Literature DB >> 11708545

Heme oxygenase (HO) isoforms in experimental C6 glioma: an immunocytochemical study.

S Lo1, H S Bell, S Yamaguchi, S B Wharton, I R Whittle.   

Abstract

Abstract Because of their potential to regulate tumoural blood flow and interactions with nitric oxide the expression of the type 1 and 2 isoforms of heme oxygenase (HO-1 and HO-2) were evaluated in implanted C6 striatal gliomas. Immunocytochemistry using antibodies specific for HO-1 and HO-2 were used in 20 C6 glioma tumours. The bulk of the tumour parenchyma and endothelium was negative for both HO isoforms. Isolated, but weak staining for HO-1 was seen in most tumours with focally increased expression in perinecrotic regions. Cells morphologically resembling macrophages stained with both HO-1 and HO-2, but were not numerous. These findings suggest that carbon monoxide, unlike nitric oxide, does not have a major role in regulating tumoural blood flow in this experimental glioma model. These findings once again demonstrate the differences between human malignant glioma and experimental implantation glioma models.

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Year:  2001        PMID: 11708545     DOI: 10.1080/02688690120082422

Source DB:  PubMed          Journal:  Br J Neurosurg        ISSN: 0268-8697            Impact factor:   1.596


  2 in total

1.  Analysis of heme oxygenase isomers in rat.

Authors:  Zhen-Wei Xia; Wen-Jun Cui; Xue-Hong Zhang; Qing-Xiang Shen; Jian Wang; Yun-Zhu Li; Shen-Nian Chen; Shan-Chang Yu
Journal:  World J Gastroenterol       Date:  2002-12       Impact factor: 5.742

2.  Upregulation of heme oxygenase-1 in colorectal cancer patients with increased circulation carbon monoxide levels, potentially affects chemotherapeutic sensitivity.

Authors:  Hongzhuan Yin; Jun Fang; Long Liao; Hiroshi Maeda; Qi Su
Journal:  BMC Cancer       Date:  2014-06-14       Impact factor: 4.430

  2 in total

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