Journal Home > Volume 5 , Issue 2

This study was designed to determine the neuroprotective potentials of aqueous and methanol extracts from Heinsia crinita leaves in vitro. The total phenol and flavonoid contents of the extracts were determined using colorimetric method while phenolic characterization of the leaf was analyzed via high performance liquid chromatography-diode array detector (HPLC-DAD). The effects of the extracts on Fe2+-induced lipid peroxidation in rats’ brain homogenate, monoamine oxidase (MAO), Na+/K+-ATPase, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) activities were also assessed. The aqueous extract had higher total phenol and flavonoid contents than the methanol extract. HPLC-DAD revealed that quercetin ellagic, chlorogenic and caffeic acids were the most abundant phenolic compounds in the leaves. The aqueous extract had higher inhibitory effects on MAO, AChE and BChE activities while there was no significant difference between their Fe2+-induced lipid peroxidation inhibitory effects. Furthermore, both extracts stimulated Na+/K+-ATPase activity; however, methanol extract had higher stimulatory effect. The neuroprotective properties of H. crinita leaves could be associated with its inhibitory effects on Fe2+-induced lipid peroxidation and modulation of MAO, Na+/K+-ATPase, AChE, and BChE activities. Therefore, H. crinita leaves could be used as a functional food and dietary intervention for the management of some neurodegenerative diseases. Nevertheless, the aqueous extracts exhibited better neuroprotective properties.


menu
Abstract
Full text
Outline
About this article

In vitro neuroprotective potentials of aqueous and methanol extracts from Heinsia crinita leaves

Show Author's information Ganiyu ObohaEsther E. NwannaaSunday I. OyeleyeaTosin A. OlasehindebOpeyemi B. OgunsuyiaAline A. Boligonc
Functional Foods and Nutraceuticals Unit, Department of Biochemistry, Federal University of Technology, Akure, Nigeria
Nutrition and Toxicology Division, Food Technology Department, Federal Institute of Industrial Research Oshodi, P.M.B. 21023 Lagos, Nigeria
Phytochemical Research Laboratory, Department of Industrial Pharmacy, Federal University of Santa Maria, Build 26, Room 1115, Santa Maria CEP 97105-900, Brazil

Peer review under responsibility of Beijing Academy of Food Sciences.

Abstract

This study was designed to determine the neuroprotective potentials of aqueous and methanol extracts from Heinsia crinita leaves in vitro. The total phenol and flavonoid contents of the extracts were determined using colorimetric method while phenolic characterization of the leaf was analyzed via high performance liquid chromatography-diode array detector (HPLC-DAD). The effects of the extracts on Fe2+-induced lipid peroxidation in rats’ brain homogenate, monoamine oxidase (MAO), Na+/K+-ATPase, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) activities were also assessed. The aqueous extract had higher total phenol and flavonoid contents than the methanol extract. HPLC-DAD revealed that quercetin ellagic, chlorogenic and caffeic acids were the most abundant phenolic compounds in the leaves. The aqueous extract had higher inhibitory effects on MAO, AChE and BChE activities while there was no significant difference between their Fe2+-induced lipid peroxidation inhibitory effects. Furthermore, both extracts stimulated Na+/K+-ATPase activity; however, methanol extract had higher stimulatory effect. The neuroprotective properties of H. crinita leaves could be associated with its inhibitory effects on Fe2+-induced lipid peroxidation and modulation of MAO, Na+/K+-ATPase, AChE, and BChE activities. Therefore, H. crinita leaves could be used as a functional food and dietary intervention for the management of some neurodegenerative diseases. Nevertheless, the aqueous extracts exhibited better neuroprotective properties.

Keywords: Neurodegeneration, Oxidative stress, Malondialdehyde, Polyphenols, Heinsia crinita

References(51)

[1]

W.R. Marksberry, M.A. Lovell, Damage to lipids, proteins, DNA and RNA in mild cognitive impairment, Arch. Neurol. 64 (2007) 954-956.

[2]

G. Oboh, J.B.T. Rocha, Distribution and antioxidant activity of polyphenols in ripe and unripe tree pepper (Capsicum pubescens), J. Food Biochem. 31 (2007) 456-473.

[3]

B. Uttara, A.V. Singh, P. Zamboni, R.T. Mahajan, Oxidative stress and neurodegenerative diseases: a review of upstream and downstream antioxidant therapeutic options, Clin. Neuropharmacol. 7 (2009) 65-74.

