HELIX POMATIA LECTIN-BINDING AND PREDICTIVE VALUE IN BREAST-CANCER

A number of studies have shown that altered cellular glycosylation, as detected by binding of Helix pomatia lectin to paraffin sections, is associated with metastatic disease and consequent poor patient prognosis in breast and other cancers. In a 24-year retrospective study, sections of 373 primary breast cancers were stained for binding of the lectin using two different histochemical techniques: a direct method (using peroxidase-conjugated lectin) and an indirect method (using native, unconjugated lectin). Similar percentages of cases were positive (79%) and negative (21%) for lectin binding with either technique, but there was enormous inconsistency when individual cases were examined. A total of 38/373 (10.2%) cases that were negative by the indirect method were positive by the direct method, and 37/373 (9.9%) cases that were negative by the direct method were positive by the indirect method. Life tables calculated for lectin staining vs nonstaining cases showed a very strong correlation between lectin binding and long-term survival (p < 0.0001) when staining was performed by the indirect method, but only very weak correlation with prognosis (p < 0.03, borderline significance) when the direct technique was employed. SDS-PAGE revealed that there were differences in breast cancer glycoproteins recognized by native lectin and peroxidase-conjugated lectin immobilized on Sepharose 4B affinity beads. Helix pomatia lectin binding appears to be an intriguing and potentially valuable marker of biological behavior in breast cancer. This study emphasizes the importance of selecting an appropriate immunohistochemical technique for its visualization.

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NM23 EXPRESSION VERSUS HELIX-POMATIA LECTIN-BINDING IN HUMAN BREAST-CANCER METASTASES

International Journal of Oncology ◽

10.3892/ijo.4.6.1353 ◽

1994 ◽

Author(s):

M NOGUCHI ◽

M EARASHI ◽

I OHNISHI ◽

K KINOSHITA ◽

M THOMAS ◽

...

Keyword(s):

Breast Cancer ◽

Human Breast Cancer ◽

Lectin Binding ◽

Helix Pomatia ◽

Human Breast ◽

Breast Cancer Metastases ◽

Cancer Metastases ◽

Helix Pomatia Lectin

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DNA ploidy and helix pomatia lectin binding as predictors of regional lymph node metastases and prognostic factors in breast cancer

Breast Cancer Research and Treatment ◽

10.1007/bf00682701 ◽

1993 ◽

Vol 26 (1) ◽

pp. 67-75 ◽

Cited By ~ 7

Author(s):

Masakuni Noguchi ◽

Michael Thomas ◽

Hirohisa Kitagawa ◽

Kazuo Kinishita ◽

Shinich Kinami ◽

...

Keyword(s):

Breast Cancer ◽

Prognostic Factors ◽

Lymph Node ◽

Lymph Node Metastases ◽

Dna Ploidy ◽

Regional Lymph Node ◽

Lectin Binding ◽

Helix Pomatia ◽

Node Metastases ◽

Helix Pomatia Lectin

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HELIX-POMATIA LECTIN AND C-ERBB-2 EXPRESSION VERSUS AXILLARY AND INTERNAL MAMMARY LYMPH-NODE METASTASES IN PROGNOSTIC ASSESSMENT OF BREAST-CANCER

Oncology Reports ◽

10.3892/or.1.1.155 ◽

1994 ◽

Author(s):

M NOGUCHI ◽

M THOMAS ◽

H KITAGAWA ◽

K KINOSHITA ◽

M EARASHI ◽

...

Keyword(s):

Breast Cancer ◽

Lymph Node ◽

Lymph Node Metastases ◽

Helix Pomatia ◽

Internal Mammary Lymph Node ◽

Prognostic Assessment ◽

Internal Mammary ◽

Node Metastases ◽

Helix Pomatia Lectin

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Lectin-binding properties of human breast cancer cell lines and human milk with particular reference to Helix pomatia agglutinin.

Journal of Histochemistry & Cytochemistry ◽

10.1177/43.3.7868857 ◽

1995 ◽

Vol 43 (3) ◽

pp. 275-281 ◽

Cited By ~ 25

Author(s):

U Schumacher ◽

E Adam ◽

S A Brooks ◽

A J Leathem

Keyword(s):

Breast Cancer ◽

Cell Lines ◽

Binding Sites ◽

Lectin Binding ◽

Helix Pomatia ◽

Breast Cancer Cell Lines ◽

Human Breast ◽

Membrane Glycoproteins ◽

Tissue Sections ◽

Helix Pomatia Agglutinin

Several studies have shown binding of a variety of lectins to breast cancer cells in tissue sections. In particular, binding of the lectin from the Roman snail, Helix pomatia agglutinin (HPA), to breast cancer cells is linked with a poor prognosis. The molecular basis for lectin binding to metastatic breast cancers is not known. To elucidate this in a model system, lectin-binding patterns of seven human breast cancer cell lines were investigated, their cell membranes were isolated, and HPA binding was assessed. In addition, the influence of fixation and processing on lectin-binding sites was also investigated. Binding of lectins to the tumor cells was very heterogeneous between and within the different cell lines and was influenced by fixation and processing. However, some cell lines showed HPA-binding sites both in vivo and in tissue sections. Analysis of the isolated cell membrane glycoproteins from these cell lines on Western blots revealed that HPA can bind to several membrane glycoproteins. In contrast, human milk shows only one major milk glycoprotein that is HPA-positive. Therefore, a switch in glycosylation appears to be taking place during the transformation to a metastatic phenotype.

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