Associate Professor, Oral Biology;
|
|
![]() |
CONTACT INFORMATION Richard B. Presland, Ph.D. |
EDUCATION AND TRAINING Ph.D., 1987, University of Adelaide, South Australia, in biochemistry and molecular biology B. Sc. (Hons.) in Biochemistry and M. Sc. (Hons.) in Biochemistry, University of Otago, Dunedin, New Zealand RESEARCH INTERESTS Epithelial tissues, such as those that line the oral cavity and skin, function to protect animals from physical, chemical, and microbial attack, and desiccation. They are essential for survival. During keratinocyte differentiation, living cells undergo desquamation to form the dead, cornified cells at the epithelial surface. These “squames” comprise a major part of the epithelial barrier and are continuously being renewed. Our research focuses in two areas important to this process: S100 calcium-binding proteins (including profilaggrin) that function in many calcium-dependent processes in cells; and caspase-14, an epithelial protease that is a member of the caspase family of cysteine endoproteases. We are currently using a variety of molecular and cellular methods to study the function of the profilaggrin N-terminus in keratinocyte differentiation. These include the yeast two-hybrid assay to examine protein-protein interactions in vivo, as well as gene expression in bacteria and cultured mammalian cells to study protein-protein interactions and protein function. Like profilaggrin, caspase-14 is also expressed in keratinizing epithelia late in keratinocyte differentiation. Recently, we determined the substrate specificity of recombinant caspase-14 expressed in E. coli. The precise function of caspase-14 in epidermis and other keratinizing epithelia is the subject of present investigation. REPRESENTATIVE PUBLICATIONS Presland RB, Fleckman P, Haydock PV, Nirunsuksiri W, Dale BA. Characterization of the human epidermal profilaggrin gene: Genomic organization and identification of an S-100-like calcium binding domain at the amino terminus. J. Biol. Chem. 267:23772-23781, 1992. Dale BA, Resing KA, Presland RB. Keratohyalin granule proteins. In: Keratinocyte Handbook, I Leigh, F Watt, B Lane (Eds.), pp. 323-350. Cambridge University Press, UK, 1994. Presland RB, Bassuk JA, Kimball JR, Dale BA. Characterization of two distinct calcium-binding sites in the amino-terminus of human profilaggrin. J. Invest. Dermatol. 104: 218-223, 1995. Nirunsuksiri W, Presland RB, Lewis P, Dale BA, Fleckman P. Decreased profilaggrin expression in ichthyosis vulgaris is a result of selectively impaired post-transcriptional control. J. Biol. Chem. 270: 871-876, 1995. Dale BA, Presland RB, Lewis SP, Underwood RA, Fleckman P. Transient expression of epidermal filaggrin in cultured cells causes collapse of intermediate filament networks with alteration of cell shape and nuclear integrity. J. Invest. Dermatol. 108: 179-187, 1997. Presland RB, Kimball JR, Kautsky MB, Lewis SP, Lo CY, Dale BA. Evidence for specific proteolytic cleavage of the N-terminal domain of human profilaggrin during epidermal differentiation. J. Invest. Dermatol. 108: 170-178, 1997. Ishida-Yamamoto A, Takahashi H, Presland RB, Dale BA, Iizuka H. Translocation of profilaggrin N-terminal domain into keratinocyte nuclei with fragmented DNA in normal human skin and loricrin keratoderma. Lab. Invest. 78: 1245-1253, 1998. Kuechle MK, Thulin CD, Presland RB, Dale BA. Profilaggrin requires both linker and filaggrin peptide sequences to form granules: implications for profilaggrin processing in vivo. J. Invest. Dermatol. 