教員イメージ
ANDO Kanae
准教授

安藤 香奈絵 アンドウ カナエ あんどう かなえ

プロフィール

所属

東京都立大学理学部 生命科学科
理学研究科 生命科学専攻

最終学歴・学位

Ph.D., 2001, Pharmaceutical Sciences, University of Tokyo

専門・研究分野

Neuroscience, Cell Biology, Molecular Biology

研究

研究テーマ

Mechanisms underlying brain aging and neurodegenerative diseases

研究キーワード

Neurobiology, mitochondria, Alzheimer's disease, aging, neurodegeneration, drosophila model of disease

研究イメージ
研究紹介

詳細情報

Naoko Nozawa,Marie Noguchi,Kanako Shinno,Maki Tajima,Shingo Aizawa,Taro Saito,Akiko Asada,Takuya Ishii,Masahiro Ishizuka,Koichi M. Iijima,Kanae Ando. (2021) '5-Aminolevulinic acid and sodium ferrous citrate ameliorate muscle aging and extend healthspan in Drosophila' FEBS Open Bio. https://doi.org/10.1002/2211-5463.13338

Saito T, Chiku T, Oka M, Wada-Kakuda S, Nobuhara M, Oba T, Shinno K, Abe S, Asada A, Sumioka A, Takashima A, Miyasaka T, Ando K. Disulfide bond formation in microtubule-associated tau protein promotes tau accumulation and toxicity in vivo. Hum Mol Genet. 2021 Oct 13;30(21):1955-1967. doi: 10.1093/hmg/ddab162. PMID: 34137825; PMCID: PMC8522637.

Oka M, Suzuki E, Asada A, Saito T, Iijima KM and Ando, K. (2021) “Increasing neuronal glucose uptake attenuates brain aging and promotes lifespan under dietary restriction in Drosophila.” iScience, Volume 24, Issue 1, 22 January 2021, 101979. https://doi.org/10.1016/j.isci.2020.101979

Oba T, Saito T, Asada A, Shimizu S, Iijima KM, Ando K.* Microtubule Affinity Regulating Kinase 4 with an Alzheimer's disease-related mutation promotes tau accumulation and exacerbates neurodegeneration. J Biol Chem. 2020 Oct 5:jbc.RA120.014420. doi: 10.1074/jbc.RA120.014420.

Samimi N., Asada A. and Ando K. *Tau abnormalities and autophagic defects in neurodegenerative disorders; a feed-forward cycle (2019) Galen Medical Journal, GMJ.2020;9:e1681

Saito T, Oba T, Shimizu S, Asada A, Iijima KM, Ando K.
Cdk5 increases MARK4 activity and augments pathological tau accumulation and toxicity through tau phosphorylation at Ser262.
Hum Mol Genet. 2019 Jun 7. pii: ddz120. doi: 10.1093/hmg/ddz120.

Chiku T, Hayashishita M, Saito T, Oka M, Shinno K, Ohtake Y, Shimizu S, Asada A, Hisanaga SI, Iijima KM, Ando K.
S6K/p70S6K1 protects against tau-mediated neurodegeneration by decreasing the level of tau phosphorylated at Ser262 in a Drosophila model of tauopathy.
Neurobiol Aging. 2018 Nov;71:255-264. doi: 10.1016/j.neurobiolaging.2018.07.021. Epub 2018 Aug 3.


Sekiya, M., Maruko-Otake, A., Hearn, S., Sakakibara, Y., Fujisaki, N., Suzuki, E., Ando, K.*, Iijima, K. M.
EDEM Function in ERAD Protects against Chronic ER Proteinopathy and Age-Related Physiological Decline in Drosophila.
Dev Cell. 2017 Jun 19;41(6):652-664.e5. doi: 10.1016/j.devcel.2017.05.019.

