Platelet monoamine oxidase and phenolsulphotransferase M and P in cancer.
Phenolsulphotransferase and monoamine oxidase inactivate a wide range of dietary and endogenous phenols/monoamines by sulphoconjugation and oxidative deamination respectively. In this study, both enzymes were measured in platelets from cancer patients and controls. Of the two variants of phenolsulphotransferase, activity of the P form was normal in all groups. Activity of the M form was, however, significantly less than control values in patients with cancer of the rectum and bowel but not in other cancer patient groups. If this finding reflects enzyme activity elsewhere in the body and is not merely a manifestation of an abnormal platelet population, the deficit could expose affected subjects to the action of potentially carcinogenic dietary phenols. Platelet monoamine oxidase activity was significantly raised in the cancer group as a whole, and in all sub-types investigated apart from breast cancer. The increase in the cancer group as a whole was independent of sex, age, drugs, radiotherapy, smoking or platelet count. Its mechanism and significance are unknown but there may be links with the patients' psychiatric state.
D000328:Adult; D000367:Age Factors; D000368:Aged; D015239:Arylsulfotransferase; D001792:Blood Platelets / Q000201:enzymology*; D005260:Female; D006801:Humans; D008297:Male; D008875:Middle Aged; D008995:Monoamine Oxidase / Q000097:blood*; D009369:Neoplasms / Q000201:enzymology*; D010976:Platelet Count; D012737:Sex Factors; D012907:Smoking; D013466:Sulfurtransferases / Q000097:blood*
D008995:Monoamine Oxidase; D013466:Sulfurtransferases; D015239:Arylsulfotransferase