[4]

T. Thomas, Monoamine oxidase-B inhibitors in the treatment of Alzheimers disease, Neurobiol. Aging 21 (2000) 343-348.

[5]

G.B. Baker, D. Matveychuk, E.M. MacKenzie, S.M. Dursun, D.D. Mousseau, Monoamine oxidase inhibitors and neuroprotective mechanisms, Bull. Clin. Psychopharmacol. 22 (2012) 293-296.

[6]

G.R. de Lores Arnaiz, M.G.L. Ordieres, Brain Na+, K+-ATPase activity in aging and disease, Int. J. Biomed. Sci. 10 (2) (2014) 85.

[7]

F. Kreutz, E.B. Scherer, A.G. Ferreira, F.S. Petry, C.L. Pereira, F. Santana, A.T. Wyse, C.G. Salbego, V.M. Trindade, Alterations on Na+,K+-ATPase and acetylcholinesterase activities induced by amyloid-b peptide in rat brain and GML ganglioside neuroprotective action, Neurochem. Res. 38 (2013) 2342-2350.

[8]

L.G. Lees, Inhibition of sodium-potassium-ATPase: a potentially ubiquitous mechanism contributing to central nervous system neuropathology, Brain Res. Rev. 16 (1991) 283-300.

[9]

P.K. Mukherjee, V. Kumar, M. Mal, P.J. Houghton, Acetylcholinesterase inhibitors from plants, Phytomedicine 14 (2007) 289-300.

[10]

L.N. Zhang, Y.J. Sun, S. Pan, J.X. Li, Y.E. Qu, Y. Li, Y.L. Wang, Z.B. Gao, Na+/K+-ATPase, a potent neuroprotective modulator against Alzheimer disease, Fundam. Clin. Pharmacol. 27 (2013) 96-103.

[11]

S. Vladimir-Kneevic, B. Blaekovic, M. Kindl, J. Vladic, A.D. Lower-Nedza, A.H. Brantner, Acetylcholinesterase inhibitory, antioxidant and phytochemical properties of selected medicinal plants of the Lamiaceae family, Molecules 19 (2004) 767-782.

[12]

P.E. Ebong, G.O. Igile, B.I. Mgbeje, I.A. Iwara, A.E. Odongo, U.L. Onofiok, E.A. Oso, Hypoglycemic, hepatoprotective and nephroprotective effects of methanolic leaf extract of Heinsia crinita (Rubiaceae) in alloxan-induced diabetic albino wistar rats, IOSR J. Pharm. 4 (2014) 37-43.

[13]

K.H. Enyi-idoh, E.M. Ikpeme, G.C. Iwuh, Antibacterial activity of Gnetum africanum and Heinsia crinita on diarrhoeagenic bacteria stool isolates from children in Calabar south LGA, Cross river state, Nigeria, Transnatl. J. Sci. Technol. 3 (2012) 28-36.

[14]

V.L. Singleton, R. Orthofer, R.M. Lamuela-Raventos, Analysis of total phenols and other oxidation substrates and antioxidants by means of Folin–Ciocalteau's reagent, Methods Enzymol. 299 (1999) 152-178.

[15]

A. Meda, C. Lamien, M. Romito, J. Millogo, O.G. Nacoulma, Determination of the total phenolic, flavonoid and proline contents in Burkina Faso honey, as well as their radical scavenging activity, Food Chem. 91 (2005) 571-577.

[16]

B.C. Adedayo, G. Oboh, S.I. Oyeleye, I.I. Ejakpovi, A.A. Boligon, M.L. Athayde, Blanching alters the phenolic constituents and in vitro antioxidant and anticholinesterases properties of fireweed (Crassocephalum crepidioides), J. Taibah Univ. Med. Sci. 10 (2015) 419-426.

[17]

E.E. Nwanna, S.I. Oyeleye, O.B. Ogunsuyi, G. Oboh, A.A. Boligon, M.L. Athayde, In vitro neuroprotective properties of some commonly consumed green leafy vegetables in Southern Nigeria, NFS J. 2 (2016) 19-24.

[18]
Public Health Service (PHS), Public Health Service Policy on Humane Care and Use of Laboratory Animals (PL 99-158. Health Research Extension Act, 1985), US Department of Health and Human Services, Washington, DC, 1996.
[19]

N. Belle, G. Dalmolin, G. Fonini, Polyamines reduce lipid peroxidation induced by different pro-oxidant agents, Brain Res. 1008 (2004) 245-251.

[20]

H. Ohkawa, N. Ohishi, K. Yagi, Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction, Anal. Biochem. 95 (1979) 351-358.

[21]

A.L. Green, T.M. Haughton, A colorimetric method for the estimation of monoamine oxidase, Biochem. J. 78 (1961) (1961) 172-176.

[22]

W. Turski, E. Turska, G.M. Bellard, Modification of the spectrophotometric method of the determination of monoamine oxidase, Vopr. Med. Khim. 14 (1973) 211-220.

[23]

A.T. Wyse, E.L. Streck, P. Worm, A. Wajner, F. Ritter, C.A. Netto, Preconditioning prevents the inhibition of Na+/K+-ATPase activity after brain ischemia, Neurochem. Res. 25 (2000) 969-973.

[24]

C.H. Fiske, Y. Subbarow, The colorimetric determination of phosphorous, J. Biol. Chem. 66 (1925) 375-400.

[25]

N.S. Perry, P.J. Houghton, A. Theobald, P. Jenner, E.K. Perry, In-vitro inhibition of human erythrocyte acetylcholinesterase by Salvia lavandulaefolia essential oil and constituent terpenes, J. Pharm. Pharmacol. 52 (2000) 895-902.

[26]

G.L. Ellman, K.D. Courtney, V. Andres, R.M. Featherstone, A new and rapid colorimetric determination of acetylcholinesterase activity, Biochem. Pharmacol. 7 (1961) 88-95.

[27]

D.A. Butterfield, A. Castegna, C.B. Pocernich, J. Drake, G. Scapagnini, V. Calabrese, Nutritional approaches to combat oxidative stress in Alzheimer's disease, J. Nutr. Biochem. 13 (2002) 444-461.

[28]

G.R. Martinez, A.P. Loureiro, S.A. Marques, S. Miyamoto, L.F. Yamaguchi, J. Onuki, et al., Oxidative and alkylating damage in DNA, Mutat. Res. 544 (2003) 115-127.

[29]

Y. Zhao, J. Dou, T. Wu, H.A. Aisa, Investigating the antioxidant and acetylcholinesterase inhibition activities of Gossypium herbaceam, Molecules 18 (1) (2013) 951-962.

[30]

J. Olfsson, R. Adolfsson, C.G. Gottfries, B.E. Roos, Changes in the brain catecholamines in patients with dementia of Alzheimer type, Br. J. Psychiatry 135 (1979) 216-223.

[31]

H. Bayır, P.M. Kochanek, V.E. Kagan, Oxidative stress in immature brain after traumatic brain injury, Dev. Neurosci. 28 (2006) 420-431.

[32]

H. Benamar, W. Rached, A. Derdour, A. Marouf, Screening of Algerian medicinal plants for acetylcholinesterase inhibitory activity, J. Biol. Sci. 10 (2010) 1-9.

[33]

J. Kaur, D. Sharma, R. Singh, Acetyl-l-carnitine enhances Na+/K+-ATPase glutathione-S-transferase and multiple unit activity and reduces lipid peroxidation and lipofuscin concentration in aged rat brain regions, Neurosci. Lett. 301 (2001) 1-4.

[34]

P. Arivazhagan, C. Panneerselvam, Alpha-lipoic acid increases Na+ K+-ATPase activity and reduces lipofuscin accumulation in discrete brain regions of aged rats, Ann. N. Y. Acad. Sci. 1019 (2004) 350-354.

[35]

A.J. Lees, Dopamine agonists in Parkinson's disease: a look at apomorphine, Fundam. Clin. Pharmacol. 7 (1993) 121-128.

[36]

A.T. Wyse, C.S. Bavaresco, E.A. Reis, A.I. Zugno, B. Tagliari, T. Calcagnotto, et al., Training in inhibitory avoidance causes a reduction of Na+,K+-ATPase activity in rat hippocampus, Physiol. Behav. 80 (2004) 475-479.

[37]

S. Subash, M.M. Essa, A. Al-Asmi, S.A. Vaishnav, N. Braidy, T. Manivasagam, et al., Pomegranate from Oman alleviates the brain oxidative damage in transgenic mouse model of Alzheimer's disease, J. Tradit. Compl. Med. 4 (2014) 232-238.

