Ph.D., University of California, Berkeley
Caleb Mills Distinguished Teaching Award, 2005
Office: Science Building 287I
Research Interests: molecular endocrinology; mechanism of hormone and growth factor signal transduction.
The endocrine research program in Dr. Hughes' laboratory is concerned with understanding of the mechanisms whereby receptors mediate the actions of prolactin, growth hormone, and interleukin-2. Part of Dr. Hughes' research involves identification of the cellular events which follow activation of the receptors for prolactin and interleukin-2 in T lymphocytes, and the immunoregulatory role of prolactin. The lab is also studying the protein stathmin (also called Op18) and related proteins, changes in stathmin in response to various growth factors, identification of stathmin-binding proteins, and the range of stathmin occurrence in the animal and plant kingdoms.
Reprints for some publlications are available as PDF files. By accessing the PDF file, the user agrees to abide by all copyright laws and education fair-use regulations.
King, C.S., Ko, W., Aloor, J.J., Prentice, D.A., Hughes, J.P. 2002. Stathmin binds Hsp70 in the Nb2 lymphoma. Proceedings of the Indiana Academy of Science (in press)
Ko, W., Johnson, M.T., Prentice, D.A., Hughes, J.P. 2001. Stathmin expression in the placenta and embryonic brain. Proceedings of the Indiana Academy of Science 110, 35-40. ( Download PDF - 148 kB)
Flurkey, W. H, M. Kelley, J. P. Hughes, T. J. Mulkey, and D. A. Prentice. 1998. Identification of stathmin-like proteins in plants. Plant Physiology and Biochemistry 36: 449-455. ( Download PDF - 5.8 meg)
Prentice, D.A., King, C.S., Ko, W., Hughes, J.P. (1998) Isolation of stathmin-binding proteins from the Nb2 lymphoma and PC12 cells. Abstracts of the Annual Meeting of the American Society for Biochemistry and Molecular Biology.
Prentice, D.A., King, C.S., Vasi, N.H., and Hughes, J.P. 1997. Novel method for isolation of stathmin-binding proteins. Molecular Biology of the Cell 8, 129a.
Gio, J., J.P. Hughes, B. Auperin, H. Buteau, M. Edery, H. Zhuang, D.M. Wojchowski and N.D. Horseman. . 1996. Interactions among JANUS kinases and the prolactin (PRL) receptor in the regulation of a PRL response element. Molecular Endocrinology 10(7):847-856. ( Download PDF - 209 kB)
Hughes, J. P., W. H. Flurkey, D. A. Prentice and M. T. Fox. 1993. Stathmin in mung bean leaves and rat brain. Biochemical and Biophysical Research Communications 196: 589-595.
Meyer, N., D. A. Prentice, M. T. Fox, and J. P. Hughes. 1992. Prolactin-induced proliferation of the Nb2 lymphoma is associated with protein kinase-C independent phosphorylation of stathmin. Endocrinology 131: 1977-1984. ( Download PDF - 517 kB)
Fox, M. T., D. A. Prentice, and J. P. Hughes. 1991. Increases in pi 1 and annexin II proteins correlate with differentiation in the PC 12 pheochromocytoma. Biochemical and Biophysical Research Communications 177: 1188-1193. ( Download PDF - 378 kB)
Rayhel, E. J., D. A. Prentice, P. S. Tabor, W. H. Flurkey, R. W. Geib, R. F. Laherty, S. B. Schnitzer, R. Chen and J. P. Hughes. 1988. Inhibition of Nb2 T lymphoma cell growth by transforming growth factor-ß. Biochemical Journal 253: 295. ( Download PDF - 765 kB)
Rayhel, E.J. T.J. Fields, J.A. Albright, T. Diamantstein and J.P. Hughes. 1988. Interleukin 2 and a lactogen regulate proliferation and protein phosphorylation in Nb2 cells. Biochem Jour. 249:333-338. ( Download PDF - 143 kB)
Atkinson, P. R., J. E. Seely, H. G. Klembe and J. P. Hughes. 1988. Receptor binding and Nb2 cell mitogenic activities of glycosylated vs. unglycosylated porcine prolactin. Biochemical and Biophysical Research Communications 155: 1187. ( Download PDF - 390 kB)
Lanker, T., W. H. Flurkey and J. P. Hughes. 1988. Cross_reactivity of polyclonal and monoclonal antibodies to polyhenoloxidaseinhigherplants. Phytochemistry 27: 3731. ( Download PDF - 458 kB)
Hughes, J.P., L.L. Wheeler, T.J. Fields, J.M. Schepper, and H.G. Friesen. 1986. Isolation of growth hormone receptor. In: Human Growth Hormone. Ed. S. Raiti and R.A. Tolman, Plenum Publishing. pages 455-461. ( Download PDF - 334 kB)
Hughes, J.P. and H.G. Friesen. 1985. The nature and regulation of the receptors for pituitary growth hormones. Ann. Rev. Physiol. 47:469-482. ( Download PDF - 419 kB)
Hughes, J.P., H.P. Elsholtz and H.G. Friesen. 1985. Growth hormone and prolactin receptors. In: Polypeptide Hormone Receptors, Ed. B.I. Posner. Marcel Dekker, Inc. pages 157-199. ( Download PDF - 3076 kB)
Schepper, J.M. E.P. Hughes, M.C. Postel-Vinay, and J.P. Hughes. 1984. Cleavage of growth hormone by rabbit liver plasmalemma enhances binding. Journal of Biological Chemistry 259(21):12945-12948. ( Download PDF - 124 kB)
Simpson, J.S.A., J.P. Hughes and H.G. Friesen. 1983. A monoclonal antibody to the growth hormone receoptor of rabbit liver membranes. Endocrinology 112(6):2137-2141. ( Download PDF - 96 kB)
Hughes, J.P., J.S.A. Simpson and H.G. Friesen. 1983. Analysis of growth hormone and lactogenic binding sites cross-linked to iodinated human growth hormone. Endocrinology 112(6):1980-1985. ( Download PDF - 147 kB)
Hughes, J.P., E. Tokuhiro, J. Steven, A. Simpson and H.G. Friesen. 1983. 20K is bound with high affinity by one rate and one of two rabbit growth hormone receptors. Endocrinology 113(5):1904-1906. ( Download PDF - 60 kB)
Hughes, J.P. T. Tanaka, P.W. Gout, C.T. Beer, R.L. Noble, and H.G. Friesen. 1982. Effects of iodination on human growth hormone and prolactin: characterized by bioassay, radioimmunoassay, radioreceptor assay, and electrophoresis. Endocrinology 111(3):827-832. ( Download PDF - 137 kB)
Hughes, J.P., H.P. Elsholtz and H.G. Friesen. 1982. Up-regulation of lactogenic receptors - an immunological artifact? Endocrinology 111(2):702-704. ( Download PDF - 253 kB)
Hughes, J.P. 1979. Identification and characterization of high and low affinity binding sites for growth hormone in rabbit liver. Endocrinology 105(2):414-420. ( Download PDF - 1373 kB)
Hughes, J.P. and I.M. Lytle. 1975. Corticosteroids of the Peccary (dicotyles tajacu). General and Comparative Endocrinology 26:277-280. ( Download PDF - 56 kB)