Abstract
The physiologic actions of PTH on kidney and bone are initiated by hormonal binding to receptors in the plasma membrane of responsive cells. Occupation of receptors by PTH leads to activation of adenylate cyclase and increased cellular levels of cAMP. Cyclic AMP in turn activates a protein kinase(s), which results in specific substrate phosphorylation and ultimately biologic effects. Most, though not all, evidence supports such a mechanism of PTH action (1). Perhaps most compelling in this regard is the functional hypoparathyroidism seen in a subgroup of patients with pseudohypoparathyroidism (type Ia) who have a genetic deficiency in the stimulatory guanine nucleotide binding component (Ns) of adenylate cyclase (2,3).
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© 1986 Plenum Press, New York
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Nissenson, R.A., Mann, E., Winer, J., Teitelbaum, A., Arnaud, C.D. (1986). Solubilization of a Guanine Nucleotide-Sensitive Parathyroid Hormone-Receptor Complex from Canine Renal Cortex. In: Massry, S.G., Olmer, M., Ritz, E. (eds) Phosphate and Mineral Homeostasis. Advances in Experimental Medicine and Biology, vol 208. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5206-8_41
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DOI: https://doi.org/10.1007/978-1-4684-5206-8_41
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