β-Lactolin improves mitochondrial function in Aβ-treated mouse hippocampal neuronal cell line and a human iPSC-derived neuronal cell model of Alzheimer's disease.


Journal

FASEB journal : official publication of the Federation of American Societies for Experimental Biology
ISSN: 1530-6860
Titre abrégé: FASEB J
Pays: United States
ID NLM: 8804484

Informations de publication

Date de publication:
04 2022
Historique:
revised: 06 03 2022
received: 27 08 2021
accepted: 14 03 2022
entrez: 23 3 2022
pubmed: 24 3 2022
medline: 23 4 2022
Statut: ppublish

Résumé

Mitochondrial dysfunctions are a key hallmark of Alzheimer's disease (AD). β-Lactolin, a whey-derived glycine-threonine-tryptophan-tyrosine tetrapeptide, has been previously reported to prevent AD-like pathologies in an AD mouse model via regulation of microglial functions. However, the direct effect of β-lactolin on neuronal cells and neuronal mitochondrial functions remains unknown. Here, we investigated the effects of β-lactolin on mitochondrial functions in amyloid β (Aβ)-treated mouse hippocampal neuronal HT22 cells and human induced-pluripotent cell (hiPSC)-derived AD model neurons. Adding β-lactolin to Aβ-treated HT22 cells increased both the oxygen consumption rate and cellular ATP concentrations, suggesting that β-lactolin improves mitochondrial respiration and energy production. Using high content image analysis, we found that β-lactolin improved mitochondrial fragmentation, membrane potential, and oxidative stress in Aβ-treated cells, eventually preventing neuronal cell death. From a mechanistic perspective, we found that β-lactolin increased gene expression of mitofusin-2, which contributes to mitochondrial fusion events. Finally, we showed that β-lactolin improves both mitochondrial morphologies and membrane potentials in hiPSC-derived AD model neurons. Taken together, β-lactolin improved mitochondrial functions AD-related neuronal cell models and prevented neuronal cell death. The dual function of β-lactolin on both neuron and microglia marks an advantage in maintaining neuronal health.

Identifiants

pubmed: 35319792
doi: 10.1096/fj.202101366RR
doi:

Substances chimiques

Amyloid beta-Peptides 0
Oligopeptides 0
Whey Proteins 0
beta-lactolin 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e22277

Informations de copyright

© 2022 The Authors. The FASEB Journal published by Wiley Periodicals LLC on behalf of Federation of American Societies for Experimental Biology.

