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Am J Physiol Endocrinol Metab 281: E545-E557, 2001;
0193-1849/01 $5.00
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Vol. 281, Issue 3, E545-E557, September 2001

Parathyroid hormone receptor internalization is independent of protein kinase A and phospholipase C activation

Hesham A. W. Tawfeek, Jian Che, Fang Qian, and Abdul B. Abou-Samra

Endocrine Unit, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114

Parathyroid hormone (PTH) and PTH-related peptide (PTHrP) binding to their common receptor stimulates second messenger accumulation, receptor phosphorylation, and internalization. LLC-PK1 cells expressing a green fluorescent protein-tagged PTH/PTHrP receptor show time- and dose-dependent receptor internalization. The internalized receptors colocalize with clathrin-coated pits. Internalization is stimulated by PTH analogs that bind to and activate the PTH/PTHrP receptor. Cell lines expressing a mutant protein kinase A regulatory subunit that is resistant to cAMP and/or a mutant receptor (DSEL mutant) that does not activate phospholipase C internalize their receptors normally. In addition, internalization of the wild-type receptor and the DSEL mutant is stimulated by the PTH analog [Gly1,Arg19]hPTH-(1-28), which does not stimulate phospholipase C. Forskolin, IBMX, and the active phorbol ester, phorbol-12-myristate-13-acetate, did not promote receptor internalization or increase PTH-induced internalization. These data indicate that ligand-induced internalization of the PTH/PTHrP receptor requires both ligand binding and receptor activation but does not involve stimulation of adenylate cyclase/protein kinase A or phospholipase C/protein kinase C.

parathyroid hormone/parathyroid hormone-related peptide receptor; G protein-coupled receptor; cytoplasmic loops; extracelluar domains; internalization; green fluorescent protein


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