Heme oxygenase isozymes in bone: Induction of HO-1 mRNA following physiological levels of mechanical loading in vivo

S C F Rawlinson, G Zaman, J R Mosley, A A Pitsillides, L E Lanyon

Research output: Contribution to journalArticlepeer-review

Abstract

Heme oxygenases (HO) are responsible for the production of carbon monoxide, which has been suggested to act similarly to nitric oxide as a signaling molecule. Inducible HO-1 and constitutive HO-2 were located in sections of weight-bearing ulnae of the rat by immunocytochemistry. Intense HO-1 localization was restricted to peri- and endosteal sites, whereas HO-2 staining occurred in osteoblasts and osteocytes throughout the cortex. Northern blot hybridization of mRNA levels for HO-1 and HO-2 extracted from bones was also performed. Six hours after a single 10 min period of noninvasive mechanical loading of the ulna in vivo, generating physiological levels of strain sufficient to initiate an osteogenic response, the level of mRNA for the inducible HO-1 isoform was increased, but that of HO-2 was unchanged. The presence of a constitutive and strain-related upregulation of an inducible enzyme capable of producing carbon monoxide suggests that carbon monoxide may participate not only in bone cells' basal metabolism but also in their adaptive responses to mechanical load. (C) 1998 by Elsevier Science Inc. All rights reserved.

Original languageEnglish
Pages (from-to)433-436
Number of pages4
JournalBone
Volume23
Issue number5
Publication statusPublished - Nov 1998

Keywords

  • heme oxygenase
  • osteocytes
  • osteoblasts
  • mechanical load
  • NITRIC-OXIDE
  • CARBON-MONOXIDE
  • PROSTACYCLIN SYNTHASE
  • ENDOTHELIAL-CELLS
  • MOLECULAR-CLONING
  • RESPONSE GENES
  • MESSENGER-RNA
  • RAT-BRAIN
  • STRESS
  • CDNA

Cite this