Oka,M., Naoki Fujisaki, N., Maruko-Otake, A., Ohtake, Yl., Shimizu, S., Saito, T., Hisanaga,S., Iijima,KM., and Ando, K.* Ca2+/calmodulin-dependent protein kinase II promotes neurodegeneration caused by tau phosphorylated at Ser262/356 in a transgenic Drosophila model of tauopathy. Journal of Biochemistry, 2017 Nov 1;162(5):335-342

Oka, M., Iijima, K.M. and Ando, K.* (2017) Loss of synaptic mitochondria and dementia. Zikkennigaku, 2017, Yodosha (Japanese)

*Ando, K., Oka, M., Ohtake, Y., Hayashishita, M., Shimizu, S., Hisanaga, S., and Iijima, K.M.* Tau phosphorylation at Alzheimer's disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated. Biochemical and Biophysical Research Communications, Volume 478, Issue 2, Pages 929-934(2016)

*Ando, K., Maruko-Otake, A., Ohtake, Y., Hayashishita, M., Sekiya, M., and Iijima, K. M*. Stabilization of microtubule-unbound tau via tau phosphorylation at Ser262/356 by Par-1/MARK contributes to augmentation of AD-related phosphorylation and Aβ42-induced tau toxicity. PLoS Genetics 12(3): e1005917, 2016.

Electron microscopy of the brains of Drosophila Models of Alzheimer’s disease. Ando, K*., Hearn, A., Suzuki, E., Maruko-Otake, A., Sekiya, M., and Iijima, M.K*.  Neuromethods, Springer, Humana Press, in press (2015).

Global Analysis of Phosphorylation of Tau by the Checkpoint Kinases Chk1 and Chk2.
Mendoza, J., Sekiya, M., Taniguchi, T., Iijima, K. M., Wang, R*. and Ando, K*.
Journal of Proteome Research. 2013 Jun 7;12(6):2654-65. doi: 10.1021/pr400008f.

Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer’s disease-related tau phosphorylation via PAR-1
Iijima-Ando, K.*, Sekiya, M., Maruko-Otake, A., Ohtake, Y., Suzuki, E., Lu, B. & Iijima, K. M.* 
PLoS Genetics Aug;8(8):e1002918. Epub 2012 Aug 30.

Matsushima, T., Saito, Y., Elliott, J. I., Iijima-Ando, K., Nishimura, M., Kimura, N., Hata, S., Yamamoto, Y., Nakaya, T., and Suzuki, T
Membrane microdomain localization of APP C-terminal fragments regulated by the phosphorylation at cytoplasmic Thr668 residue. J Biol Chem, 287(23):19715-24. (2012)

Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer’s disease.
Iijima, K.*, Gatt, A., and Iijima-Ando, K.*
Hum Mol Genet. Aug 1;19(15):2947-57. (2010)

A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration. Iijima-Ando, K.*, Zhao, L., Gatt, A., Shenton, C., and Iijima, K.*  
Hum Mol Genet. May 15;19(10):1930-8. (2010)

Transgenic Drosophila models of Alzheimer’s disease and tauopathies. (Review).
Iijima-Ando*, K and Iijima*, K.
Brain Structure & Function, 214(2-3):245-62. (2009)

Regulation of energy stores and feeding by neuronal and peripheral CREB activity in Drosophila.
Iijima, K*, Zhao, L., Shenton, C., and Iijima-Ando, K.*
PLoS ONE 4(12): e8498.(2009)

Mitochondrial Mislocalization Underlies Aβ42-Induced Neuronal Dysfunction in a Drosophila Model of Alzheimer’s Disease. Iijima-Ando*, K., Hearn, S. A., Shenton, C., Gatt, A., Zhao, L., and Iijima, K*.
PLoS ONE 4(12): e8310 (2009)

JNK/FOXO-mediated neuronal expression of fly homologue of Peroxiredoxin II reduces oxidative stress and extends lifespan in Drosophila.
Lee, K-S., Iijima-Ando, K., Iijima, K., Lee, W-J., Lee, J.H., Yu, K., and Lee, D-S.
J Biol Chem, 284(43):29454-61 (2009)

