundke-Iqbal I, Iqbal K. Alzheimer’s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med 1996; 2:7837.
- Alonso AC et al. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc Natl Acad Sci U S A 1994;91: 5562–6.
- Schmitt H, Gozes I, Littauer UZ. Decrease in levels and rates of synthesis of tubulin and actin in developing rat brain. Brain Res 1977; 121:327–42.
- Avila J, et al. Role of tau protein in both physiological and pathological conditions. Physiol Rev 2004; 84:361–84.
- Ebneth A, et al. Overexpression of Tau Protein Inhibits Kinesin-dependent Trafficking of Vesicles, Mitochondria, and Endoplasmic Reticulum: Implications for Alzheimer’s Disease. J Cell Biol 1998; 143:777–94.
- Gong C-X, Iqbal K. Hyperphosphorylation of microtubule-Associated protein Tau: A promising therapeutic target for Alzheimer disease. Curr Med Chem 2008; 15:2321–8.
- Simi_c G, et al. Tau Protein Hyperphosphorylation and aggregation in Alzheimer’s disease and other tauopathies, and possible neuroprotective strategies. Biomolecules 2016;6.
- Griffin WS et al. Brain interleukin 1 and S-100 immunoreactivity are elevated in Down syndrome and Alzheimer disease. Proc Natl Acad Sci U S A 1989; 86:7611–5.
- Rogers J, et al. Expression of immune system-associated antigens by cells of the human central nervous system: relationship to the pathology of Alzheimer’s disease. Neurobiol Aging 1988;9:339-49.
- Miguel-Alvarez M, et al. Non-steroidal anti-inflammatory drugs as a treatment for Alzheimer’s disease: a systematic review and meta-analysis of treatment effect. Drugs Aging 2015; 32:139–47.
- McGeer PL, Rogers J. Anti-inflammatory agents as a therapeutic approach to Alzheimer’s disease. Neurology 1992; 42:447–9.
- Plassman BL, et al. Documented head injury in early adulthood and risk of Alzheimer’s disease and other dementias. Neurology 2000; 55:1158–66.
- Quintanilla RA, et al. Interleukin-6 induces Alzheimer-type phosphorylation of tau protein by deregulating the cdk5/p35 pathway. Exp Cell Res 2004; 295:245–57.
- Terry AV Jr, Buccafusco JJ: The cholinergichypothesis of age and Alzheimer’s disease-related cognitive deficits: recent challenges and their implications for novel drug development. J Pharmacol Exp Ther 2003; 306: 821–827.
- Schaeffer EL, Gattaz WF: Cholinergic and glutamatergic alterations beginning at the early stages of Alzheimer disease: participation of the phospholipase A2 enzyme. Psychopharmacology (Berl) 2008; 198: 1–27.
- Fisher A: M1 muscarinic agonists target major hallmarks of Alzheimer’s disease – an update. Curr Alzheimer Res 2007; 4: 577–580.
- Shen J, Wu J: Nicotinic cholinergic mechanisms in Alzheimer’s disease. Int Rev Neurobiol 2015; 124: 275–292.
- Dong XX, Wang Y, Qin Z: Molecular mechanisms of excitotoxicity and their relevance to pathogenesis of neurodegenerative diseases. Acta Pharmacol Sin 2009; 30: 379–387.
- Navarro A, Boveris A: The mitochondrial energy transduction system and the aging process. Am J Physiol Cell Physiol 2007; 292:C670–C686.
- Cummings JL, Doody R, Clark C: Disease modifying therapies for Alzheimer disease: challenges to early intervention. Neurology 2007; 69: 1622–1634.
- Wu LG, Saggau P: Presynaptic inhibition of elicited neurotransmitter release. Trends Neurosci 1997; 20: 204–212.
- Roberson ED, et al: Reducing endogenoustau ameliorates amyloid beta-induced deficits in an Alzheimer’s disease mouse model. Science 2007; 316: 750–754.
- Lin MT, Beal MF: Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 2006; 443: 787–795.
- Rafii MS, Aisen PS: Recent developments in Alzheimer’s disease therapeutics. BMC Med 2009; 7: 7.]
- Zhao Y, Zhao B: Oxidative stress and the pathogenesis of Alzheimer’s disease. Oxid Med Cell Longev 2013; 2013: 316523.
- Salomone S, et al. New pharmacological strategies for treatment of Alzheimer’s disease: focus on disease modifying drugs. Br J Clin Pharmacol 2012; 73:504-17.
- Pei JJ, Ogren MS, Winblad B. Neurofibrillary degeneration in Alzheimer’s disease: from molecular mechanisms to identification of drug targets. Curr Opinion Psychiatry 2008; 21:555-61.
- Seren L, Coma M, Rodr M, Guez L. A novel GSK-3α inhibitor reduces Alzheimer’s pathology and rescues neuronal loss in vivo. Neurobiol Dis 2009; 35:359-67.
- Swerdlow RH, Khan SM. A mitochondrial cascade hypothesis for sporadic Alzheimer’s disease. Med Hypotheses 2004; 63:8–20.
- Nordberg A, Darreh-Shori T, Svenson A, Guan Z. AChE and BuChE activities in CSF of mild AD patients following 12 mo of rivastigmine treatment. J Neurol Sci 2001; 187: P0144.