Hiroaki Kaku, PhD
Research Assistant Professor, Department of Investigative Medicine
1000 Oakland Drive
Kalamazoo, MI 49008
Hiroaki Kaku, PhD, completed his undergraduate work at the University of Tokyo, Japan and also received a PhD in Immunology from the University of Tokyo in 2004. Dr. Kaku spent 1 year at the University of Tokyo as a postdoctoral fellow. He then continued his postdoctoral training in Dr. Rothsteins lab, first at Boston University then at the Feinstein Institute for Medical Research, studying the molecular mechanisms of B cell activation. In 2009, Dr. Kaku was promoted to an Institute Scientist at the Feinstein Institute for Medical Research. In 2014, Dr. Kaku turned its focus onto cellular stress. He is now interested in how our cells fight against various cellular stresses and why the failure of this protection causes various diseases such as cataracts, neurodegenerative diseases, and myopathies. The cells and tissues in our bodies are continuously exposed to various stresses including heat, cold, UV, oxidative and toxic stresses, and infection. Heat shock proteins (HSPs) play a crucial role in protecting cells from these stresses therefore maintaining cellular viability and tissue homeostasis. HSPs are found in all living organisms from bacteria and plants to humans. HSPs are divided into 6 major groups: small HSPs (sHSPs), HSP40, HSP60, HSP70, HSP90, and large HSPs. Dr. Kaku currently focuses on the functions of sHSPs since they are involved in the mechanism of aging-related diseases including cataracts, neurodegenerative diseases, and myopathies. Thus, he aims to elucidate how sHSPs render resistance to cellular stresses in Dr. Rothstein's lab.
Education and Training
- PhD 2004, Immunology, The University of Tokyo
- MS 1999, Developmental Medical Science, The University of Tokyo
- BS 1997, Health Sciences and Nursing, The University of Tokyo
- Immunity, Cellular
Kaku H., Ludlow A.V., Gutknecht M.F., Rothstein T.L. FAIM Opposes Aggregation of Mutant SOD1 That Typifies Some Forms of Familial Amyotrophic Lateral Sclerosis Frontiers in Neuroscience. 2020;14 doi: 10.3389/fnins.2020.00110.
Kaku H., Rothstein T.L. FAIM Is a Non-redundant Defender of Cellular Viability in the Face of Heat and Oxidative Stress and Interferes With Accumulation of Stress-Induced Protein Aggregates Frontiers in Molecular Biosciences. 2020;7 doi: 10.3389/fmolb.2020.00032.
Kaku H., Holodick N., Tumang J., Rothstein T. CD25<sup>+</sup> B-1a cells express Aicda Frontiers in Immunology. 2017;8 doi: 10.3389/fimmu.2017.00672.
Kaku H., Cheng K., Al-Abed Y., Rothstein T. A novel mechanism of B cell-mediated immune suppression through CD73 expression and adenosine production Journal of Immunology. 2014;193:5904-5913. doi: 10.4049/jimmunol.1400336.
Rothstein T., Griffin D., Holodick N., Quach T., Kaku H. Human B-1 cells take the stage Annals of the New York Academy of Sciences. 2013;1285:97-114. doi: 10.1111/nyas.12137.
Tumang J., Holodick N., Vizconde T., Kaku H., Francés R., Rothstein T. A CD25<sup>-</sup> positive population of activated B1 cells expresses LIFR and responds to LIF Frontiers in Immunology. 2011;2 doi: 10.3389/fimmu.2011.00006.
Kaku H., Rothstein T. Octamer binding protein 2 (Oct2) regulates PD-L2 gene expression in B-1 cells through lineage-specific activity of a unique, intronic promoter Genes and Immunity. 2010;11:55-66. doi: 10.1038/gene.2009.68.
Kaku H., Rothstein T.L. Fas apoptosis inhibitory molecule enhances CD40 signaling in B cells and augments the plasma cell compartment (Journal of Immunology (2009) 183, (1667-1674)) Journal of Immunology. 2010;185:771. doi: 10.4049/jimmunol.1090047.
Kaku H., Rothstein T. Fas apoptosis inhibitory molecule enhances CD40 signaling in B cells and augments the plasma cell compartment Journal of Immunology. 2009;183:1667-1674. doi: 10.4049/jimmunol.0900056.
Kaku H., Rothstein T. Fas apoptosis inhibitory molecule expression in B cells is regulated through IRF4 in a feed-forward mechanism Journal of Immunology. 2009;183:5575-5581. doi: 10.4049/jimmunol.0901988.
Hara-Yokoyama M., Kimura T., Kaku H., Wakiyama M., Kaitsu Y., Inoue M., Kusano S., Shirouzu M., Yokoyama S., Katada T., Hirabayashi Y., Takatsu K., Yanagishita M. Alteration of enzymatic properties of cell-surface antigen CD38 by agonistic anti-CD38 antibodies that prolong B cell survival and induce activation International Immunopharmacology. 2008;8:59-70. doi: 10.1016/j.intimp.2007.10.010.
Francés R., Tumang J., Kaku H., Gurdak S., Rothstein T. B-1 cells express transgelin 2: Unexpected lymphocyte expression of a smooth muscle protein identified by proteomic analysis of peritoneal B-1 cells Molecular Immunology. 2006;43:2124-2129. doi: 10.1016/j.molimm.2005.12.011.
Yokoyama M., Kimura T., Tsuchida S., Kaku H., Takatsu K., Hirabayashi Y., Yanagishita M. Roles of membrane domains in the signaling pathway for B cell survival Sphingolipid Biology. 2006:245-251. doi: 10.1007/4-431-34200-1_18.
Kaku H., Horikawa K., Obata Y., Kato I., Okamoto H., Sakaguchi N., Gerondakis S., Takatsu K. NF-κB is required for CD38-mediated induction of C<inf>γ</inf>1 germline transcripts in murine B lymphocytes International Immunology. 2002;14:1055-1064.
Horikawa K., Kaku H., Nakajima H., Davey H., Henninghausen L., Iwamoto I., Yasue T., Kariyone A., Takatsu K. Essential role of stat5 for IL-5-dependent IgH switch recombination in mouse B cells Journal of Immunology. 2001;167:5018-5026. doi: 10.4049/jimmunol.167.9.5018.