Drosophila models of Alzheimer’s amyloidosis; the challenge of dissecting the complex mechanisms of toxicity of amyloid-β 42. (Review)
Iijima, K.* and Iijima-Ando, K.*
Journal of Alzheimer's Disease, 2008, Dec;15(4):523-40. (2008)

Overexpression of Neprilysin Reduces Alzheimer Amyloid β 42 (Aβ42)-induced Neuron Loss and Intraneuronal Aβ42 Deposits but Causes a Reduction in cAMP-responsive Element-binding Protein-mediated Transcription, Age-dependent Axon Pathology, and Premature Death in Drosophila. Iijima-Ando, K.*, Hearn, S.A., Granger, L., Shenton, C., Gatt, A., Chiang, H.C., Hakker, I., Zhong, Y., and Iijima, K.*
J Biol Chem 283, 19066-19076. (2008)

Abeta42 mutants with different aggregation profiles induce distinct pathologies in Drosophila. Iijima, K., Chiang, H. C., Hearn, S. A., Hakker, I., Gatt, A., Shenton, C., Granger, L., Leung, A., Iijima-Ando, K., and Zhong, Y.
PLoS ONE 3, e1703 (2008)

Physiological mouse brain amyloid-beta levels are not related to the phosphorylation state of threonine-668 of Alzheimer’s APP.
Sano, Y., Nakaya, T., Pedrini, S., Furukori, K., Iijima-Ando, K., Iijima, K., Mathews, P.M., Itohara, S., Gandy, S, and Suzuki, T.
PLoS ONE, 1, e51. (2006)

cAMP-response element-binding protein and heat-shock protein 70 additively suppress polyglutamine-mediated toxicity in Drosophila. Iijima-Ando, K.*, Wu, P., Drier, E. A., Iijima, K., and Yin, J. C.* (* Corresponding authors)
Proc Natl Acad Sci U S A 102, 10261-10266. (2005)

Asaumi, M., Iijima, K., Sumioka, A., Iijima-Ando, K., Kirino, Y., Nakaya, T., Suzuki, T. (2005)
Interaction of N-Terminal Acetyltransferase with the Cytoplasmic Domain of β-Amyloid Precursor Protein and Its Effect on Aβ Secretion. J. Biochem. 137(2):147-55.

Ando, K., Iijima, K., Elliott, J. I., Kirino, Y. and Suzuki, T. (2001) Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of β-amyloid. J Biol Chem, 276,40353-61

Iijima, K., Ando, K., Takeda, S., Satoh, Y., Seki, T., Itohara, S., Greengard, P., Narin, A. C., Kirino, Y., and Suzuki, T. (2000) Neuron-specific phosphorylation of Alzheimer's precursor protein by Cdk5. J Neurochem 75, 1085-91.

Ando, K., Oishi, M., Takeda, S., Iijima, K., Isohara, T., Nairn, A. C., Kirino, Y., Greengard, P., and Suzuki, T. (1999) Role of phosphorylation of Alzheimer's amyloid precursor protein during neuronal differentiation. J Neurosci 19, 4421-7.

Isohara, T., Horiuchi, A., Watanabe, T., Ando, K., Czernik, A. J., Uno, I., Greengard, P., Nairn, A. C., and Suzuki, T. (1999). Phosphorylation of the cytoplasmic domain of Alzheimer's beta-amyloid precursor protein at Ser655 by a novel protein kinase. Biochem Biophys Res Commun 258, 300-5.

