This is a picture of Ken Nishimoto.ASSOCIATE PROFESSOR
This is a picture of Ken Nishimoto.
EDUCATION:
B.A. 1973 University of California, Los Angeles, Los Angeles CA Ph.D. 1980 University of California, San Diego, San Diego, CA Postdoctoral 1980-1982 University of Connecticut, Farmington, CT
PROFESSIONAL EXPERIENCE:
1982-1988 Research Assistant Professor of Orthopaedics, University of Southern California, Los Angeles, CA
1988-1994 Assistant Professor of Biochemistry, University of Tennessee, Memphis, Memphis, TN
1994-Present Associate Professor of Biochemistry, University of Tennessee, Memphis, Memphis, TN
RESEARCH INTERESTS:
We are interested in extracellular matrix protein biochemistry, biosynthesis, and function. Our main focus is on proteins which undergo a vitamin K-dependent post-translational modification of peptide bound glutamic acid residues to g-carboxyglutamic acid (Gla). In bone, the Gla-containing proteins are the most abundant non collagenous protein. We are studying Gla- containing proteins to understand their biological function.
To accomplish this goal, we have developed tools to specifically measure two Gla- containing proteins, the messenger RNAs encoding these proteins, and the unique post-translationally modified amino acid, Gla. The proteins are measureable by radioimmunoassays developed in the laboratory against bone Gla protein, and Matrix Gla protein. We have cloned the cDNA corresponding to mRNA encoding these proteins. mRNA levels are quantified by reverse transcription and polymerase chain reaction. In situ hybridization methods show cells expressing the genes. A colorimetric assay for Gla-containing proteins has been developed in the lab to detect the amino acid Gla. These methods are used in cell culture, tissue/organ culture, on intact tissues, and in whole animal studies.
These proteins exist in all vertebrates. Comparison of amino acid sequences from species which diverged over 200 million years ago show a high degree of sequence homology implying these proteins serve needed roles for survival, yet the biological function remains unknown. We hope to understand the biological role(s) of these extracellular matrix proteins.
HONORS AND PROFESSIONAL ASSOCIATIONS:
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1. Nishimoto, S.K. and Price, P.A. (1979) Proof That the g-Carboxyglutamic Acid Containing Protein is Synthesized in Calf Bone. J. Biol. Chem. 254, 437-441.
2. Nishimoto, S.K. and Price, P.A. (1980) Secretion of the Vitamin K-Dependent Protein of Bone by Rat Osteosarcoma Cells. J. Biol. Chem. 255, 6579-6583.
5. Price, P.A. and Nishimoto, S.K. (1980) Radioimmunoassay for the Vitamin K- Dependent Protein of Bone and its Discovery in Plasma. Proc. Natl. Acad. Sci. USA 77, 2234-2238.
6. Nishimoto, S.K., Kajiwara, T., Ledger, P.W., and Tanzer, M.L. (1982) Effects of the Ionophore Monensin on Type II Collagen and P proteoglycan Synthesis and Secretion by Cultured Chondrocytes. J. Biol. Chem. 257, 11712-11716.
9. Nishimoto, S.K., Chang, C., Gendler, E., Stryker, W.F. and Nimni, M.E. (1985) The Effect of Aging on Bone Formation in Rats: Biochemical and Histological Evidence for Decreased Bone Forming Capacity. Calcif. Tiss. Int. 37, 617-624.
10. Nishimoto, S.K. and Price, P.A. (1985) The Vitamin K-Dependent Bone Protein is Accumulated Within Cultured Osteosarcoma Cells in the Presence of the Vitamin K Antagonist Warfarin. J. Biol. Chem. 260, 2832-2836.
11. Nishimoto, S.K., Salka, C. and Nimni, M.E. (1987) Modulation of Bone g- Carboxyglutamic Acid Protein Secretion by Glucocorticoids and Retinoic Acid. J. Bone and Mineral Res. 2, 571-577.
12. Nishimoto, S.K., Stryker, W.F. and Nimni, M.E. (1987) Calcification of Osteoblast-like Rat Osteosarcoma Cells in Agarose Suspension Cultures. Calcif. Tiss. Int. 41, 274-280.
17. Nishimoto, S.K. (1990) A Colorimetric Assay Specific for g-Carboxyglutamic Acid-Containing Proteins. Its Utility in Protein Purification Procedures Anal. Biochem. 186, 273-279.
20. Nishimoto, S.K., Araki, N., Robinson, F.D., and Waite, J.H. (1992) Discovery of Bone g-Carboxyglutamic Acid Protein in Mineralized Scales. The Abundance and Structure of Lepomis Macrochirus Bone g-Carboxyglutamic Acid Protein. J. Biol Chem. 267, 11600-11605.
21. Araki, N., Robinson, F.D. and Nishimoto, S.K. (1993) Rapid and Sensitive Method for Quantitation of Bone Gla Protein mRNA using competitive Polymerase Chain Reaction. J. Bone and Mineral Res., 8, 313-322.
22. Nishimoto, S.K., Robinson, F.D. and Snyder, D.L. (1993) Effect of Aging and Dietary Restriction on Matrix Gla Protein and Other Components of Rat Tracheal Cartilage. Matrix, 13, 373-380.
23. Nishimoto, S.K., Zhao, J. and Dass, C. (1994) Isolation and Characterization of the Reaction Product of 4-diazobenzenesulfonic Acid and g- Carbosyglutamic Acid. Anal. Biochem.,216, 159-164.
24. Thiede, M.A., Smock, S.A., Petersen, D.L., Grasser, W., Thompson, D.D., and Nishimoto, S.K. (1994) Presence of mRNA Encoding Osteocalcin a Marker of Bone Turnover in Bone Marrow Megakaryocytes and Peripheral Blood Platelets. Endocrinology 135, 929-937.
25. Zhao, J., Araki, N. and Nishimoto, S.K. (1995) Quantitation of Matrix Gla Protein by Competitive Polymerase Chain Reaction Using Glyceraldehyde-3- Phosphate Dehydrogenase as an Internal Control. Gene, in press.
5 Book & Symposium Chapters and 15 Published Meeting Abstracts.