112: 843-852, 1999. Dale BA, Presland RB. Filaggrins. In: Guidebook to the Cytoskeletal and Motor Proteins. RD Vale and TE Kreis (Eds.), pp. 333-337. Oxford University Press, UK, 1999. Kuechle MK, Presland RB, Lewis SP, Fleckman P, Dale BA. Inducible expression of filaggrin increases keratinocyte suspectibility to apoptotic cell death. Cell Death Diff. 7: 566-573, 2000. Presland RB, Dale BA. Epithelial structural proteins of skin and oral cavity: function in health and disease. Crit. Rev. Oral Biol. Med. 11: 383-408, 2000. Presland RB, Boggess D, Lewis SP, Hull C, Fleckman P, Sundberg JP. Loss of normal profilaggrin and filaggrin in flaky tail (ft/ft) mice: an animal model for the filaggrin-deficient skin disease ichthyosis vulgaris. J. Invest. Dermatol. 115: 1072-1081, 2000. Pearton DJ, Nirunsuksiri W, Rehemtulla A, Lewis SP, Presland RB, Dale BA. Proprotein convertases expression and localization in epidermis: evidence for multiple roles and substrates. Exp. Dermatol. 10:193-203, 2001. Livingston RJ, Sybert VP, Smith LT, Dale BA, Presland RB, Stephens K. Expression of a truncated keratin 5 may contribute to severe palmar/plantar hyperkeratosis in epidermolysis bullosa simplex patients. J. Invest. Dermatol. 116:970-974, 2001. Kuechle MK, Predd HM, Fleckman P, Dale BA, Presland RB. Caspase 14, a
keratinocyte specific caspase: mRNA splice variants and expression pattern in
embryonic and adult mouse. Cell Death Diff. 8:868-870, 2001. Presland RB, Kuechle MK, Lewis SP, Fleckman P, Dale BA. Regulated expression of human filaggrin in keratinocytes results in cytoskeletal disruption, loss of cell-cell adhesion, and cell cycle arrest. Exp. Cell Res. 270:199-213, 2001. Presland RB, Jurevic RJ. Making sense of the epithelial barrier: what molecular biology and genetics tell us about the functions of oral mucosal and epidermal tissues. J. Dent. Educ. 66:564-574, 2002. Chien AJ, Presland RB, Kuechle MK. Processing of native caspase-14 occurs at an atypical cleavage site in normal epidermal differentiation. Biochem. Biophys. Res. Commun. 296:911-917, 2002. Pearton DJ, Dale BA, Presland RB. Functional analysis of the profilaggrin N-terminal peptide. Identification of peptide sequences that regulate cytoplasmic and nuclear distribution. J. Invest. Dermatol., in press. Pearton DJ, Dale BA, Presland RB. Functional analysis of the profilaggrin N-terminal peptide. Identification of peptide sequences that regulate cytoplasmic and nuclear distribution. J. Invest. Dermatol. 119:661-669, 2002. Hitomi K, Presland RB, Nakayama T, Fleckman P, Dale BA, Maki M. Analysis of epidermal-type transglutaminase (transglutaminase 3) in human stratified epithelia and cultured keratinocytes using monoclonal antibodies. J. Dermatol. Sci. 32:95-103, 2003. Presland RB, Coulombe PA, Eckert RL, Mao-Qiang M, Feingold KR, Elias PM. Barrier function in transgenic mice overexpressing K16, involucrin, and filaggrin in the suprabasal epidermis. J. Invest. Dermatol. 123:603-606, 2004. Presland RB, Fleckman P. Tetracycline-regulated gene expression in epidermal keratinocytes. Methods Mol. Biol. 289:273-286, 2005. Wang H, Presland RB, Piepkorn M. A search for CDKN2A/p16INK4a mutations in melanocytic nevi from patients with melanoma and spouse controls by use of laser-captured microdissection. Arch. Dermatol. 141:177-180, 2005. Reviews Presland RB, Dale BA. Epithelial structural proteins of skin and oral cavity: function in health and disease. Crit. Rev. Oral Biol. Med. 11: 383-408, 2000. Presland RB, Jurevic RJ. Making sense of the epithelial barrier: what molecular biology and genetics tell us about the functions of oral mucosal and epidermal tissues. J. Dent. Educ. 66:564-574, 2002. Dermatology Home | Dermatology Table of Contents | DOM Home | UW Home
Please honor our
copyrights and disclaimer. |
|