TY - JOUR
T1 - Electron spin resonance studies of nitrosyl haemoglobin in human liver, colon and stomach tumour tissues
AU - Symons, Martyn C.R.
AU - Rowland, Ian J.
AU - Deighton, Nigel
AU - Shorrock, Kenneth
AU - West, Kevin P.
N1 - Funding Information:
We would like to express our thanks to the Cancer Research Campaign and The Association for International Cancer Research for funding this work. We would also like to thank the surgeons of Leicester Royal Infirmary who provided the tissue samples. The major part of this work was carried out at Leicester University.
PY - 1994
Y1 - 1994
N2 - Iron nitrosyl haemoglobin (HbFeNO) gives well defined ESR spectra, and can be detected at room temperature, in contrast with most transition metal complexes of biological importance. This is because the unpaired electron remains strongly localised on the NO ligand. It is of importance because it proves the formation of nitric oxide, which unfortunately cannot be detected directly by ESR spectroscopy. We have studied a range of tissues taken from human liver, colon and stomach tumours which have been directly frozen to 77K and studied at 77K. The results show that formation of HbFeNO is rare in tissue adjacent to tumour tissue ("peripheral tissue" but is always found in necrotic central regions, if present. However, in several cases, HbFeNO was also detected in tumour tissue which was not necrotic. Two factors contribute to the formation of this complex. One is the presence of "free" NO molecules in the cellular regions, and the other is the presence of deoxyferrohaemoglobin, since neither ferrihaemoglobin nor oxyhaemoglobin react to give this complex. [For systems containing myoglobin these comments include the possibility of the formation of nitrosylmyoglobin, which gives very similar ESR spectra.]
AB - Iron nitrosyl haemoglobin (HbFeNO) gives well defined ESR spectra, and can be detected at room temperature, in contrast with most transition metal complexes of biological importance. This is because the unpaired electron remains strongly localised on the NO ligand. It is of importance because it proves the formation of nitric oxide, which unfortunately cannot be detected directly by ESR spectroscopy. We have studied a range of tissues taken from human liver, colon and stomach tumours which have been directly frozen to 77K and studied at 77K. The results show that formation of HbFeNO is rare in tissue adjacent to tumour tissue ("peripheral tissue" but is always found in necrotic central regions, if present. However, in several cases, HbFeNO was also detected in tumour tissue which was not necrotic. Two factors contribute to the formation of this complex. One is the presence of "free" NO molecules in the cellular regions, and the other is the presence of deoxyferrohaemoglobin, since neither ferrihaemoglobin nor oxyhaemoglobin react to give this complex. [For systems containing myoglobin these comments include the possibility of the formation of nitrosylmyoglobin, which gives very similar ESR spectra.]
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U2 - 10.3109/10715769409056571
DO - 10.3109/10715769409056571
M3 - Article
C2 - 7827691
AN - SCOPUS:0028501439
SN - 1071-5762
VL - 21
SP - 197
EP - 202
JO - Free Radical Research
JF - Free Radical Research
IS - 4
ER -