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Japanese Journal of Clinical Oncology Pages 135-139

Increased Level of Circulating Adhesion Molecules in the Sera of Breast Cancer Patients with Distant Metastases
Introduction
Materials And Methods
Results
Discussion
Acknowledgements
References

Increased Level of Circulating Adhesion Molecules in the Sera of Breast Cancer Patients with Distant Metastases

Increased Level of Circulating Adhesion Molecules in the Sera of Breast Cancer Patients with Distant Metastases Nami Matsuura1, Tatsuhiko Narita2, Chikako Mitsuoka2, Naoko Kimura2, Reiji Kannagi2, Tsuneo Imai1, Hiroomi Funahashi1 and Hiroshi Takagi1

1Department of Surgery II, Nagoya University School of Medicine, Nagoya and 2Laboratory of Experimental Pathology, Aichi Cancer Center Research Institute, Nagoya, Japan

The adhesion of circulating cancer cells to the vascular endothelium is an important step in the hematogenous metastasis of cancer. E-selectin expressed on endothelial cells and carbohydrate ligands expressed on cancer cells mediate this adhesion. We investigated the clinical significance of such cell adhesion molecules in breast cancer. The cytosol concentration of sialyl Lewisx was found more elevated in cancerous tissue than that in adjacent non-cancerous tissue. In the serum, sialyl Lewisx and soluble E-selectin were seen elevated in patients with advanced and recurrent breast cancer, especially in those with distant metastases. From the above, we have concluded that sialyl Lewisx and soluble E-selectin could be used as tumor markers with a close relationship to the metastasis of breast cancer.

Key words: breast cancer - cell adhesion molecules - E-selectin - sialyl Lewisx

INTRODUCTION

The adhesion of circulating cancer cells to the vascular endothelium is an important step in the hematogenous metastasis of cancer. Carbohydrate antigens, such as sialyl Lewisx (s-Lex) and sialyl Lewisa are expressed on the surface of cancer cells, and E-selectin is expressed on the surface of endothelial cells to effect this adhesion (1 -12 3 ). We reported previously that E-selectin and s-Lex mediated the adhesion of breast cancer cells to endothelal cells, and the prognosis of patients expressing s-Lex in their cancerous tissue was poorer than in those with negative expression (4 ,5 ). Soluble forms of such cell adhesion molecules are detected in the sera of patients with different diseases, including cancer (6 -12 9 ). Serum s-Lex is currently employed as a tumor marker, SLX, in the clinical medicine of lung, ovarian and gastrointestinal cancers (10 ). However, there has been no investigation reported yet on the clinical significance of SLX in breast cancer. The expression of E-selectin on endothelial cells is enhanced by inflammatory cytokines, such as interleukin 1[beta] (IL-I[beta]) or tumor necrotic factor [alpha] (TNF[alpha]) (11 ). As yet there are only a few studies on the regulatory mechanism of E-selectin expression on endothelial cells in cancer metastasis (12 ,13 ). We reported previously that cancer cells induced the expression of E-selectin on the endothelium directly, or indirectly mediated by interaction with leukocytes (14 ,15 ). As such a regulatory mechanism of E-selectin has been shown to exist in vivo, it can then be surmised that the level of E-selectin in the sera of patients with cancer becomes elevated. In the current study, the authors investigated the clinical significance of such cell adhesion molecules in breast cancer.

MATERIALS AND METHODS

Measurements of the cytosol concentration of s-Lex were conducted on surgical tissue specimens from 80 cases of primary breast cancer. After resection, approximately 0.5 g of specimen was immediately put into a liquid nitrogen tank and kept at -80oC until tissue extraction. Extraction was made by the routine method used in preparing assays of the estrogen receptor (ER). Specifically, the frozen tissue was pulverized in a freezer-mill and treated with a homogenizer in 3 ml of 10 mM Tris, 1 mM EDTA buffer, pH 7.4, containing 12 mmol of thioglycerol and 10% (v/v) glycerol. The homogenate was centrifuged at 105 000 G at 4oC for 60 min. The concentration of s-Lex in the cytosol fraction thus obtained was determined by using an SLX radioimmunoassy kit (Otsuka Pharmaceutical Co., Tokushima, Japan) and for ER by enzyme immunoassay (EIA), with >= 10 fmol/mg protein being considered positive. The total protein concentration in the materials was determined by Lowry's method.

