Distribution of heme oxygenase isoforms in rat liver characterized by novel monoclonal antibodies

Nobuhito Goda, M. Naito, T. Tamatani, Y. Ishimura, M. Suematsu

Research output: Contribution to journalArticle

Abstract

Carbon monoxide (CO) derived from heme oxygenase has been shown to play a role in controlling hepatobiliary function (J. Clin. Invest. 96, 1995), but intrahepatic distribution of the enzyme is unknown. We examined distribution of two kinds of the heme oxygenase isoforms (HO-1 and HO-2) in rat liver immunohistochemically using newly raised monoclonal antibodies. Mouse T cell lines (WR19L) transfected with rat HO-1 and HO-2 cDNAs were established, and BALB/c mice were injected with their microsomal fractions to obtain B lymphocytes for development of antibody-producing hybridomas. Monoclonal antibodies against HO-1 and -2 obtained by this method were named GTS-1 and GTS-2, respectively, and no crossreactivity was evident as assessed by Western blotting analysis using cell lysates from rHO-1 and rHO-2 transfectant cells. The results showed that distribution of the two isoforms had distinct topographic patterns: HO-1, an inducible isoform, was observed only in Kupffer cells, while HO-2, a constitutive form, distributed to parenchymal cells, but not to Kupffer cells. Both isoforms were undetectable in hepatic stellate cells nor sinusoidal endothelial cells. These results indicate that CO endogenously generated by the HO reaction is derived not only from the intrasinusoidal compartment (Kupffer cells), but also from the extrasinusoidal space (parenchymal cells), and thus shed light on microtopographic basis for CO-mediated vasorelaxing mechanisms in the liver.

Original languageEnglish
JournalFASEB Journal
Volume12
Issue number5
Publication statusPublished - 1998 Mar 20
Externally publishedYes

Fingerprint

Heme Oxygenase (Decyclizing)
heme
oxygenases
Liver
Kupffer Cells
Rats
monoclonal antibodies
Protein Isoforms
Kupffer cells
Carbon Monoxide
Monoclonal Antibodies
carbon monoxide
liver
rats
cells
Hepatic Stellate Cells
T-cells
Lymphocytes
Endothelial cells
Hybridomas

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Distribution of heme oxygenase isoforms in rat liver characterized by novel monoclonal antibodies. / Goda, Nobuhito; Naito, M.; Tamatani, T.; Ishimura, Y.; Suematsu, M.

In: FASEB Journal, Vol. 12, No. 5, 20.03.1998.

Research output: Contribution to journalArticle

Goda, N, Naito, M, Tamatani, T, Ishimura, Y & Suematsu, M 1998, 'Distribution of heme oxygenase isoforms in rat liver characterized by novel monoclonal antibodies', FASEB Journal, vol. 12, no. 5.
Goda, Nobuhito ; Naito, M. ; Tamatani, T. ; Ishimura, Y. ; Suematsu, M. / Distribution of heme oxygenase isoforms in rat liver characterized by novel monoclonal antibodies. In: FASEB Journal. 1998 ; Vol. 12, No. 5.
@article{4807d7752e514b9eafd0af4de0e0e0ff,
title = "Distribution of heme oxygenase isoforms in rat liver characterized by novel monoclonal antibodies",
abstract = "Carbon monoxide (CO) derived from heme oxygenase has been shown to play a role in controlling hepatobiliary function (J. Clin. Invest. 96, 1995), but intrahepatic distribution of the enzyme is unknown. We examined distribution of two kinds of the heme oxygenase isoforms (HO-1 and HO-2) in rat liver immunohistochemically using newly raised monoclonal antibodies. Mouse T cell lines (WR19L) transfected with rat HO-1 and HO-2 cDNAs were established, and BALB/c mice were injected with their microsomal fractions to obtain B lymphocytes for development of antibody-producing hybridomas. Monoclonal antibodies against HO-1 and -2 obtained by this method were named GTS-1 and GTS-2, respectively, and no crossreactivity was evident as assessed by Western blotting analysis using cell lysates from rHO-1 and rHO-2 transfectant cells. The results showed that distribution of the two isoforms had distinct topographic patterns: HO-1, an inducible isoform, was observed only in Kupffer cells, while HO-2, a constitutive form, distributed to parenchymal cells, but not to Kupffer cells. Both isoforms were undetectable in hepatic stellate cells nor sinusoidal endothelial cells. These results indicate that CO endogenously generated by the HO reaction is derived not only from the intrasinusoidal compartment (Kupffer cells), but also from the extrasinusoidal space (parenchymal cells), and thus shed light on microtopographic basis for CO-mediated vasorelaxing mechanisms in the liver.",
author = "Nobuhito Goda and M. Naito and T. Tamatani and Y. Ishimura and M. Suematsu",
year = "1998",
month = "3",
day = "20",
language = "English",
volume = "12",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "5",

