11.BETA.-Hydroxysteroid Dehydrogenase Activity in Human Aortic Smooth Muscle Cells.

• HATAKEYAMA Haruhiko

  Third Department of Internal Medicine, Fukui Medical University

• INABA Satoru

  Third Department of Internal Medicine, Fukui Medical University

• MIYAMORI Isamu

  Third Department of Internal Medicine, Fukui Medical University

Abstract

11β-Hydroxysteroid dehydrogenases (11β-HSD) interconvert cortisol, the physiological glucocorticoid, and its inactive metabolite cortisone in humans. There are two isoforms. The type 1 isoform (11β-HSD1) catalyzes both 11β-dehydrogenation (cortisol to cortisone) and the reverse oxoreduction (cortisone to cortisol), but the type 2 isoform (11β-HSD2) catalyzes only 11β-dehydrogenation. The diminished dehydrogenase activity has been demonstrated in resistance vessels of genetically hypertensive rats. However, the isoform(s) that plays a significant role in conferring the dehydrogenase activity on vasculature has not been determined. We investigated 11β-HSD activities in human vascular smooth muscle cells by manipulating 11β-HSD expressions with antisense oligonucleotides. The results showed that 11β-HSD2 dominates functioning in the dehydrogenase mode in these cells. This indicates that impairment of 11β-HSD2 activity in vascular wall may be related to the pathogenesis of hypertension. (Hypertens Res 2001; 24: 33-37)

Journal

• Hypertension Research

  Hypertension Research 24 (1), 33-37, 2001

  The Japanese Society of Hypertension

Keywords

• 11β-hydroxysteroid dehydrogenases (11β-HSD)
• antisense oligonucleotide
• human aortic smooth muscle cells (HASMC)
• hypertension

Details

• CRID: 1390282679695538560
• NII Article ID: 10008741934
• NII Book ID: AA10847079
• DOI: 10.1291/hypres.24.33
• COI: 1:CAS:528:DC%2BD3MXhtl2iur8%3D
• ISSN: 13484214
• ISSN: 09169636
• PubMed: 11213028
• Web Site: https://search.jamas.or.jp/link/ui/2001156886
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• Abstract License Flag: Disallowed