Suzuki, T., Ando, K., Isohara, T., Oishi, M., Lim, G. S., Satoh, Y., Wasco, W., Tanzi, R. E., Nairn, A. C., Greengard, P., Gandy, S. E., and Kirino, Y. (1997). Phosphorylation of Alzheimer beta-amyloid precursor-like proteins. Biochemistry 36, 4643-9.
1996-1998 Scholarship from the Japan Scholarship Foundation
1998-2001 Japan Society for the Promotion of Science (JPSP) Research Fellowships for Young Scientists
2002-2005 Human Frontier Science Program Long Term Fellowships
2019 Best Teaching Award from TMU
2005-2006 Postdoctoral fellowship from Hereditary Disease Foundation
2010-2011 Jefferson Intramural Pilot Research Award
2010-2012 New Investigator Research Grant Award in Alzheimer’s Association
2019 Best Teaching Award, Tokyo Metropolitan University 2019年度東京都立大学ベスト・ティーチング・アワード特別賞「生命科学英語課程:卒業に必要な全ての単位が英語で取得できるプログラムの確立」
Society for Neuroscience
The Japanese Biochemical Society
The Japanese Society for Neurochemistry
Japan Society for Dementia Research
The Pharmaceutical Society of Japan
Organizer, Biology English program
  • 基礎ゼミナール
  • 細胞生物学実験(神経分子機能)
  • Special Lecture in Biology(生物学特別講義)
  • General Physiology(生理学概論)
  • Special Lecture in Molecular Biology 1(分子生物学特別講義)
  • Special Lecture in Biology(生物学特別講義)
  • Molecular Biology(分子生物学各論)
  • Special Lecture in Biology(生物学特別講義)
  • Special Lecture in Biology(生物学特別講義)
  • 生化学実験(神経分子機能)
  • Special Lecture in Biology(生物学特別講義)
  • General Physiology(生理学概論)
  • Special Lecture in Biology(生物学特別講義)
  • Special Lecture in Biology(生物学特別講義)
  • Molecular Biology(分子生物学各論)
  • Special Lecture in Biology(生物学特別講義)
  • Special Lecture in Biology(生物学特別講義)
  • 生命科学特別演習Ⅰ(研究発表)
  • 生命科学特別演習Ⅰ(研究発表)
  • 生命科学セミナー1(神経分子機能1)
  • 生命科学セミナー1(神経分子機能1)
  • 生命科学セミナー2(神経分子機能1)
  • 生命科学セミナー2(神経分子機能1)
  • 生命科学セミナー1(神経分子機能2)
  • 生命科学セミナー1(神経分子機能2)
  • 生命科学セミナー2(神経分子機能2)
  • 生命科学セミナー2(神経分子機能2)
  • 生命科学セミナー1(神経分子機能3)
  • 生命科学セミナー1(神経分子機能3)
  • 生命科学セミナー2(神経分子機能3)
  • 生命科学セミナー2(神経分子機能3)
  • 生命科学セミナー1(神経分子機能4)
  • 生命科学セミナー1(神経分子機能4)
  • 生命科学セミナー2(神経分子機能4)
  • 生命科学セミナー2(神経分子機能4)
  • 生命科学実験1(神経分子機能)
  • 生命科学実験1(神経分子機能)
  • 生命科学実験2(神経分子機能)
  • 生命科学実験2(神経分子機能)
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 細胞科学特別講義
  • 細胞科学特別講義
  • 生命科学特別演習Ⅰ(研究発表)
  • 生命科学セミナー1(神経分子機能1)
  • 生命科学セミナー2(神経分子機能1)
  • 生命科学セミナー1(神経分子機能2)
  • 生命科学セミナー2(神経分子機能2)
  • 生命科学セミナー1(神経分子機能3)
  • 生命科学セミナー2(神経分子機能3)
  • 生命科学セミナー1(神経分子機能4)
  • 生命科学セミナー2(神経分子機能4)
  • 生命科学実験1(神経分子機能)
  • 生命科学実験2(神経分子機能)
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 生命科学特別講義
  • 細胞科学特別講義
  • 研究室インターンシップ(生体理工学)
  • 研究室インターンシップ(生体理工学)
  • 人間生物学

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連絡先

研究室

Office: 9-478 Lab: 9-493

オフィスアワー

Wednesday 13:00-14:30

内線番号

内線4443

メールアドレス

k_ando●tmu.ac.jp
(メールを送信される場合は●を@に変換してください)