The prognostic value of tumor-associated carbohydrate structures correlated with gene amplifications in human breast carcinomas

Fukutomi, Takashi; Hirohashi, Setsuo; Tsuda, Hitoshi; Nanasawa, Takeshi; Yamamoto, Hiroshi; Itabashi, Michio; Shimosato, Yukío

doi:10.1007/bf02470985

Cited by 17 publications

(10 citation statements)

References 20 publications

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“…Although it is inappropriate to make generalisations regarding cell characteristics involved in a complex process such as metastasis formation on the basis of correlations observed in one model system, our findings do support the recent retrospective studies in human cancers (Leathem & Brooks, 1987;Nishiyama et al, 1987;Springer, 1989;Brooks & Leathem, 1991;Fukutomi et al, 1991;Kakeji et al, 1991;Schumacher et al, 1992;Shiraishi et al, 1992) implicating a role for HPA-binding glycoconjugates in site-specific metastasis development.…”

Section: Discussionsupporting

confidence: 73%

“…In particular the N-acetyl-D-galactosamine-binding lectins (e.g. Helix pomatia agglutinin or HPA) have been correlated with poor prognosis and metastatic development in patients with malignant disease of the bladder (Nishiyama et al, 1987), breast (Leathem & Brooks, 1987;Springer, 1989;Brooks & Leathem, 1991;Fukutomi et al, 1991;Schumacher et al, 1992), gastrointestinal tract (Kakeji et al, 1991) and prostate (Shiraishi et al, 1992). Most experimental studies on the role of membrane glyconjugates in the metastatic process have been performed in syngeneic rodent tumour systems (Tao & Burger, 1977;Dennis et al, 1981;Finne et al, 1989;Hagmar et al, 1990).…”

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confidence: 99%

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Helix pomatia agglutinin binding in human tumour cell lines: correlation with pulmonary metastases in nude mice

Kjønniksen

Rye²,

Fodstad³

1994

Br J Cancer

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Summary The extent of lectin binding by three human melanoma (LOX, FEMX-I and SESX) and two sarcoma lines (MHMX and OHSX) was related to their potential for experimental metastasis formation in athymic nude mice. The Helix pomatia agglutinin (HPA), which recognises the N-acetyl-D-galactosamine ligand, showed differential binding to the cell lines in a manner that correlated with their ability to give lung colonies after i.v. injection in the mice (P<0.005). The degree of HPA binding and lung colony formation of the cell lines studied was ranked in the following order, LOX> MHMX> OHSX> SESX > FEMX-I. Similar patterns were not observed with the other lectins used in this study (WGA, Con A, PNA and UEA-I). The high HPA reacting LOX melanoma line shows extensive pulmonary metastatic formation with no extrapulmonary colonies, whereas the low HPA reacting FEMX-I cells give only extrapulmonary metastases with no detectable colonies in the lungs. Precoating of tumour cells with HPA prior to injection did not reduce the ability of cells to give pulmonary metastases, suggesting that the HPA epitope was not functionally associated with the pulmonary metastatic potential observed in nude mice. These findings support recent human studies of a correlation between HPA binding and incidence of metastasis, however, our data indicate that there is no causal relationship. Further analyses are required to identify the specific HPA-binding glycoconjugates that may be involved.Cancer cells often display aberrant glycosylation of surface membrane proteins and lipids (Hakomori & Kannagi, 1983;Reading & Hutchins, 1985). The altered structure or expression of these sugar-containing molecules on malignant cells is thought to be important for some of the events leading to the formation of metastasis (Nicolson, 1984) (Leathem & Brooks, 1987;Springer, 1989;Brooks & Leathem, 1991;Fukutomi et al., 1991;Schumacher et al., 1992), gastrointestinal tract (Kakeji et al., 1991) and prostate (Shiraishi et al., 1992). Most experimental studies on the role of membrane glyconjugates in the metastatic process have been performed in syngeneic rodent tumour systems (Tao & Burger, 1977;Dennis et al., 1981;Finne et al., 1989;Hagmar et al., 1990). In the present study we have used human melanoma and sarcoma cell lines in nude mice to examine whether a relationship between lectin binding and metastatic potential could be detected. Materials and methods AnimalsCongenitally nude mice (Balb/c) were bred and maintained as previously described (Fodstad et al., 1988a). Animals (4-6 weeks of age) of both sexes were used. (Fodstad et al., 1986) and the MHMX unclassified sarcoma. The cell lines were all established from biopsies of patients at the Norwegian Radium Hospital. The cells were cultured as monolayers and as xenografts in nude mice. The monolayer cultures were maintained at 37°C in RPMI-1640 medium (Gibco, Paisley, UK) supplemented with 10% fetal calf serum (Serva, Heidelberg, Germany), 1,000 IU ml-' penicillin, 1I00 lg ml-' streptomycin and 2 mg I' L-glutam...

