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Copper (Cu) and zinc (Zn) are involved in inflammatory process. This study was to investigate the clinical significance of Cu and Zn homeostasis alterations in acute appendicitis (AA). One hundred twenty-two AA patients and 102 healthy controls were enrolled in this study. Of which, 85 patients' appendixes were collected after appendectomy. Another six appendixes from colon cancer patients were collected as tissue controls. The contents of Cu and Zn in serum or appendix were detected, and the Cu to Zn ratio (CZr) was calculated. The concentrations of serum ceruloplasmin (CP), Cu/Zn superoxide dismutase (SOD1), interleukin-6 (IL-6), and interleukin-22 in serum were measured, as well as the activity of CP and SOD1. The serum Zn concentration and SOD1 activity, appendix contents of Cu and Zn significantly decreased in AA patients, compared with those of controls, while serum CZr, concentrations of CP, SOD1, and IL-6, as well as CP activity increased significantly in AA patients. Additionally, serum concentrations of Zn, CP, CZr, or SOD1 activity varied in different pathological types of AA. Indicators such as serum SOD1 activity might serve as predictors for pathological classification before surgery. The serum Zn and CZr may be helpful for diagnosis of pure AA. The Cu and Zn homeostasis was altered in AA patients, which might contribute to inflammatory process of AA. [ABSTRACT FROM AUTHOR]

The objective of this research was to develop a method for measuring Cu/Zn-superoxide dismutase (Cu/Zn-SOD) (E.C. 1.15.1.1) in HL-60 cells and subsequently examine the relationship between cellular copper levels and the activity of this copper-requiring enzyme. In cells such as the neutrophil or HL-60 promyelocyte cell line, the activity of Cu/Zn-SOD cannot be measured because of an increase in the oxidation rate of the substrate by some unknown compound in the cells. Others have utilized heat treatment to inactivate the responsible compounds, however, we found that heat treatment of HL-60 cells resulted in a loss of over half of the activity of the enzyme. The method described here utilizes sodium azide to inhibit the substance(s) that are responsible for the enhanced rate of pyrogallol's oxidation. Gel filtration data confirmed that the compound responsible for the enhanced rate of pyrogallol oxidation was sensitive to azide and did not affect Cu/Zn-SOD activity. When HL-60 cells were incubated with various levels of copper, Cu/Zn-SOD activity did not reflect the cellular copper levels. [ABSTRACT FROM AUTHOR]