Neuroprotective properties of latanoprost

Close metadata

Recommended articles:

Clinical outcomes of laser activation of hydraulic permeability of the sclera in the treatment of advanced glaucoma. Russian Annals of Ophthalmology. 2023;(6):19-25

Comparison of the effectiveness and safety of glaucoma drugs in the therapy of primary open-angle glaucoma. Russian Annals of Ophthalmology. 2023;(6):101-108

The association between myopia and glaucoma. Russian Annals of Ophthalmology. 2024;(1):93-98

Role of point-by-point light sensitivity in the assessment of glaucoma progression. Russian Annals of Ophthalmology. 2024;(2-2):34-42

Influence of corneal curvature and peripheral thickness on tonometry readings. Russian Annals of Ophthalmology. 2024;(2-2):43-50

Thresholds and variability of retinal light sensitivity in each point of the examined visual field. Russian Annals of Ophthalmology. 2024;(2-2):116-122

Factors affecting the hypotensive effect of selective laser trabeculoplasty in primary open-angle glaucoma. Russian Annals of Ophthalmology. 2024;(2):54-62

Structure of pediatric ophthalmic pathology in Uzbekistan. Russian Annals of Ophthalmology. 2024;(2):97-101

The impact of therapy with Mexidol on neurological deficit and functional outcome in patients with ischemic stroke: a systematic review and meta-analysis. S.S. Korsakov Journal of Neurology and Psychiatry. 2023;(12-2):49-60

Cognitive impairment in patients with arterial hypertension. S.S. Korsakov Journal of Neurology and Psychiatry. 2024;(4-2):41-48

Glaucoma is the main cause of irreversible blindness in the world. Latanoprost — an ester prodrug of prostaglandin F_2α (PGF_2α) — was the first prostaglandin analogue used to treat glaucoma. The review shows that latanoprost possesses direct neuroprotective properties such as blocking the entry of calcium ions into neurons and inhibiting the action of caspase-3, inhibiting the activity of cyclooxygenase and activation of polypeptide 2B1 (OATP2B1) and Klotho protein. It is emphasized that when the drug is instilled into the eye, the concentration of the drug inside the vitreous body is twice as high as what is required to ensure the survival of retinal ganglion cells.

Keywords:

glaucoma

prostaglandin analogues

latanoprost

neuroprotection

Xalatan

Xalacom

Authors:

Kurysheva N.I.

Medical Biological University of Innovations and Continuing Education of the State Research Center — Burnasyan Federal Medical Biophysical Center of Federal Medical Biological Agency;
Burnasyan Federal Medical Biophysical Center of the Federal Medical Biological Agency;
Academy of Postgraduate Education of the Federal Scientific and Clinical Center of the Federal Medical Biological Agency

SPIN RSCI: 3531-5880
Scopus AuthorID: 6603842519
ORCID: 0000-0002-2265-6671

Received:

11.06.2022

Accepted:

21.06.2022

List of references:

Kurysheva NI. Neuroprotection and neuroregeneration: prospects in the treatment of glaucoma: monograph. M. 2013:88. (In Russ.).
Sharif NA, Kelly CR, Crider JY, Williams GW, Xu SX. Ocular hypotensive FP prostaglandin (PG) analogs: PG receptor subtype binding affinities and selectivities, and agonist potencies at FP and other PG receptors in cultured cells. J Ocul Pharmacol Ther. 2003;19(6):501-515. https://doi.org/10.1089/108076803322660422
Ota T, Aihara M, Narumiya S, Araie M. The effects of prostaglandin analogues on IOP in prostanoid FP-receptor-deficient mice. Invest Ophthalmol Vis Sci. 2005;46(11):4159-4163. https://doi.org/10.1167/iovs.05-0494
Cazevieille C, Muller A, Meynier F, Dutrait N, Bonne C. Protection by prostaglandins from glutamate toxicity in cortical neurons. Neurochem Int. 1994; 24(4):395-398. https://doi.org/10.1016/0197-0186(94)90118-x
Yamagishi R, Aihara M, Araie M. Neuroprotective effects of prostaglandin analogues on retinal ganglion cell death independent of intraocular pressure reduction. Exp Eye Res. 2011;93(3):265-270. https://doi.org/10.1016/j.exer.2011.06.022
Cantor LB, Hoop J, Wudunn D, Yung CW, Catoira Y, Valluri S, Cortes A, Acheampong A, Woodward DF, Wheeler LA. Levels of bimatoprost acid in the aqueous humour after bimatoprost treatment of patients with cataract. Br J Ophthalmol. 2007;91(5):629-632. https://doi.org/10.1136/bjo.2006.110155
Jiang J, Ganesh T, Du Y, Thepchatri P, Rojas A, Lewis I, Kurtkaya S, Li L, Qui M, Serrano G, Shaw R, Sun A, Dingledine R. Neuroprotection by selective allosteric potentiators of the EP2 prostaglandin receptor. Proc Natl Acad Sci USA. 2010;107(5):2307-2312. https://doi.org/10.1073/pnas.0909310107
McCullough L, Wu L, Haughey N, Liang X, Hand T, Wang Q, Breyer RM, Andreasson K. Neuroprotective function of the PGE2 EP2 receptor in cerebral ischemia. J Neurosci. 2004;24(1):257-268. https://doi.org/10.1523/JNEUROSCI.4485-03.2004
Echeverria V, Clerman A, Doré S. Stimulation of PGE receptors EP2 and EP4 protects cultured neurons against oxidative stress and cell death following beta-amyloid exposure. Eur J Neurosci. 2005;22(9):2199-2206. https://doi.org/10.1111/j.1460-9568.2005.04427.x
Liu D, Wu L, Breyer R, Mattson MP, Andreasson K. Neuroprotection by the PGE2 EP2 receptor in permanent focal cerebral ischemia. Ann Neurol. 2005;57(5):758-761. https://doi.org/10.1002/ana.20461
Ahmad AS, Zhuang H, Echeverria V, Doré S. Stimulation of prostaglandin EP2 receptors prevents NMDA-induced excitotoxicity. J Neurotrauma. 2006; 23(12):1895-1903. https://doi.org/10.1089/neu.2006.23.1895
Hutchinson AJ, Chou CL, Israel DD, Xu W, Regan JW. Activation of EP2 prostanoid receptors in human glial cell lines stimulates the secretion of BDNF. Neurochem Int. 2009;54(7):439-446. https://doi.org/10.1016/j.neuint.2009.01.018
Zhou P, Qian L, Chou T, Iadecola C. Neuroprotection by PGE2 receptor EP1 inhibition involves the PTEN/AKT pathway. Neurobiol Dis. 2008;29(3): 543-551. https://doi.org/10.1016/j.nbd.2007.11.010
Abe T, Kunz A, Shimamura M, Zhou P, Anrather J, Iadecola C. The neuroprotective effect of prostaglandin E2 EP1 receptor inhibition has a wide therapeutic window, is sustained in time and is not sexually dimorphic. J Cereb Blood Flow Metab. 2009;29(1):66-72. https://doi.org/10.1038/jcbfm.2008.88