}

TY - JOUR

T1 - Distribution of heme oxygenase isoforms in rat liver characterized by novel monoclonal antibodies

AU - Goda, Nobuhito

AU - Naito, M.

AU - Tamatani, T.

AU - Ishimura, Y.

AU - Suematsu, M.

PY - 1998/3/20

Y1 - 1998/3/20

N2 - Carbon monoxide (CO) derived from heme oxygenase has been shown to play a role in controlling hepatobiliary function (J. Clin. Invest. 96, 1995), but intrahepatic distribution of the enzyme is unknown. We examined distribution of two kinds of the heme oxygenase isoforms (HO-1 and HO-2) in rat liver immunohistochemically using newly raised monoclonal antibodies. Mouse T cell lines (WR19L) transfected with rat HO-1 and HO-2 cDNAs were established, and BALB/c mice were injected with their microsomal fractions to obtain B lymphocytes for development of antibody-producing hybridomas. Monoclonal antibodies against HO-1 and -2 obtained by this method were named GTS-1 and GTS-2, respectively, and no crossreactivity was evident as assessed by Western blotting analysis using cell lysates from rHO-1 and rHO-2 transfectant cells. The results showed that distribution of the two isoforms had distinct topographic patterns: HO-1, an inducible isoform, was observed only in Kupffer cells, while HO-2, a constitutive form, distributed to parenchymal cells, but not to Kupffer cells. Both isoforms were undetectable in hepatic stellate cells nor sinusoidal endothelial cells. These results indicate that CO endogenously generated by the HO reaction is derived not only from the intrasinusoidal compartment (Kupffer cells), but also from the extrasinusoidal space (parenchymal cells), and thus shed light on microtopographic basis for CO-mediated vasorelaxing mechanisms in the liver.

AB - Carbon monoxide (CO) derived from heme oxygenase has been shown to play a role in controlling hepatobiliary function (J. Clin. Invest. 96, 1995), but intrahepatic distribution of the enzyme is unknown. We examined distribution of two kinds of the heme oxygenase isoforms (HO-1 and HO-2) in rat liver immunohistochemically using newly raised monoclonal antibodies. Mouse T cell lines (WR19L) transfected with rat HO-1 and HO-2 cDNAs were established, and BALB/c mice were injected with their microsomal fractions to obtain B lymphocytes for development of antibody-producing hybridomas. Monoclonal antibodies against HO-1 and -2 obtained by this method were named GTS-1 and GTS-2, respectively, and no crossreactivity was evident as assessed by Western blotting analysis using cell lysates from rHO-1 and rHO-2 transfectant cells. The results showed that distribution of the two isoforms had distinct topographic patterns: HO-1, an inducible isoform, was observed only in Kupffer cells, while HO-2, a constitutive form, distributed to parenchymal cells, but not to Kupffer cells. Both isoforms were undetectable in hepatic stellate cells nor sinusoidal endothelial cells. These results indicate that CO endogenously generated by the HO reaction is derived not only from the intrasinusoidal compartment (Kupffer cells), but also from the extrasinusoidal space (parenchymal cells), and thus shed light on microtopographic basis for CO-mediated vasorelaxing mechanisms in the liver.

UR - http://www.scopus.com/inward/record.url?scp=33749356824&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749356824&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33749356824

VL - 12

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 5

ER -