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Yoshihiko Yamada, Ph.D.

Yoshihiko Yamada, Ph.D.Senior Investigator
Chief, Molecular Biology Section

BETHESDA MD 20892-4370

Phone: (301) 496-2111
Fax: (301) 402-0897

Biographical Sketch

Dr. Yoshihiko Yamada received his Ph.D. from Osaka University Faculty of Science. After receiving his Ph.D., he began his postdoctoral training at the University of Pittsburgh, where he investigated gene regulation of bacteriophages and plasmids. In 1978, he moved to the National Cancer Institute at NIH to study gene evolution and regulation of collagen genes. In 1983, he joined the NIDCR, where he has been studying the functions of basement membrane components, cartilage matrices, and other extracellular matrices during development and diseases. He is a recipient of the Young Investigator Research Grant from the University of Pittsburgh as well as an NIH Director's Award, the CRADA, Eli Lilly and Company Award, a research grant from Seikagaku Corporation, the Debio Peptide Award, and the William J. Gies Award.

Research Interests/Scientific Focus

The overall goal of the Molecular Biology Section is to discover novel molecular mechanisms that underlie the development of hard tissues and ectodermal organs, by identifying novel functions of previously unstudied genes and defining the roles of the extracellular matrix (ECM). They have focused on the novel roles of protein factors and ECM components in proliferation, differentiation, and cell adhesion during development of teeth, cartilage, and other tissues. These studies are aimed at developing reagents useful for diagnostic and therapeutic applications. Most recently, we identified several novel proteins from a tooth germ cDNA library, including the transcription factor epiprofin, the adhesion protein fibulin7 (TM14), and the gap junction protein pannexin 3. These proteins are expressed in teeth as well as in tissues such as cartilage, bone, and skin. We expect that identification of common and distinct molecular mechanisms for the function of these proteins in specific tissue types will uncover key concepts that underlie both normal development and disease.

Selected Publications

  1. Arikawa-Hirasawa E, Watanabe H, Takami H, Hassell JR, Yamada Y. 1999. Perlecan is essential for cartilage and cephalic development. Nat Genet. 23(3): 354-358.
  2. Tsumaki N, Tanaka K, Arikawa-Hirasawa E, Nakase T, Kimura T, Thomas JT, Ochi T, Luyten FP, Yamada Y. 1999. Role of CDMP-1 in skeletal morphogenesis: Promotion of mesenchymal cell recruitment and chondrocyte differentiation. J Cell Biol. 144(1): 161- 173.
  3. Arikawa-Hirasawa E, Wilcox WR, Le AH, Silverman N, Govindraj P, Hassell JR, Yamada Y. 2001. Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional null mutations of the perlecan gene. Nat Genet. 27(4): 431-434.
  4. Arikawa-Hirasawa E, Wilcox WR, Yamada Y. 2001. Dyssegmental dysplasia, Silverman-Handmaker type: Unexpected role of perlecan in cartilage development. Amer J Med Genetics. 106: 254-257.
  5. Arikawa-Hirasawa E, Rossi SG, Rotundo RL, Yamada Y. 2002. Absence of acetylcholinesterase at the neuromuscular junctions of perlecan-null mice. Nat Neurosci. 5(2): 119-123.
  6. Arikawa-Hirasawa E, Le AH, Nishino I, Nonaka I, Ho NC, Francomano CA, Govindraj P, Hassell JR, Devaney JM, Spranger J, Stevenson RE, Iannaccone S, Dalakas MC, Yamada Y. 2002. Structural and functional mutations of the perlecan gene cause Schwartz-Jampel syndrome, with myotonic myopathy and chondrodysplasia. Am J Hum Genet. 70(5): 1368-1375.
  7. Fukumoto S, Kiba T, Hall B, Iehara N, Nakamura T, Longenecker G, Krebsbach PH, Nanci A, Kulkarni AB, Yamada Y. 2004. Ameloblastin is a cell adhesion molecule required for maintaining the differentiation state of ameloblasts. J Cell Biol. 167(5): 973-983.
  8. Matsunobu T, Torigoe1 K, Ishikawa1 M, de Vega S, Kulkarni AB, Iwamoto Y, and Yamada Y. 2009. Critical roles of the TGF-β type I receptor ALK5 in perichondrial formation and function, cartilage integrity, and osteoblast differentiation during growth plate development. Dev Biol. 332: 325-338. 
  9. Ishikawa M, Iwamoto T, Nakamura T, Doyle A, Fukumoto S, and Yamada Y, 2011, Pannexin 3 functions as an ER Ca2+ channel, hemichannel, and gap junction to promote osteoblast differentiation. J Cell Biol. 193: 1257-1274.
  10. Suzuki N, Fukushi M, Kosaki K, Doyle AD, de Vega S, Yoshizaki K, Akazawa C, Arikawa-Hirasawa E, and Yamada Y. 2012. Teneurin-4 is a novel regulator of oligodendrocyte differentiation and myelination of small-diameter axons in the CNS. J Neurosci. 32:11586-11599.
  11. Nakamura T, Yoshitomi Y, Sakai K, Patel V, Fukumoto S, and Yamada, Y. 2014. Epiprofin orchestrates epidermal keratinocyte proliferation and differentiation, J Cell Sci. 127: 5261-5272.
  12. Ishikawa M, Williams LG, Ikeuchi T, Sakai K, Fukumoto S, and Yamada Y. 2016. Pannexin 3 and connexin 43 modulate skeletal development via distinct functions and expression patterns. J Cell Sci, 129: 1018-30.
  13. Nakamura T, Jimenez-Rojo L, Koyama E, Pacifici M, de Vega S, Iwamoto M, Fukumoto S, Unda F, and Yamada Y. 2016. Epiprofin regulates enamel formation and tooth morphogenesis by controlling epithelial-mesenchymal interactions during tooth development. J Bone Miner Res, 32-3L 601-610.
  14. Ishikawa M, and Yamada, Y. 2017. The role of Pannexin 3 in Bone biology. J Dent Res, 96-4: 372-379.


  • "Peptides with laminin activity" by Y. Yamada, J. Graf, Y., Iwamoto, F. Robey, H.K. Kleinman, M. Sasaki, and G.R. Martin, U.S. Patent 5,092,885.
  • "Laminin A chain: deduced amino acid sequence, Expression vectors and active synthetic peptides" by Y. Yamada, H.K. Kleinman, M. Sasaki, and G.R. Martin, U.S. Patent 5,211,657.

Invention Report

  • Teneurin-4-deficient mice as a tremor model, E-209-2009​

Complete CV and Publications (PDF File, 139KB)

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This page last updated: September 08, 2017