Carlson NG, Rojas MA, Black JD, Redd JW, Hille J, Hill KE, Rose JW. Microglial inhibition of neuroprotection by antagonists of the EP1 prostaglandin E2 receptor. J Neuroinflammation. 2009;6:5. https://doi.org/10.1186/1742-2094-6-5
Bilak M, Wu L, Wang Q, Haughey N, Conant K, St Hillaire C, Andreasson K. PGE2 receptors rescue motor neurons in a model of amyotrophic lateral sclerosis. Ann Neurol. 2004;56(2):240-248. https://doi.org/10.1002/ana.20179
Zeevalk GD, Nicklas WJ. Chemically induced hypoglycemia and anoxia: relationship to glutamate receptor-mediated toxicity in retina. J Pharmacol Exp Ther. 1990;253(3):1285-1292.
Roman R, Bartkowski H, Simon R. The specific NMDA receptor antagonist AP-7 attenuates focal ischemic brain injury. Neurosci Lett. 1989;104(1-2): 19-24. https://doi.org/10.1016/0304-3940(89)90322-4
Iversen LL. Pharmacological approaches to the treatment of ischaemic neuronal damage. Eye (Lond). 1991;5(Pt 2):193-197. https://doi.org/10.1038/eye.1991.34
Benzi G, Arrigoni E, Pastoris O, Villa RF, Dagani F, Marzatico F, Agnoli A. Effect of some drugs on cerebral energy state during and after hypoxia and complete or incomplete ischemia. Biochem Pharmacol. 1979;28(3): 435-439. https://doi.org/10.1016/0006-2952(79)90111-4
Drago F, Valzelli S, Emmi I, Marino A, Scalia CC, Marino V. Latanoprost exerts neuroprotective activity in vitro and in vivo. Exp Eye Res. 2001;72(4): 479-486. https://doi.org/10.1006/exer.2000.0975
Gill R, Foster AC, Woodruff GN. Systemic administration of MK-801 protects against ischemia-induced hippocampal neurodegeneration in the gerbil. J Neurosci. 1987;7(10):3343-3349. https://doi.org/10.1523/JNEUROSCI.07-10-03343.1987
Meldrum B, Garthwaite J. Excitatory amino acid neurotoxicity and neurodegenerative disease. Trends Pharmacol Sci. 1990;11(9):379-387. https://doi.org/10.1016/0165-6147(90)90184-a
Warner MA, Neill KH, Nadler JV, Crain BJ. Regionally selective effects of NMDA receptor antagonists against ischemic brain damage in the gerbil. J Cereb Blood Flow Metab. 1991;11(4):600-610. https://doi.org/10.1038/jcbfm.1991.110
Dykens JA, Stern A, Trenkner E. Mechanism of kainate toxicity to cerebellar neurons in vitro is analogous to reperfusion tissue injury. J Neurochem. 1987;49(4):1222-1228. https://doi.org/10.1111/j.1471-4159.1987.tb10014.x
Goldberg MP, Weiss JH, Pham PC, Choi DW. N-methyl-D-aspartate receptors mediate hypoxic neuronal injury in cortical culture. J Pharmacol Exp Ther. 1987;243(2):784-791.
Choi DW, Koh JY, Peters S. Pharmacology of glutamate neurotoxicity in cortical cell culture: attenuation by NMDA antagonists. J Neurosci. 1988; 8(1):185-196. https://doi.org/10.1523/JNEUROSCI.08-01-00185.1988
Murphy T, Parikh A, Schnaar R, Coyle J. Arachidonic acid metabolism in glutamate neurotoxicity. In Arachidonic Acid Metabolism in the Nervous System. (Barkai AI and Bazan NG, Eds.). Ann N Y Acad Sci. 1989;559: 474-477.
Dawson VL, Dawson TM, London ED, Bredt DS, Snyder SH. Nitric oxide mediates glutamate neurotoxicity in primary cortical cultures. Proc Natl Acad Sci USA. 1991;88(14):6368-6371. https://doi.org/10.1073/pnas.88.14.6368
Pang L, Hoult JR. Induction of cyclooxygenase and nitric oxide synthase in endotoxin-activated J774 macrophages is differentially regulated by indomethacin: Enhanced cyclooxygenase-2 protein expression but reduction of inducible nitric oxide synthase. Eur J Pharmacol. 1996 Dec 12;317(1): 151-155. https://doi.org/10.1016/S0014-2999(96)00703-0