Références

Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Comm. 1984;120:885-890.
Querfurth HW, LaFerla FM. Alzheimer's disease. N Engl J Med. 2010;362:329-344.
Amor S, Puentes F, Baker D, van der Valk P. Inflammation in neurodegenerative diseases. Immunology. 2010;129:154-169.
Fung A, Vizcaychipi M, Lloyd D, Wan Y, Ma D. Central nervous system inflammation in disease related conditions: mechanistic prospects. Brain Res. 2012;1446:144-155.
Cadonic C, Sabbir MG, Albensi BC. Mechanisms of mitochondrial dysfunction in Alzheimer's disease. Mol Neurobiol. 2016;53:6078-6090.
Cha M-Y, Han S-H, Son SM, et al. Mitochondria-specific accumulation of amyloid β induces mitochondrial dysfunction leading to apoptotic cell death. PLoS One. 2012;7:e34929.
Nunnari J, Suomalainen A. Mitochondria: in sickness and in health. Cell. 2012;148:1145-1159.
Hoppins S, Lackner L, Nunnari J. The machines that divide and fuse mitochondria. Annu Rev Biochem. 2007;76:751-780.
Archer SL. Mitochondrial dynamics-mitochondrial fission and fusion in human diseases. N Engl J Med. 2013;369:2236-2251.
Bertholet AM, Delerue T, Millet AM, et al. Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity. Neurobiol Dis. 2016;90:3-19.
Martinou J-C, Youle RJ. Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics. Dev Cell. 2011;21:92-101.
Fukuyama H, Ogawa M, Yamauchi H, et al. Altered cerebral energy metabolism in Alzheimer's disease: a PET study. J Nucl Med. 1994;35:1-6.
Chandrasekaran K, Hatanpää K, Brady DR, Rapoport SI. Evidence for physiological down-regulation of brain oxidative phosphorylation in Alzheimer's disease. Exp Neurol. 1996;142:80-88.
Caspersen C, Wang N, Yao J, et al. Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J. 2005;19:2040-2041.
Hauptmann S, Scherping I, Dröse S, et al. Mitochondrial dysfunction: an early event in Alzheimer pathology accumulates with age in AD transgenic mice. Neurobiol Aging. 2009;30:1574-1586.
Fu Y-J, Xiong S, Lovell MA, Lynn BC. Quantitative proteomic analysis of mitochondria in aging PS-1 transgenic mice. Cell Mol Neurobiol. 2009;29:649-664.
Wu Z, Zhu Y, Cao X, Sun S, Zhao B. Mitochondrial toxic effects of Aβ through mitofusins in the early pathogenesis of Alzheimer's disease. Mol Neurobiol. 2014;50:986-996.
Kang S, Byun J, Son SM, Mook-Jung I. Thrombospondin-1 protects against Aβ-induced mitochondrial fragmentation and dysfunction in hippocampal cells. Cell Death Discov. 2018;4:1-12.
Wang X, Su B, Lee H-G, et al. Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J Neurosci. 2009;29:9090-9103.
Reddy PH, Yin X, Manczak M, et al. Mutant APP and amyloid beta-induced defective autophagy, mitophagy, mitochondrial structural and functional changes and synaptic damage in hippocampal neurons from Alzheimer's disease. Hum Mol Genet. 2018;27:2502-2516.
Wang X, Su B, Zheng L, Perry G, Smith MA, Zhu X. The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease. J Neurochem. 2009;109:153-159.
Perez Ortiz JM, Swerdlow RH. Mitochondrial dysfunction in Alzheimer's disease: role in pathogenesis and novel therapeutic opportunities. Br J Pharmacol. 2019;176:3489-3507.
Camfield DA, Owen L, Scholey AB, Pipingas A, Stough C. Dairy constituents and neurocognitive health in ageing. Br J Nutr. 2011;106:159-174.
Ozawa M, Ninomiya T, Ohara T, et al. Dietary patterns and risk of dementia in an elderly Japanese population: the Hisayama Study. Am J Clin Nutr. 2013;97:1076-1082.
Ano Y, Ozawa M, Kutsukake T, et al. Preventive effects of a fermented dairy product against Alzheimer's disease and identification of a novel oleamide with enhanced microglial phagocytosis and anti-inflammatory activity. PLoS One. 2015;10:e0118512.
Ano Y, Ayabe T, Kutsukake T, et al. Novel lactopeptides in fermented dairy products improve memory function and cognitive decline. Neurobiol Aging. 2018;72:23-31.