The subjects for the serum assay consisted of 154 female patients on whom histopathological diagnoses had been achieved and who were treated at the Department of Surgery II, Nagoya University School of Medicine and affiliated institutions. The patients consisted of 74 cases of primary breast cancer, 41 cases of postoperative recurrent breast cancer, 25 cases of postoperative non-recurrent breast cancer and 14 cases of benign breast diseases (9 cases of fibrocystic diseases and 5 cases of fibroadenoma). The postoperative non-recurrent breast cancer patients were those who had been followed up for at least 5 years after operation and had shown no signs of recurrence for at least one year from the date of the blood sampling taken in this study. The diagnosis of distant metastasis was carried out by using imaging techniques, such as plain X-ray, CT scan, ultrasonography and bone scintigraphy. Blood samples were collected in the early morning. The serum was then separated and stored at -40oC. The concentrations of soluble E-selectin (sE-selectin) in the blood samples were determined by an EIA measurement kit (R&D systems, Minneapolis, MN) (6 ). The SLX in these same blood samples was determined by radioimmunoassy. The cut-off values were set at 68 ng/ml for sE-selectin and 38 U/ml for SLX (6 ,10 ,16 ).

The histopathological findings were typed according to the General Rules of the Japanese Breast Cancer Society (17 ). Student's t test and Pearson's least-squares method were used in the statistical analyses.

RESULTS

The mean +- SD of SLX concentration in the cytosol in the 80 specimens of breast cancer tissue was 26.28 +- 32.15 U/mg protein, range 0 to 200 U/mg protein (Fig. 1 ). In the adjacent non-cancerous tissues of 7 cases, the cytosol concentration of SLX was 0 to 2.6 U/mg protein. The SLX concentration in cytosol in cancerous tissue was thus higher than that of non-cancerous tissue in every patient (Table 1 ). Cytosol concentration of SLX in the cancerous tissue of scirrhous carcinoma was significantly lower than in those of papillo-tubular carcinoma or solid tubular carcinoma. However, no significant correlation was found between the cytosol SLX concentration in cancerous tissue and the other clinicopathological factors such as tumor diameter, lymph node status and ER status (Table 2 ).


Figure 1. Distribution of cytosol concentration of SLX in 80 breast cancer tissues.

Table 1 . Comparisons of cytosol SLX concentrations in cancerous and non-cancerous portions of breast cancer tissues
Case Cytosol SLX (U/mg protein)
  CA non-CA
1 13.9 0
2 22.0 0
3 39.5 0
4 54.1 0
5 19.1 0.2
6 17.4 0.3
7 30.5 2.6
SLX, sialyl Lewisx tumor marker; CA, cancerous portions; non-CA, non-cancerous portions (of breast tissue).

Table 2. . Correlation between cytosol SLX concentration and clinicopathological factors
Factor n Mean +- SD of SLX (U/mg protein)
(Total) 80 26.8 +- 32.2
Tumor diameter
  <3 cm 45 26.3 +- 30.4
  >= 3 cm 35 27.5 +- 34.8
Lymph node involvement
  Negative 30 22.6 +- 31.1
  Positive 50 29.4 +- 32.8
Histopathological type
  Papillo-tubular carcinoma* 25 32.9 +- 38.2
  Solid tubular carcinoma* 32 30.1 +- 35.9
  Scirrhous carcinoma 21 15.1 +- 10.8
  Mucinous carcinoma 2 21.4 +- 4.2
Estrogen receptor status
<10 fmol/mg protein 44 31.3 +- 41.0
>= 10 fmol/mg protein 36 21.4 +- 14.8
*compared with scirrhous carcinoma, P < 0.05; SLX, sialyl Lewisx tumor marker.

Table 3 . . Correlation of serum SLX and sE-selectin with metastasis in cancer bearing patients
Distant metastasis n SLX (U/ml)* sE-selectin (ng/ml)*
Without 72 28.8 +- 18.1[dagger] 50.4 +- 23.3[Dagger]
With 43 87.5 +- 142.1[dagger] 106.2 +- 61.7[Dagger]
Metastatic sites
Bone 14 70.1 +- 58.8 105.8 +- 48.9
Pulmonary 10 47.5 +- 32.8 102.8 +- 75.7
Liver 1 496 86.3
Brain 2 34.6 +- 4.7 102.4 +- 61.8
Bone + Pulmonary 5 66.0 +- 46.3 91.2 +- 33.7
Bone + Liver 2 56.2 +- 36.4 58.6 +- 19.0
Multiple 9 144.1 +- 264.1 133.5 +- 82.8
*mean +- SD, [dagger]P < 0.01, [Dagger]P < 0.001; n, number of patients; SLX, sialyl Lewisx tumor marker; sE-selectin, soluble E-selectin.

