NDLI: CBP/p300-Interacting Protein CITED1 Modulates Parathyroid Hormone Regulation of Osteoblastic Differentiation

Content Provider	PubMed Central
Author	Yang, Dehong Guo, Jun Paola, Divieti Shioda, Toshi Bringhurst, F. Richard
Copyright Year	2008
Abstract	PTH regulates osteoblastic differentiation and activity and exerts different overall skeletal effects in vivo, depending on the schedule and dose of administration. In clonal Wt9 murine osteoblastic cells, mRNA and protein levels of CITED1 transcriptional coactivator were strongly up-regulated by human (h) PTH(1–34). Stimulation of CITED1 mRNA by PTH was transient, peaking at 4 h, concentration dependent, and blocked by actinomycin D but not cycloheximide. The stimulation was mimicked by forskolin, phorbol ester, and the cAMP-selective PTH analog [G1,R19] hPTH (1–28) and inhibited completely by the protein kinase A inhibitor, H89 and partially by phorbol ester-induced protein kinase C depletion. Increased CITED1 expression was not maintained during persistent (24 h) PTH exposure. Cultured primary calvarial osteoblasts from neonatal homozygous or hemizygous CITED1-knockout (KO) mice achieved 2-fold greater mineralized nodule formation in comparison with wild type (WT) osteoblasts. This effect was blocked by restoration of CITED1 expression via adenoviral gene transfer. Intermittent administration of hPTH(1–34) (10 nm, for 4 h every 48 h) for 3–6 wk increased mineralization up to 2-fold over basal levels in both WT and CITED1 KO mouse calvarial cell cultures. Whereas the cAMP-selective [G1,R19]hPTH(1–28) analog [at 100 nm, equivalent to 10 nm hPTH(1–34)] did not stimulate mineralization in WT cultures, it was twice as effective as hPTH(1–34) in CITED1 KO cultures. Thus, CITED1 negatively regulates osteoblastic differentiation in vitro and inhibits the cAMP-dependent stimulation of differentiation by intermittent PTH. We conclude also that PTH receptor signaling pathways independent of cAMP restrain osteoblastic differentiation, an effect normally obscured in the presence of CITED1 but revealed in its absence.
Related Links	http://dx.doi.org/10.1210/en.2007-0826
Ending Page	1735
Page Count	8
Starting Page	1728
File Format	PDF
ISSN	00137227
e-ISSN	19457170
Journal	Endocrinology
Issue Number	4
Volume Number	149
Language	English
Publisher	The Endocrine Society
Publisher Date	2008-04-01
Access Restriction	Open
Rights Holder	The Endocrine Society
Subject Keyword	Endocrinology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Endocrinology

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