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Department of biochemistry and Molecular biology

Hiroko Hama, PhD

Associate Professor
Biochemistry and Molecular Biology

2001-2009     Assistant Professor, Dept of Biochemistry & Molecular Biology, MUSC
1998-2001     Research Assistant Professor, Utah State University
1995-1997     Assistant Instructor, University of Texas Southwestern Medical Center at Dallas
1993-1995     Postdoctoral Fellow, University of California San Diego
1991-1993     Postdoctoral Fellow, Harvard Medical School

1990              Ph.D., Okayama University, Okayama, Japan

Contact Info
Office: 843-792-6949
Lab: 843-792-8906
Fax: 843-792-8568

Research Interests

The research in our laboratory focuses on a class of sphingolipids containing 2-hydroxy fatty acids (hFA-sphingolipids). hFA-sphingolipids are uniquely abundant in myelin in the mammalian nervous system. The enzyme fatty acid 2-hydroxylase (FA2H) is responsible for the biosynthesis of myelin hFA-sphingolipids. Mutations in the FA2H gene cause leukodystrophy (progressive degeneration of the white matter of the brain) in children. We have developed Fa2h knockout mice as a model of the human FA2H deficiency. We are using this mouse model to develop therapeutics for the leukodystrophy. Additional projects are aimed at elucidating the mechanism of how FA2H and hFA-sphingolipids are involved in myelination, glial cell signaling, and cell differentiation.

Recent Publications

Kota, V., and Hama. H. (2014) 2′-Hydroxy ceramide in membrane homeostasis and cell signaling. Adv. Biol. Regul. 54, 223-230.

Scheid, I., Maruani, A., Huguet, G., Leblond, C.S., Nygren, G., Anckarsäter, H., Beggiato, A., Rastam, M., Amsellem, F., Gillberg, I.C., Elmaleh, M., Leboyer, M., Gillberg, C., Betancur, C., Coleman, M., Hama, H., Cook, E.H., Bourgeron, T., Delorme, R. (2013) Heterozygous FA2H mutations in autism spectrum disorders. BMC Med. Genet. 14, 124.

Kota, V., Dhople, V. M., Smythe, N. M., Fullbright, G., Szulc, Z.M., Bielawska, A., and Hama, H. (2013) 2'-Hydroxy C16-ceramide induces apoptosis-associated proteomic changes in C6 glioma cells. J. Proteome Res. 12, 4366-4375.

Willet, K.A., and Hama. H. (2013) Mouse model of FA2H deficiency. In Movement Disorders: Genetics and Models, Second Edition. LeDoux, M.S. (ed) Academic Press, in press.

Kota, V., Szulc, Z., and Hama, H. (2012) Identification of C6-ceramide-interacting proteins in D6P2T Schwannoma cells. Proteomics 12, 2179-84.

Dan, P., Edvardson, S., Bielawski, J., Hama, H., and Saada, A. (2011) 2-Hydroxylated sphingomyelin profiles in cells from patients with mutated fatty acid 2-hydroxylase. Lipids in Health and Disease, 10:84.

Potter, K.A., Kern, M.J., Fullbright, G., Bielawski, J., Scherer, S.S., Yum, S., Li, J., Cheng, H., Han, X., Kummetha-Venkata, J., Khan Pathan, A.A., Rohrer, B., Hama, H. (2011) Central nervous system dysfunction in a mouse model of FA2H deficiency. Glia, 59(7):1009-21.

Kruer, M.C., Paisán-Ruiz, C., Boddaert, N., Yoon, M.Y., Hama, H., Gregory, A., Malandrini, A., Woltjer, R.L., Munnich, A., Polster, B.J., Palmeri, A., Edvardson, S., Hardy, J., Houlden, H.H., and Hayflick, S.J. (2010) Defective FA2H leads to a novel form of neurodegeneration with brain iron accumulation (NBIA). Ann. Neurol. 68:611-8.

Hama, H. (2010) Fatty acid 2-hydroxylation in mammalian sphingolipid biology. Biochim. Biophys. Acta 1801, 405-414.

Alderson, N.L. and Hama, H. (2009) Fatty acid 2-hydroxylase regulates cAMP-induced cell cycle exit in D6P2T Schwannoma cells. J. Lipid Res. 50, 1203-1208.

Edvardson, S., Hama, H., Shaag, A., Gomori, J.M., Berger, I., Soffer, D., Korman, S.H., Taustein, I., Saada, A., and Elpeleg, O. (2008) Mutations in the fatty acid 2-hydroxylase gene are associated with leukodystrophy with spastic paraparesis and dystonia.  Am. J. Hum. Genet. 83, 643-648.

Ponnusamy, S., Alderson, N.L., Hama, H., Bielawski, J., Jiang, J.C., Bhandari, R., Snyder, S.H., Jazwinski, M., and Ogretmen, B. (2008) Regulation of telomere length by fatty acid elongase 3 in yeast: Involvement of inositol phosphate metabolism and ku70/80 function.  J. Biol. Chem. 283: 27514-24.

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