Drago F, Marino A, Floriddia ML, Marino V. Latanoprost exerts neuroprotective activity in vitro and in vivo. Invest Ophthalm Vis Sci. 1999;40;265S.
Dahlmann-Noor AH, Vijay S, Limb GA, Khaw PT. Strategies for optic nerve rescue and regeneration in glaucoma and other optic neuropathies. Drug Discov Today. 2010;15(7-8):287-299. https://doi.org/10.1016/j.drudis.2010.02.007
Zheng J, Feng X, Hou L, Cui Y, Zhu L, Ma J, Xia Z, Zhou W, Chen H. Latanoprost promotes neurite outgrowth in differentiated RGC-5 cells via the PI3K-Akt-mTOR signaling pathway. Cell Mol Neurobiol. 2011;31(4): 597-604. https://doi.org/10.1007/s10571-011-9653-x
Narayanan SP, Flores AI, Wang F, Macklin WB. Akt signals through the mammalian target of rapamycin pathway to regulate CNS myelination. J Neurosci. 2009;29(21):6860-6870. https://doi.org/10.1523/JNEUROSCI.0232-09.2009
Park KK, Liu K, Hu Y, Kanter JL, He Z. PTEN/mTOR and axon regeneration. Exp Neurol. 2010;223(1):45-50. https://doi.org/10.1016/j.expneurol.2009.12.032
Lingor P, Tönges L, Pieper N, Bermel C, Barski E, Planchamp V, Bähr M. ROCK inhibition and CNTF interact on intrinsic signalling pathways and differentially regulate survival and regeneration in retinal ganglion cells. Brain. 2008;131(Pt 1):250-263. https://doi.org/10.1093/brain/awm284
Vidal L, Díaz F, Villena A, Moreno M, Campos JG, Pérez de Vargas I. Reaction of Müller cells in an experimental rat model of increased intraocular pressure following timolol, latanoprost and brimonidine. Brain Res Bull. 2010;82(1-2):18-24. https://doi.org/10.1016/j.brainresbull.2010.02.011
Kudo H, Nakazawa T, Shimura M, Takahashi H, Fuse N, Kashiwagi K, Tamai M. Neuroprotective effect of latanoprost on rat retinal ganglion cells. Graefes Arch Clin Exp Ophthalmol. 2006;244(8):1003-1009. Published: 13 January 2006. https://doi.org/10.1007/s00417-005-0215-0
Kanamori A, Naka M, Fukuda M, Nakamura M, Negi A. Latanoprost protects rat retinal ganglion cells from apoptosis in vitro and in vivo. Exp Eye Res. 2009;88(3):535-541. https://doi.org/10.1016/j.exer.2008.11.012
Nakanishi Y, Nakamura M, Mukuno H, Kanamori A, Seigel GM, Negi A. Latanoprost rescues retinal neuro-glial cells from apoptosis by inhibiting caspase-3, which is mediated by p44/p42 mitogen-activated protein kinase. Exp Eye Res. 2006;83(5):1108-1117. https://doi.org/10.1016/j.exer.2006.05.018
Chen W, Jump DB, Grant MB, Esselman WJ, Busik JV. Dyslipidemia, but not hyperglycemia, induces inflammatory adhesion molecules in human retinal vascular endothelial cells. Invest Ophthalmol Vis Sci. 2003;44(11): 5016-5022. https://doi.org/10.1167/iovs.03-0418
Joussen AM, Poulaki V, Le ML, Koizumi K, Esser C, Janicki H, Schraermeyer U, Kociok N, Fauser S, Kirchhof B, Kern TS, Adamis AP. A central role for inflammation in the pathogenesis of diabetic retinopathy. FASEB J. 2004;18(12):1450-1452. https://doi.org/10.1096/fj.03-1476fje
Joussen AM, Poulaki V, Mitsiades N, Kirchhof B, Koizumi K, Döhmen S, Adamis AP. Nonsteroidal anti-inflammatory drugs prevent early diabetic retinopathy via TNF-alpha suppression. FASEB J. 2002;16(3):438-440. Published online January 30, 2002. https://doi.org/10.1096/fj.01-0707fje
Du Y, Sarthy VP, Kern TS. Interaction between NO and COX pathways in retinal cells exposed to elevated glucose and retina of diabetic rats. Am J Physiol Regul Integr Comp Physiol. 2004;287(4):R735-R741. https://doi.org/10.1152/ajpregu.00080.2003
