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Biosynthesis and function of all-trans- and 9-cis retinoic acid in parathyroid cells

Liu, Wei (author)
Uppsala universitet,Institutionen för kirurgiska vetenskaper,Endocrine Surgery
Hellman, Per (author)
Uppsala universitet,Institutionen för kirurgiska vetenskaper,Endocrine Surgery
Li, Qing (author)
Uppsala universitet,Institutionen för genetik och patologi
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Yu, Wen-Ru (author)
Uppsala universitet,Institutionen för kirurgiska vetenskaper
Juhlin, Claes (author)
Uppsala universitet,Institutionen för kirurgiska vetenskaper,Endocrine Surgery
Nordlinder, Hans (author)
Uppsala universitet,Institutionen för genetik och patologi
Rollman, Ola (author)
Uppsala universitet,Institutionen för medicinska vetenskaper,Dermatology and Venereology
Åkerström, Göran (author)
Uppsala universitet,Institutionen för kirurgiska vetenskaper,Endocrine Surgery
Törmä, Hans (author)
Uppsala universitet,Institutionen för medicinska vetenskaper,Dermatology and Venereology
Melhus, Håkan (author)
Uppsala universitet,Institutionen för medicinska vetenskaper,Osteoporos
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 (creator_code:org_t)
Elsevier BV, 1996
1996
English.
In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 229:3, s. 922-929
  • Journal article (peer-reviewed)
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  • We demonstrate that cultured human and bovine parathyroid cells incubated with all-trans-[11,12-3H]-retinol convert this tracer into all-trans- and 9-cis-retinoic acid. By using RT-PCR, cellular retinol-binding protein type I (CRBP I), cellular retinoic acid binding protein I and II (CRABP I and II), retinoic acid receptors (RARs) alpha, beta and gamma, and 9-cis-retinoic acid receptor (RXR) alpha transcripts were detected in human parathyroid cDNA. CRBP I and CRABP I expression was confirmed by immunohistochemistry. Both 9-cis- and all-trans-RA were found to suppress parathyroid hormone (PTH) secretion from dispersed human adenomatous parathyroid cells, which was augmented by combined treatment with 1mM RA and 100 nM 1,25 (OH)2D3. The present data establish parathyroid gland as a target for retinoids and as a site of synthesis of the hormonal forms of vitamin A (retinol), all-trans- and 9-cis-retinoic acid.

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