Tin-protoporphyrin inhibits heme oxygenase and prevents the decline in hepatic heme and cytochrome P-450 contents produced in nude mice by tumor transplantation. Academic Article uri icon

Overview

abstract

  • Heme and hemeprotein perturbations are present in nude mice bearing transplanted tumors. Hepatic microsomal heme oxygenase activity is increased 50-100% in tumor bearing nu/nu mice when compared with normal controls. This elevation in activity of the rate-limiting enzyme of heme degradation is associated with a 50% depletion of microsomal heme and cytochrome P-45 concentrations in liver. The synthetic heme analogue, Sn-protoporphyrin, a potent inhibitor of heme oxygenase, lowers the activity of heme oxygenase in tumor bearing animals to below control levels. This effect is associated with a normalization of hepatic heme and cytochrome P-450 contents. These findings might have implications for protecting normal cells during tumor growth and chemotherapy.

publication date

  • January 29, 1988

Research

keywords

  • Carcinoma
  • Cytochrome P-450 Enzyme System
  • Heme
  • Heme Oxygenase (Decyclizing)
  • Leukemia, Experimental
  • Metalloporphyrins
  • Microsomes, Liver
  • Mixed Function Oxygenases
  • Porphyrins
  • Protoporphyrins

Identity

Scopus Document Identifier

  • 0023855409

PubMed ID

  • 3422558

Additional Document Info

volume

  • 150

issue

  • 2