Kuro-o M, Matsumura Y, Aizawa H, Kawaguchi H, Suga T, Utsugi T, Ohyama Y, Kurabayashi M, Kaname T, Kume E, Iwasaki H, Iida A, Shiraki-Iida T, Nishikawa S, Nagai R, Nabeshima YI. Mutation of the mouse klotho gene leads to a syndrome resembling ageing. Nature. 1997;390(6655): 45-51. https://doi.org/10.1038/36285
Imura A, Iwano A, Tohyama O, Tsuji Y, Nozaki K, Hashimoto N, Fujimori T, Nabeshima Y. Secreted Klotho protein in sera and CSF: implication for post-translational cleavage in release of Klotho protein from cell membrane. FEBS Lett. 2004;565(1-3):143-147. https://doi.org/10.1016/j.febslet.2004.03.090
Chang Q, Hoefs S, van der Kemp AW, Topala CN, Bindels RJ, Hoenderop JG. The beta-glucuronidase Klotho hydrolyzes and activates the TRPV5 channel. Science. 2005;310(5747):490-493. https://doi.org/10.1126/science.1114245
Manya H, Inomata M, Fujimori T, Dohmae N, Sato Y, Takio K, Nabeshima Y, Endo T. Klotho protein deficiency leads to overactivation of mu-calpain. J Biol Chem. 2002;277(38):35503-35508. https://doi.org/10.1074/jbc.M206033200
Ryu M, Yasuda M, Shi D, Shanab AY, Watanabe R, Himori N, Omodaka K, Yokoyama Y, Takano J, Saido T, Nakazawa T. Critical role of calpain in axonal damage-induced retinal ganglion cell death. J Neurosci Res. 2012; 90(4):802-815. https://doi.org/10.1002/jnr.22800
Liu S, Yin F, Zhang J, Qian Y. The role of calpains in traumatic brain injury. Brain Inj. 2014;28(2):133-137. https://doi.org/10.3109/02699052.2013.860479
Farinelli P, Arango-Gonzalez B, Völkl J, Alesutan I, Lang F, Zrenner E, Paquet-Durand F, Ekström PA. Retinitis Pigmentosa: over-expression of anti-ageing protein Klotho in degenerating photoreceptors. J Neurochem. 2013; 127(6):868-879. https://doi.org/10.1111/jnc.12353
Kokkinaki M, Abu-Asab M, Gunawardena N, Ahern G, Javidnia M, Young J, Golestaneh N. Klotho regulates retinal pigment epithelial functions and protects against oxidative stress. J Neurosci. 2013;33(41):16346-16359. https://doi.org/10.1523/JNEUROSCI.0402-13.2013
Zeldich E, Chen C-D, Colvin TA, Bove-Fenderson EA, Liang J, Tucker Zhou TB, Harris DA, Abraham CR. The neuroprotective effect of Klotho is mediated via regulation of members of the redox system. J Biol Chem. 2014; 289(35):24700-24715. https://doi.org/10.1074/jbc.M114.567321
Yamamoto K, Sato K, Yukita M, Yasuda M, Omodaka K, Ryu M, et al. The neuroprotective effect of latanoprost acts via klotho-mediated suppression of calpain activation after optic nerve transection. J Neurochem. 2016; 140(3): 495-508. https://doi.org/10.1111/jnc.13902
Stalmans I, Oddone F, Cordeiro MF, Hommer A, Montesano G, Ribeiro L, et al. Comparison of preservative-free latanoprost and preservative-free bimatoprost in a multicenter, randomized, investigator-masked cross-over clinical trial, the SPORT trial. Graefe’s Arch Clin Exp Ophthalmol. 2016; 254(6):1151-1158. https://doi.org/10.1007/s00417-016-3299-9
Kurysheva NI, Azizova OA, Piryazev AP. A Comparative Study into Antioxidant Activity of Fixed Combinations in Topical Glaucoma Treatment. Rossiiskij oftal’mologicheskij zhurnal. 2013;2(6):41-44. (In Russ.).
Fuma S, Shimazawa M, Imamura T, Kanno Y, Takano N, Tsuruma K, et al. Neuroprotective Effect of Ocular Hypotensive Drugs: Latanoprost/Timolol in Combination Are More Effective than Each as Monotherapy in RGC5. Biol Pharm Bull. 2016;39(2):192-198. https://doi.org/10.1248/bpb.b15-00584

Close metadata