Ano Y, Ohya R, Takaichi Y, et al. β-lactolin, a whey-derived lacto-tetrapeptide, prevents Alzheimer's disease pathologies and cognitive decline. J Alzheimers Dis. 2020;73:1331-1342.
Park YH, Shin SJ, Kim HS, et al. Omega-3 fatty acid-type docosahexaenoic acid protects against Aβ-mediated mitochondrial deficits and pathomechanisms in Alzheimer's disease-related animal model. Int J Mol Sci. 2020;21:3879.
Honda M, Minami I, Tooi N, et al. The modeling of Alzheimer's disease by the overexpression of mutant Presenilin 1 in human embryonic stem cells. Biochem Biophys Res Comm. 2016;469:587-592.
Connolly NM, Düssmann H, Anilkumar U, Huber HJ, Prehn JH. Single-cell imaging of bioenergetic responses to neuronal excitotoxicity and oxygen and glucose deprivation. J Neurosci. 2014;34:10192-10205.
Brand MD, Nicholls DG. Assessing mitochondrial dysfunction in cells. Biochem J. 2011;435:297-312.
Dranka BP, Benavides GA, Diers AR, et al. Assessing bioenergetic function in response to oxidative stress by metabolic profiling. Free Radic Biol Med. 2011;51:1621-1635.
Connolly NMC, Theurey P, Adam-Vizi V, et al. Guidelines on experimental methods to assess mitochondrial dysfunction in cellular models of neurodegenerative diseases. Cell Death Differ. 2018;25:542-572.
Chen H, Detmer SA, Ewald AJ, Griffin EE, Fraser SE, Chan DC. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J Cell Biol. 2003;160:189-200.
Park J, Choi H, Min JS, et al. Loss of mitofusin 2 links beta-amyloid-mediated mitochondrial fragmentation and Cdk5-induced oxidative stress in neuron cells. J Neurochem. 2015;132:687-702.
Reddy PH, Manczak M, Yin X, et al. Protective effects of a natural product, curcumin, against amyloid β induced mitochondrial and synaptic toxicities in Alzheimer's disease. J Investig Med. 2016;64:1220-1234.
Reddy PH, Manczak M, Yin X. Mitochondria-division inhibitor 1 protects against amyloid-β induced mitochondrial fragmentation and synaptic damage in Alzheimer's disease. J Alzheimers Dis. 2017;58:147-162.
Ayabe T, Ano Y, Ohya R, Kitaoka S, Furuyashiki T. The lacto-tetrapeptide Gly-Thr-Trp-Tyr, β-Lactolin, improves spatial memory functions via dopamine release and D1 receptor activation in the hippocampus. Nutrients. 2019;11:2469.
Ayabe T, Ohya R, Ano Y. β-lactolin, a whey-derived glycine-threonine-tryptophan-tyrosine lactotetrapeptide, improves prefrontal cortex-associated reversal learning in mice. Biosci Biotechnol Biochem. 2020;84:1039-1046.
Ramsay RR. Molecular aspects of monoamine oxidase B. Prog Neuropsychopharmacol Biol Psychiatry. 2016;69:81-89.
Mishra A, Singh S, Tiwari V, Chaturvedi S, Wahajuddin M, Shukla S. Dopamine receptor activation mitigates mitochondrial dysfunction and oxidative stress to enhance dopaminergic neurogenesis in 6-OHDA lesioned rats: a role of Wnt signalling. Neurochem Int. 2019;129:104463.
Mishra A, Singh S, Tiwari V, Bano S, Shukla S. Dopamine D1 receptor agonism induces dynamin related protein-1 inhibition to improve mitochondrial biogenesis and dopaminergic neurogenesis in rat model of Parkinson's disease. Behav Brain Res. 2020;378:112304.
Du H, Guo L, Yan S, Sosunov AA, McKhann GM, Yan SS. Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model. Proc Natl Acad Sci. 2010;107:18670-18675.
Calkins MJ, Manczak M, Mao P, Shirendeb U, Reddy PH. Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease. Hum Mol Genet. 2011;20:4515-4529.
Dixit S, Fessel JP, Harrison FE. Mitochondrial dysfunction in the APP/PSEN1 mouse model of Alzheimer's disease and a novel protective role for ascorbate. Free Radic Biol Med. 2017;112:515-523.
Shin SJ, Jeon SG, Kim J-I, et al. Red ginseng attenuates Aβ-induced mitochondrial dysfunction and Aβ-mediated pathology in an animal model of Alzheimer's disease. Int J Mol Sci. 2019;20:3030.
