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J Biol Chem, Vol. 273, Issue 34, 21708-21713, August 21, 1998
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From the Parathyroid cells have an intracellular machinery
for parathyroid hormone (PTH) secretion that is inversely regulated by
the extracellular calcium concentration
(Ca2+o). The recently
characterized Ca2+o-sensing
receptor (CaR) is a G protein-coupled, seven-transmembrane receptor
mediating the inhibitory effects of high
Ca2+o on PTH secretion. The CaR's
precise cell surface localization and the signal transduction
pathway(s) mediating its inhibitory effects on PTH secretion have not
been characterized fully. Here, we demonstrate that the CaR resides
within caveolin-rich membrane domains in bovine parathyroid cells.
Chief cells within bovine parathyroid glands exhibit a similar pattern
of staining for caveolin-1 and for alkaline phosphatase, a
glucosylphosphatidylinositol-anchored protein often enriched in
caveolae. Purified caveolin-enriched membrane fractions (CEMF) from
bovine parathyroid cells are highly enriched in the CaR and alkaline
phosphatase. Other signaling proteins, including Gq/11,
eNOS, and several protein kinase C isoforms (i.e. Endocrine-Hypertension Division and
Department of Medicine, Brigham and Women's Hospital,
Boston, Massachusetts 02115 and the ¶ Endocrine Division,
Children's Hospital, Boston, Massachusetts 02115
, 
,
and 
), are also present in CEMF. Activation of the CaR by high
Ca2+o increases tyrosine
phosphorylation of caveolin-1 in CEMF, suggesting that CaR-mediated
signal transduction potentially involved in
Ca2+o-regulated processes in
parathyroid cells occur in caveolae-like domains.
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