Clinical significance of arginase in colorectal cancer

Abstract

Arginase, a potent immune inhibitor, existed in much greater abundance in the cytoplasm of cancer cells than in normal cells. Serum arginase levels from 31 patients with colorectal adenocarcinoma were determined by using enzyme immunoassay (mean .t standard error = 18.96 f 4.83 ng/ml) and showed to be significantly higher than levels from control subjects (n = 115, 3.09 _+ 0.22 ng/ml) (P < 0.005). Surgical samples of 15 patients were individually homogenized and assayed by the same method and revealed that the arginase level in tissues with colorectal cancer was two times greater than the level found in normal mucosal tissues (1.74 k 0.31 pg/g tissue versus 0.77 _+ 0.09 K g / g tissue, P < 0.005). However, the serum arginase levels in patients with colorectal cancer were independent of their carcinoembryonic antigen (CEA) levels (n = 27, arginase 11.81 & 1.88 ng/ml, CEA 17.31 & 4.24 ng/ml, r = 0.084, P = 0.666). The results suggested that serum arginase level can be a valuable criterion for preoperative evaluation and possibly postoperative follow-up study. It can also combine with CEA determination to intensify the clinical assessment for colorectal cancer. Cancer 1992; 70:733-736.

Differential gene-expression profiles associated with gastric adenoma

“…Arginase II has been reported to be overexpressed in cancerous tissues in general (Harris et al, 1983;Leu and Wang, 1992;Suer Gokmen et al, 1999;del Ara et al, 2002;Porembska et al, 2003) and it is well established that this gene is overexpressed in gastric adenocarcinomas (Wu et al, 1996). Since ARG2 catalyses the conversion of arginine to ornithine, a crucial metabolite in biosynthesis of glutamic acid, proline and polyamines (Vockley et al, 1996), an increase in the level of arginase may reflect accelerated metabolism due to cell proliferation or tumour growth.…”

Elevated Serum Arginase Activity Levels in Patients with Breast Cancer

“…[11][12][13][14][15][16][17] However, in some pathological conditions, especially in various types of cancer, the elevated activity levels of arginase enzymes in the serum have been reported in many studies, and it is suggested that arginase enzymes supply ornithine, which is a precursor for the biosynthesis of aliphatic polyamines, to cells. [11][12][13][14][15][16][17]21 The polyamines (putrescine, spermidine, and spermine), that are present in all mammalian cells, are essential for cell growth and proliferation and facilitate all the steps of protein synthesis. [21][22][23] In carcinogenesis, these polyamines and the arginase which supplies these polyamines have also been reported to increase.…”

“…These results correlate with the findings of previous studies carried out in other cancer types such as gastric, colorectal, large bowel, urogenital, and prostate cancers. [11][12][13][14][15][16] When the benign group was accepted as the patient group and then was compared with the healthy group as a control, the increases in the arginase activity in the benign group were not statistically significant, which thus indicates that increased activity of this enzyme may be a useful marker in patients with breast cancer. Our results are also in agreement with a previous study carried out by Straus et al, 22 who previously had shown arginase in human breast tissue by agar gel electrophoresis, but without describing the stages of breast cancer.…”

The Significance of Arginase I Administration on the Survival of Mice Bearing NS-1 Myeloma Cells

“…Arginase has been found at increased levels in the serum and cancer tissue of cancer patients, such as gastric cancer [1,2], colorectal cancer [3,4], breast cancer [5], skin cancer [6], lung cancer [7,8], prostate cancer [9], etc. The presence of these increased levels of arginase in cancer tissue may promote cell proliferation [10,11] through the action of polyamines [11] formed from ornithine.…”