Table 4. . Correlation of serum SLX and sE-selectin with metastasis in cancer bearing patients
Distant metastasis n SLX - - + +
    sE-selectin - + - +
Without 24   20 3 1 0
With 43   13 7 4 19
SLX, sialyl Lewisx tumor marker; sE-selectin, soluble E-selectin; -, below cut-off value; +, above cut-off value. The cut-off values were 68 ng/ml for sE-selectin and 38 U/ml for SLX.


Figure 2. Serum levels of SLX in each patient group. BC, breast cancer; b, difference statistically significant at P < 0.01 and c, P < 0.05 by Student's t test. *The cut-off value was set at 38 U/ml for SLX.


Figure 3. Serum concentration of sE-selectin in each patient group. BC, breast cancer; difference statistically significant at: a, P < 0.001, b, P < 0.01and c, P <0.05 by Student's t test. *The cut-off value was set at 68 ng/ml for sE-selectin.

Fig. 2 shows the serum SLX levels in each patient group. The stage IV primary and recurrent cancer groups showed high levels of SLX in comparison with the other patient groups. The stage I, II and III primary cancer groups, however, did not show any significant difference in the serum SLX level as compared with the non-recurrent group, as well as with the benign disease group. When the cancer-bearing patients were divided into two groups on the basis of evidence, and lack thereof, of distant metastases, the mean values of serum SLX were 87.46 U/ml in patients with distant metastases and 28.80 U/ml in those with no evidence of distant metastases, i.e., the SLX level was significantly elevated in the sera of the patients with distant metastases (Table 3 ). Similarly, in the case of E-selectin, the stage IV primary and recurrent cancer groups showed a high level of sE-selectin in comparison with the other patient groups. The mean value of serum sE-selectin in patients with stage IV primary cancer was significantly higher than those with recurrent cancer (Fig. 3 ). The mean value of serum sE-selectin was 106.2 ng/ml in patients with distant metastases and 50.4 ng/ml in those with no evidence of distant metastases (Table 3 ). No significant correlation between the levels of serum SLX or sE-selectin and distant metastatic sites was observed. However, the levels of SLX and sE-selectin of patients with multiple metasatases (>3 sites) were higher than those of patients with metastases in only one or two sites (Table 3 ). This tendency was more pronounced with SLX than with sE-selectin. When the serum levels of SLX and sE-selectin were correlated with evidence of distant metastases in 67 patients with stage III and IV primary or recurrent cancer, it was found that all 19 cases having elevations of both factors had distant metastases. On the other hand, out of 24 cases without distant metastases, 20 cases had no elevation of either (Table 4 ). Fig. 4 shows the changes in thelevels of serum sE-selectin and SLX, corresponding with CEA and CA15-3 levels, in two recurrent breast cancer patients. The levels of these tumor markers were observed to change in response to the state of the disease. Changes in SLX levels almost paralleled those of CEA or CA15-3. However, the elevation of serum sE-selectin levels was detected earlier than those of the other tumor markers, and before detection of distant metastases by physiological examination or by imaging procedures.


DISCUSSION


Figure 4. sE-selectin, SLX, CEA and CA15-3 in the sera of recurrent breast cancer patients. ope, operation; meta, metastasis; rec, recurrence. [diamonds], SLX; [squf], sE-selectin; [utrif] CA15-3; [circle], CEA. The figure shows changes in serum levels of these substances from operation to death in a 52-year-old, stage IIIb case (upper panel) and in a 35-year-old, stage IIIb case (lower panel).

We reported previously that s-Lex and E-selectin were involved in the adhesion of breast cancer cells to endothelial cells (4 ). Thus it is surmised that such adhesion molecules participate in cancer metastasis. Since the advent of monoclonal antibody technology, a great many tumor related antigens have been discovered and are now used widely as tumor markers (18 ). Currently, SLX is employed as a tumor marker, especially in lung, ovarian and gastrointestinal cancers (10 ). The present study has revealed that the level of SLX is also elevated in the sera of patients with metastatic breast cancers. Thus it is felt that SLX can be used as a marker in breast cancer as well. We reported previously from an immunohistochemical study that the expression of type 2 chain carbohydrate antigens, such as s-Lex, was heightened in cancerous compared with noncancerous portions (5 ). In that study, expression of s-Lex was observed not only on the cell surface but also on the cytoplasm of cancer cells. Cell surface substances without transmembranous structure, such as carbohydrate antigens, are separated in cytosol fractions by the extraction method used in this study. We thus determined s-Lex concentrations in cytosol fractions of breast cancer tissues. Cytosol SLX concentration in the cancerous tissues was elevated compared with the noncancerous. Thus, it was found that the synthesis of s-Lex increases in association with the carcinogenesis of breast cancer. Some reports show a correlation between cell surface carbohydrate structure and cellular differentiation (18 -20 ). Our result that the cytosol concentration of SLX in the cancerous tissue of scirrhous carcinoma was significantly lower than in that of papillo-tubular carcinoma or solid tubular carcinoma, may be consistent with these. However, it is possible that the correlation between SLX concentration and histopathological types may reflect the tumor cellularity and contamination with noncancerous cells.