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Section: Discussionsupporting

confidence: 73%

mentioning

confidence: 99%

Helix pomatia agglutinin binding in human tumour cell lines: correlation with pulmonary metastases in nude mice

Kjønniksen

Rye²,

Fodstad³

1994

Br J Cancer

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“…The lectin from Helix pomatia (HPA) has emerged as an interesting marker of altered glycosylation in cancer, where expression of glycoconjugates recognised by the lectin appear to be associated with poor patient prognosis (see Mitchell and Schumacher, 1999;Brooks, 2000 for review). This association has been reported in breast cancer (Fenlon et al, 1987;Leathem and Brooks, 1987;Fukutomi et al, 1989Fukutomi et al, , 1991Alam et al, 1990;Noguchi et al, 1993aNoguchi et al, , 1993bNoguchi et al, , 1994Thomas et al, 1993), and also in adenocarcinomas at other common sites, including gastric cancer (Macartney, 1986;Kakeji et al, 1991;Maehara et al, 1995;Okuyama et al, 1998), carcinoma of the oesophagus (Yoshida et al, 1993(Yoshida et al, , 1994a colorectal carcinoma (Ikeda et al, 1994;Schumacher MD et al, 1994a, carcinoma of the thyroid (Sasano et al, 1989) and prostate cancer (Shiraishi et al, 1992). Only one published study has failed to confirm this relationship (Gusterson et al, 1993), and it appears that this may have been the fault of the inappropriate methodology employed .…”

supporting

confidence: 57%

GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane

2001

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Summary Over-expression of N-acetylgalactosamine glycoproteins as detected by binding of the lectin from Helix pomatia (HPA), is associated with metastatic competence and poor patient prognosis in a range of human adenocarcinomas. These glycoproteins remain poorly characterised, and their functional role has yet to be elucidated. This study describes characterisation of a range of human breast/breast cancer cell lines for the expression of the N-acetylgalactosaminylated glycoproteins of interest, and their comparison with normal breast epithelium and a range of clinical breast carcinoma samples. Confocal and light microscopy studies revealed cytochemical HPA-binding patterns consistent with a fundamental disruption in normal glycobiosynthetic pathways attending increasing metastatic potential. We report the most complete comparative analysis of HPA-binding ligands from cultured breast cells, clinical breast carcinoma samples and normal breast epithelium to date. Lectin blotting identified 11 major HPA-binding glycoprotein bands common to both clinical tumour samples and breast cell lines and 6 of these bands were also expressed by samples of normal breast epithelium, albeit at much lower levels. Moreover, very marked quantitative but not qualitative differences in levels of expression consistent with metastatic capability were noted.

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“…These data prompted us to determine the molecular events related to HPA-positive gastric cancers. A close relation between HPA staining and amplification of the c-myc gene or c-erbB-2 gene has been noted in human breast cancer tissues (Fukutomi et al, 1991;Thomas et al, 1993). In the present study, we clarified the correlations between HPA staining of cancer cells, abnormality of the p53 gene and the prolferating activity determined by PCNA labelling in gastric cancer.…”

Section: Survival Ratementioning

confidence: 80%

A tumour-associated cell-surface glycoprotein accompanying p53 overexpression and higher growth potential for gastric cancer

Maehara

Okuyama²,

Kakeji³

et al. 1995

Br J Cancer

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S aryTumour-associated cell-surface glycoprotein is associated with tumour progression in gastric cancer. We investigated the biological significance of tumour-associated cell-surface glycoprotein, determined by the binding of Helix pomatia agglutinin (HPA), with regrd to survival time and to the malignant potential of cancer cells in serosally invasive gastric cancer in 119 patients. HPA was positively stained in 75 of 119 patients (63.0%) with gastric cancer with serosal invasion. In patients with HPA-positive tissue, the tumour was larger than in HPA-negative cases and was frequently located in the middle third of the stomach. The incidence of lymph node metastasis was higher than in patients with HPA-negative tissue. There were no differences between the cases staining negatively and positively with HPA with respect to the other factors eained. Gastric cancer tissues with HPA-positive staining revealed a higher positive rate of abnormal p53 staining and a higher concentration of proliferating cell nuclear antigen (PCNA) labelling. The survival time of the patients with HPA positive staining was shorter than for those whose tissues were HPA negative. Thus, tumour-associated cell-surface glycoprotein is apparently closely related to the malignant potential of serosally invasive gastnc cancer.

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The prognostic value of tumor-associated carbohydrate structures correlated with gene amplifications in human breast carcinomas

Cited by 17 publications

References 20 publications

Helix pomatia agglutinin binding in human tumour cell lines: correlation with pulmonary metastases in nude mice

Helix pomatia agglutinin binding in human tumour cell lines: correlation with pulmonary metastases in nude mice

GalNAc glycoprotein expression by breast cell lines, primary breast cancer and normal breast epithelial membrane

A tumour-associated cell-surface glycoprotein accompanying p53 overexpression and higher growth potential for gastric cancer

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