Abstract
The impact of molecular and cell biology on endocrinology, as on many other fields of biomedical science, has been immense over the last decade. Genes for most of the peptide hormones have been cloned and analyzed over the last three years; more recently, the difficult task of cloning hormone receptors has been accomplished at least for several hormonal systems. Development of bacterial or mammalian cell systems to express the cDNA and genes for hormones and receptors, coupled with oligonucleotide directed mutagenesis, is permitting wide exploration of structure/activity relations for peptide hormones in endocrine signaling. The techniques of peptide chemistry can now be combined with those of molecular biology to investigate in detail the contribution of primary structure to endocrine function.
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References
Bringhurst FR, Stern AM, Yotts M, Mizrahi N, Potts, JT Jr. Peripheral metabolism of parathyroid hormone: fate of the biologically active amino-terminus in vivo. Am J Physiol. (submitted).
Nussbaum SR, Zahradnik RJ, Lavigne JR, Brennan GL, Nozawa-Ung K, Kim LV, Keutman HT, Wang CA, Potts JT Jr., Segre GV A Highly Sensitive Two-Site Immunoradiometric Assay of Parathyroid Hormone and its Clinical Utility in Evaluating Patients with Hypercalcemia. Clin Chem 33, 1364–1367, 1987.
Wiren KM, Ivashkiv L, Ma P, Freeman MW, Hellerman J, Potts JT Jr, Kronenberg HM. Mutations in Signal Sequence Cleavage Domain of Preproparathyroid Hormone Induce Stop-Transfer Function and Alter Protein Translocation and Signal Sequence Clevage. Mol Cell Biol, (submitted)
Wiren KM, Potts JT Jr, Kronenberg HM. Functional consequences of precise deletion of the pro sequence from preproparathyroid hormone. J Cell Biol, (submitted).
Freeman MW, Wiren KM, Rapoport A, Lazar M, Potts JT Jr, Kronenberg HM. Consequences of amino-terminal deletions of preproparathyroid hormone signal sequence. Molec Endocrinol, (in press).
Hellerman JG, Cone RC, Segre GV, Potts JT Jr, Rich A, Mulligan RC, Kronenberg HM. Secretion of human parathyroid hormone from rat pituitary cells infected with a recombinant retrovirus encodling preproparathyroid hormone. Proc Natl Acad Sci USA. 1984; 81:5340–5344.
Igarashi T, Muramatsu OA, Ogata E, Okazaki T, Kronenberg HM. Functional analysis of the promoter region of the humanparathyroid hormone gene: sequences responsible for basal expression and for responsiveness to 25(OH)2 vitamin D. Nature, (submitted).
Okasazi T, Kronenberg HM. Unpublished results.
Zajac J, Kronenberg HM. Unpublished results.
Maniatis T, Goodbourn S, Fischer JA. Regulation of inducible and tissue-specific gene expression. Science 236:1237–1245, 1987.
Segre GV, Rosenblatt M, Rully GL III, Laugharn J, Reit B, Potts JT Jr. Evaluation of an in vitroparathyroid hormone antagonist in vivoin dogs. Endocrinology. 1985, 116: 1024–1029.
Horiuchi N, Holick MF, Potts JT Jr, Rosenblatt M. A parathyroid hormone inhibitor in vivo: design and biological evaluation of a hormone analog. Science. 1983; 220: 1053–1055.
Doppelt SH, Neer RM, Nussbaum SR, Federico P, Potts JT Jr, Rosenblatt M. Inhibition of thein vivoparathyroid hormone-mediated calcemic response in rats by a synthetic hormone antagonist. Proc Natl Acad Sci USA. 1986; 83: 7557–7560.
Khosla S, Kronenberg HM. Unpublished results.
Suva LF, Winslow GA, Wettenhall REH, Hammonds RG, Moseley JM, Diefenbach-Jagger H, Rodda CP, Kemp BE, Rodriguez H, Chen EY, Hudson PJ, Martin TJ, Wood WI. A parathyroid hormone-related protein implicated in malignant hypercalcemia: cloning and expression. Science, August, 1987 237: 893–896.
