Gonadectomy impairs lymphocyte proliferation and macrophage function in male and female rats. Correlation with key enzyme activities of glucose and glutamine metabolism

• Published in: Cell biochemistry and function Vol. 15; no. 4; pp. 293 - 298
• Main Authors: De Azevedo, Ricardo B., Costa Rosa, Luiz F. B. P., Lacava, Zulmira G. M., Curi, Rui
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01-12-1997
• Subjects: Animals; Cell Division - drug effects; Cell Division - physiology; Citrate (si)-Synthase - metabolism; Citric Acid Cycle - physiology; Concanavalin A - pharmacology; Female; Glucose - metabolism; glucose and glutamine; Glucosephosphate Dehydrogenase - metabolism; Glutaminase - metabolism; Glutamine - metabolism; Gonadal Steroid Hormones - physiology; Lipopolysaccharides - pharmacology; lymphocytes; Lymphocytes - cytology; Lymphocytes - enzymology; macrophages; Macrophages - cytology; Macrophages - enzymology; Male; Orchiectomy; Ovariectomy; Pentose Phosphate Pathway - physiology; Rats; Rats, Inbred Strains; sex steroid hormones; Thymidine - metabolism; Thymidine - pharmacology; Tritium
• ISSN: 0263-6484; 1099-0844
• DOI: 10.1002/(SICI)1099-0844(199712)15:4<293::AID-CBF755>3.0.CO;2-1

The effect of gonadectomy on lymphocyte proliferation and macrophage function (hydrogen peroxide production and phagocytosis capacity) of male and female rats was examined and the results correlated with the activities of hexokinase, glucose‐6‐phosphate dehydrogenase, citrate synthase and phosphate‐dependent glutaminase. Also, the reversion of the changes by the treatment with oestrogen or progesterone or a combination of both was addressed. Taken as a whole, ovariectomy reduced hydrogen peroxide production and phagocytosis capacity by macrophages and also lymphocyte proliferation. Castration of male rats reduced the proliferation of lymphocytes and raised macrophage phagocytosis capacity. The effects on macrophage function were correlated with changes in glucose metabolism, particularly, in the activity of glucose‐6‐phosphate dehydrogenase. © 1997 John Wiley & Sons, Ltd.