It is widely accepted that unstimulated endothelial cells generally fail to express cell adhesion molecules such as E-selectin. The expression of E-selectin on endothelial cells is enhanced by inflammatory cytokines such as IL-I[beta] and TNF[alpha] (11 ). We reported previously that cancer cells induce the expression of E-selectin on the endothelium directly, or indirectly by releasing cytokines from leukocytes (14 ,15 ). The present study revealed that the sE-selectin level was elevated in the sera of breast cancer patients with distant metastases. This finding supports the proposition that E-selectin is induced on endothelial cells by cancer cells, and has been demonstrated experimentally in vitro. Elevated concentrations of circulating sE-selectin have been reported in studies of numerous disease states, including infections, systematic vasculitis and neoplasma (6 -12 9 ). It is surmised that small amounts of E-selectin are continuously and normally produced on vascular endothelium as it is detectable even in the sera of healthy donors (21 ). There are even reports of weak expression of E-selectin on the endothelial cells of some portal veins in the normal liver (22 ). However, the sE-selectin level becomes elevated in the sera of patients with liver cirrhosis (9 ). From these observations, it can be surmised that the elevation of serum E-selectin levels, which is observed in patients with metastatic cancer, may reflect the destruction of organs, such as the liver, as the result of tumor involvement. However, no differences in the elevated sE-selectin levels, corresponding to the various metastatic tumor sites, were observed in the current study. Thus the elevated levels of serum sE-selectin in patients with cancer is further evidence of its increased synthesis in endothelial cells, and may be a measure of the degree of E-selectin expression induced by cancer cells.

The levels of SLX and sE-selectin were observed to change in response to the state of the disease in recurrent breast cancer patients. The elevation of serum sE-selectin levels was detected earlier than that of the other tumor markers, before detection of distant metastases by physiological examination or imaging procedures, and corresponded with tumor volume. This suggests that serum sE-selectin can be used as a tumor marker with a close correlation to the metastatic state in breast cancer.

Acknowledgements

We would like to express our special thanks to Ms Yoko Nishikawa and Ms Aya Tagashira for their technical assistance, and to TFB Inc. (Tokyo, Japan) and Otsuka Pharmaceutical Co. (Tokushima, Japan) for their kind support in this investigation.

References

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10. Kannagi R, Fukushi Y, Tachikawa T, Noda A, Shin S, Shigeta K et al. Quantitative and qualitative characterization of human cancer-associated serum glycoprotein antigens expressing fucosyl or sialyl- fucosyl type 2 chain polylactosamine. Cancer Res 1986;46:2619-26. MEDLINE Abstract

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14. Narita T, Kawakami-Kimura N, Matsuura N, Hosono J, Kannagi R. Corticosteroids and medroxyprogesterone acetate inhibit the induction of E-selectin on the vascular endothelium by MDA-MB-231 breast cancer cells. Anticancer Res 1995;15:2523-8. MEDLINE Abstract

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22. Nagura H, Koshikawa T, Fukuda Y, Asai J. Hepatic vascular endothelial cells heterogenously express surface antigens associated with monocytes, macrophages and T lymphocytes. Virchows Arch (A) 1986;409:407-16.

Received September 30, 1996; accepted December 27, 1996
For reprints and all correspondence: Tatsuhiko Narita, Laboratory of Experimental Pathology, Aichi Cancer Center Research Institute, 1-1 Kanokoden, Chikusa-ku, Nagoya 464, Japan
Abbreviations: s-Lex, sialyl Lewisx; SLX, (commercial name for) sialyl Lewisx tumor marker; IL-I[beta], interleukin 1[beta]; TNF[alpha], tumor necrotic factor [alpha]; ER, estrogen receptor; EIA, enzyme immunoassay; sE-selectin, soluble E-selectin.

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