[38]

V. Javorková, O. Pechánová, R. Andriantsitohaina, N. Vrbjar, Effect of polyphenolic compounds on the renal Na+,K+-ATPase during the restoration of normotension after experimentally induced hypertension in rats, Exp. Physiol. 88 (2003) 475-482.

[39]

G. Miao, H. Zhao, K. Guo, J. Cheng, X. Zhang, Z. Cai, et al., Mechanisms underlying attenuation of apoptosis of cortical neurons in the hypoxic brain by flavonoids from the stems and leaves of Scutellaria baicalensis Georgi, Neural Regen. Res. 9 (2014) 1592-1598.

[40]

R.P. Hebbel, O. Shalev, W. Foker, B.H. Rank, Inhibition of erythrocyte Ca2+-ATPase by activated oxygen through thiol- and lipid-dependent mechanisms, Biochim. Biophys. Acta 862 (1986) 8-16.

[41]

F. Cohadon, M. Rigoulet, B. Guerin, M. Vandendriessche, Vasogenic cerebral oedema. Changes in membrane ATPases. Correction by a phospholipid precursor, Nouv. Presse Med. 8 (1979) 1589-1591.

[42]

B.M. Čolović, D.Z. Krstić, T.D. Lazarević-Pašti, A.M. Bondžić, V.M. Vasić, Acetylcholinesterase inhibitors: pharmacology and toxicology, Curr. Neuropharmacol. 11 (2013) 315-335.

[43]

G. Oboh, O.O. Bakare, A.O. Ademosun, A.J. Akinyemi, T.A. Olasehinde, Inhibition of cholinesterases and some pro-oxidant induced oxidative stress in rats brain by two tomato (Lycopersicon esculentum) varieties, Int. J. Biomed. Sci. 11 (2015) 48.

[44]

L.M. Lane, S.G. Potkin, A. Enz, Targeting acetylcholinesterase and butyrylcholinesterase in dementia, Int. J. Neuropsychopharmacol. 9 (2006) 101-124.

[45]

M.I. Fernandez-Bachiller, C.P. Perez, L. Monjas, J. Rade-mann, M.I. Rodríguez-Franco, New tacrine-4-oxo-4H-chromene hybrids as multifunctional agents for the treatment of Alzheimer's disease, with cholinergic, antioxidant, and β-amyloid-reducing properties, J. Med. Chem. 55 (2012) 1303-1317.

[46]

A.O. Ademosun, G. Oboh, A.J. Olupona, S.I. Oyeleye, T.M. Adewuni, E.E. Nwanna, Comparative study of chemical composition, in vitro inhibition of cholinergic and monoaminergic enzymes, and antioxidant potentials of essential oil from peels and seeds of sweet orange (Citrus sinensis [L.] Osbeck) fruits, J. Food Biochem. (2015), http://dx.doi.org/10.1111/jfbc.12187.

[47]

J. Mankil, P. Moonsoo, Acetylcholinesterase inhibition by flavonoids from Agrimonia pilosa, Molecules 12 (2007) 2130-2139.

[48]

L.B. Roseiroa, A.P.B. Rauter, M.L.M. Serralheiro, Polyphenols as acetylcholinesterase inhibitors: structural specificity and impact on human disease, Nutr. Aging 1 (2012) 99-111.

[49]

Y. Xie, W. Yang, X. Chen, J. Xiao, Inhibition of flavonoids on acetylcholine esterase: binding and structure–activity relationship, Food Funct. 5 (2014) 2582-2589.

[50]

D. Vauzour, Dietary polyphenols as modulators of brain functions. Biological actions and molecular mechanisms underpinning their beneficial effects, Oxid. Med. Cell Longev. (2012), http://dx.doi.org/10.1155/2012/914273.

[51]

J.E. Slemmer, J.T. Weber, Assessing antioxidant capacity in brain tissue: methodologies and limitations in neuroprotective strategies, Antioxidants 3 (4) (2014) 636-648.

Publication history
Copyright
Rights and permissions

Publication history

Received: 27 October 2015
Revised: 09 March 2016
Accepted: 31 March 2016
Published: 06 April 2016
Issue date: June 2016

Copyright

© 2016 Beijing Academy of Food Sciences.

Rights and permissions

Return