Pang PKT, Yang MCM, Keutmann HT, Kenny AD. Structure activity relationship of parathyroid hormones: separation of the hypotensive and hypercalcemic properties. Endocrinology. 1983; 112: 284–289.
Ulrich, Gray, Tam, Yang-Feng, Stsubokawa, Collins, Henzel, LeBon, Kathuria, Chen-Jacobs, Francke, Ramachandran, Fujita-Yamaguchi. Insulin-like growth factor 1 receptor primary structure: Comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J 5: 2503–2512, 1986.
Bonner TI, Buckley NJ, Young, AC Brann MR. Identification of a family of muscarinic acetyl choline receptor genes. Science 237: 527–532, 1987
Benovic JL, Mayor F, Somers RL, Caron MG, Lefkowitz RJ. Light dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase. Nature 321:869–872, 1987.
Dixon RAF, Signal IS, Rands E, Register RB, Candelore MR, Blake AD, Strader CD. Ligand binding to beta-adrenergic receptor involves its rhodopsin-like core. Nature 326: 73–77, 1987
Strader CD, Signal IS, Register RB, Candelore MR, Rands E, Dixon RAF. Identification of residues required for ligand binding to the beta-adrenergic receptors. Proc Natl Acad Sci USA 84:4384–4388, 1987
Styer L, Bourne HR. G proteins: a family of signal transducers. Ann Rev Cell Biol 2:391–419, 1986.
Pang PKT, Yang M, Oguro C, Phillips JG Ye JA. Hypotensive actions of parathyroid hormone preparations in vertebrates. J GenComp Endocrinol I98O.
Baczynsky R, Massry SG, Cohan R, Magott M, Saglikes Y, Brautbiar N. Effect of parathyroid hormone on myocardial energy metabolism in the rat. Kidney Int 27:718–725, 1987
Meytes D, Bogin E, Ma A, Dukes PP, Massry SG. Effect of parathyroid hormone on erythropoesis. J Clin invest 67:1263–1269, 1981.
Remuzzi G, Dodesini P, Livo M, Mecca G, Benigni A, Schieppati A, Poletti E, Degaetono G. Parathyroid hormone inhibits human platelet function. Lancet 1321–1323, 1981.
Yoshiraasa T, Sibley DR, Bouvier M, Lefkowitz RJ, Caron MC, Cross¬talk between cellular signalling pathways suggested by phorbol ester induced adenylate cyclase phosphorylation. Nature 327:67–70, 1987.
Hruska KA, Moskowitz D, Esbrit P, Civitelli R, Westbrook S, and Huskay M. J Clin Invest 79:230–239, 1987.
Civitelli R, Reid Ir, Dobre V, Shen V, Halstead L, Avioli LV, and Hruska K. J Bone Min Res 2 (Suppl 1): Abstr. 233, 1987.
Bringhurst FR, Zajac JD, Daggett As, Clegg C, McNight GS, Kronenberg HM Osteoblastic cell lines genetically engineered to express nonresponsive cAMP-dependent protein kinase. (American Society for Bone and Mineral Research, Annual scientific Meeting, 9th Indianapolis, Indiana,June 6-9, 1987. J Bone Min Res. 1987; 2 (Supp. 1), Abst. 235.
Abou-Samra AB, Jueppner H, Westerberg D, Potts, JT Jr, Segre GV. Parathyroid hormone modulates protein kinase-C activity in rat osteosarcoma cells. J Biol Chem. (submitted).
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© 1989 Plenum Press, New York
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Potts, J.T. et al. (1989). Chemistry, Molecular Biology and Mode of Action of Parathyroid Hormone. In: Massry, S.G., Fujita, T. (eds) New Actions of Parathyroid Hormone. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0567-5_2
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DOI: https://doi.org/10.1007/978-1-4613-0567-5_2
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