Ano Y, Ohya R, Kondo K. Antidepressant-like effect of β-lactolin, a glycine-threonine-tryptophan-tyrosine peptide. J Nutr Sci Vitaminol. 2019;65:430-434.
Cerejeira J, Lagarto L, Mukaetova-Ladinska E. Behavioral and psychological symptoms of dementia. Front Neurol. 2012;3:73.
Manji H, Kato T, Di Prospero NA, et al. Impaired mitochondrial function in psychiatric disorders. Nat Rev Neurosci. 2012;13:293-307.
Wisniewski T, Dowjat WK, Buxbaum JD, et al. A novel Polish presenilin-1 mutation (P117L) is associated with familial Alzheimer's disease and leads to death as early as the age of 28 years. NeuroReport. 1998;9:217-221.
Kuperstein I, Broersen K, Benilova I, et al. Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio. EMBO J. 2010;29:3408-3420.
Pauwels K, Williams TL, Morris KL, et al. Structural basis for increased toxicity of pathological aβ42: aβ40 ratios in Alzheimer disease. J Biol Chem. 2012;287:5650-5660.
Kita M, Obara K, Kondo S, Umeda S, Ano Y. Effect of supplementation of a whey peptide rich in tryptophan-tyrosine-related peptides on cognitive performance in healthy adults: a randomized, double-blind, placebo-controlled study. Nutrients. 2018;10:899.
Kita M, Kobayashi K, Obara K, Koikeda T, Umeda S, Ano Y. Supplementation with whey peptide rich in β-lactolin improves cognitive performance in healthy older adults: a randomized, double-blind, placebo-controlled study. Front Neurosci. 2019;13:399.
Terada T, Obi T, Bunai T, et al. In vivo mitochondrial and glycolytic impairments in patients with Alzheimer disease. Neurology. 2020;94:e1592-e1604.
Mansur A, Rabiner EA, Tsukada H, et al. Test-retest variability and reference region-based quantification of 18F-BCPP-EF for imaging mitochondrial complex I in the human brain. J Cereb Blood Flow Metab. 2021;41(4):771-779.
Ano Y, Kita M, Kobayashi K, Koikeda T, Kawashima R. Effects of β-lactolin on regional cerebral blood flow within the dorsolateral prefrontal cortex during working memory task in healthy adults: a randomized controlled trial. J Clin Med. 2021;10:480.
Ano Y, Kobayashi K, Hanyuda M, Kawashima R. β-lactolin increases cerebral blood flow in dorsolateral prefrontal cortex in healthy adults: a randomized controlled trial. Aging. 2020;12:18660.
Ano Y, Kobayashi K, Koikeda T, Kawashima R. β-lactolin, a whey-derived Gly-Thr-Trp-Tyr lactopeptide, promotes cerebral blood flow during cognitive tasks: a randomized controlled trial. Curr Dev Nutr. 2021;5:889.
Fabiani M, Gordon BA, Maclin EL, et al. Neurovascular coupling in normal aging: a combined optical, ERP and fMRI study. NeuroImage. 2014;85:592-607.
Tarantini S, Tran CHT, Gordon GR, Ungvari Z, Csiszar A. Impaired neurovascular coupling in aging and Alzheimer's disease: contribution of astrocyte dysfunction and endothelial impairment to cognitive decline. Exp Gerontol. 2017;94:52-58.
Jack C, Del Olmo A, Valles S. Can mild cognitive impairment be stabilized by showering brain mitochondria with laser photons? Neuropharmacology. 2020;171:107841.
Tarantini S, Valcarcel-Ares NM, Yabluchanskiy A, et al. Treatment with the mitochondrial-targeted antioxidant peptide SS-31 rescues neurovascular coupling responses and cerebrovascular endothelial function and improves cognition in aged mice. Aging Cell. 2018;17:e12731.

Auteurs

Tatsuhiro Ayabe (T)

Kirin Central Research Institute, Kirin Holdings Company Limited, Fujisawa, Japan.

Chika Takahashi (C)

Kirin Central Research Institute, Kirin Holdings Company Limited, Fujisawa, Japan.

Rena Ohya (R)

Kirin Central Research Institute, Kirin Holdings Company Limited, Fujisawa, Japan.

Yasuhisa Ano (Y)

Kirin Central Research Institute, Kirin Holdings Company Limited, Fujisawa, Japan.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH