Characterization of Cross-Related Antigens of Human Milk Fat Globule Membrane and Breast Tumors Detected by a New Monoclonal Antibody Panel

Dion, Arnold S.; Major, Pierre; Ishida, Masao

doi:10.1007/978-1-4613-1903-0_1

Cited by 5 publications

(13 citation statements)

References 36 publications

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“…To date, numerous antibodies have been developed which have determinant specifici ties residing on high molecular weight MFGM or breast tumor antigens [ 17,18], In this regard, we have found that MA5 and E29 [19] (obtained from Dakopatts, Santa Barbara, Calif.) detect the same antigens on immunoblots, and we are presently monitor ing available antibodies with reference to both antigen and epitope specificities (stud ies in progress). These results, as well as pre vious comparative studies utilizing E29 [20], clearly indicate that MA5 also recognizes highly immunogenic components of the epi thelial membrane antigen complex.…”

Section: Discussionmentioning

confidence: 99%

“…These results, as well as pre vious comparative studies utilizing E29 [20], clearly indicate that MA5 also recognizes highly immunogenic components of the epi thelial membrane antigen complex. In this context, we [17] and others [18] have noted that these antibodies are reactive with carbo hydrate epitopes in most instances and that, by contrast, MAS likely reacts with a peptidyl determinant [17]; i.e. antibody binding was not significantly diminished following desialylation or periodate oxidation [17].…”

Section: Discussionmentioning

confidence: 99%

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Related Glycoproteins from Normal Secretory and Malignant Breast Cells

Ishida¹,

Major²,

Ura³

et al. 1989

Tumor Biol

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Monoclonal antibody MA5 [ 1 ] recognizes an epitope present on the surface and in the cytoplasm of human breast cancer cells [2] and on the human milk fat globule membrane (MFGM). These immunoreactive determinants are found on tumor-associated glycoproteins with apparent molecular weights of 280 and 300 kdaltons, whereas the cross-related milk fat globule membrane antigen appears larger (330 kdaltons). Comparative electrophoretic migration analyses following neuraminidase digestion, as well as differential binding to various lectins, established that these molecules are extensively sialylated, and that the tumor antigens were sialylated to a greater extent than normal antigen. Immunoaffinity purification of this class of differentiation antigens from tumor and MFGM demonstrated similar size distributions, lectin affinities and buoyant densities as their respective crude antigens.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Related Glycoproteins from Normal Secretory and Malignant Breast Cells

Ishida¹,

Major²,

Ura³

et al. 1989

Tumor Biol

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“…J. Cancer (1988), 58, 362-367 363 Antibody production and radiolabelling The production and characterization of monoclonal antibodies MA6 and MA9 have been previously described (Major et al, 1987a;Dion et al, 1987 (Major et al, 1987a); a tumour membrane enriched preparation, MB5 (Major et al, 1987a) (Figure 1). Serum from the normal female LS was used in the dilution of antigen standards because her serum gave the lowest signal (LS) in our control panel of normal sera.…”

Section: Methodsmentioning

confidence: 99%

“…al., 1984;Haynes et al, 1985). Hilkens et al (1986) followed a series of advanced breast cancer patients over a period of one to six months to correlate circulating antigen levels with the clinical course of the disease; the study examined a small sample size.We previously reported the production and characterization of a panel of monoclonal antibodies reactive with components of the EMA complex expressed at high levels in human breast tumours (Major et al, 1987a;Dion et al, 1987). These antibodies react with two high molecular weight glycoproteins expressed in the majority of both primary and metastatic lesions.…”

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Double antibody radioimmunoassay for monitoring metastatic breast cancer

Schecter

Major²,

Kovac³

et al. 1988

Br J Cancer

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Summary We previously reported the production of a panel of murine monoclonal antibodies which recognize glycoproteins abnormally expressed in human breast tumours. Using two of these antibodies, a double antibody radioimmunoassay was designed to quantify levels of these breast tumour marker glycoproteins in serum. Marker levels greater than 28 units were considered abnormal. Using this criterion, 63% and 75% of patients with breast cancer stages I and II, respectively, and 88% of those with metastatic disease were found to have elevated marker levels. Thirteen percent of patients with non-malignant breast disease also had elevated marker levels. Elevated marker levels were also detected in patients with non breast neoplasms. One hundred and eleven women with metastatic disease were followed. Eighty-two percent of those with progressive disease and 73% of those where disease regressed had 20% changes in marker levels. These changes in marker levels preceded by up to 6 months changes in disease state. From these results we conclude that this assay may be useful for monitoring the course of disease in breast cancer patients. al., 1984;Haynes et al., 1985). Hilkens et al. (1986) followed a series of advanced breast cancer patients over a period of one to six months to correlate circulating antigen levels with the clinical course of the disease; the study examined a small sample size.We previously reported the production and characterization of a panel of monoclonal antibodies reactive with components of the EMA complex expressed at high levels in human breast tumours (Major et al., 1987a;Dion et al., 1987). These antibodies react with two high molecular weight glycoproteins expressed in the majority of both primary and metastatic lesions. The panel of antibodies defines six epitopes present on molecules with apparent molecular weights of 300,000 and 280,000 daltons. Immunoblots of sera reveal that identical molecules are present in the circulation of patients with disseminated breast cancer (Major et al., 1987a 2. Then, volumes of 0, 10, 20,..., 90,ul of the above antigen preparation were added to LS normal serum to a final total volume of I00,ul. 3. Finally, 1:4 dilutions of the latter preparation were made using dilution buffer (wash buffer as defined below containing 0.5% bovine albumin). These dilutions were defined as containing 0, 10, 20,..., 90 units (U) of antigen per 50 4u1. Antigen diluted in this manner gave a linear standard curve (Figure 1). Serum from the normal female LS was used in the dilution of antigen standards because her serum gave the lowest signal (LS) in our control panel of normal sera.Patient sera to be assayed were initially diluted 1:4 in buffer; all further dilutions were made in a solution of 3 parts dilution buffer and 1 part LS serum. All incubations were done at 37°C in a humidified chamber. Polyvinylchloride microtitration plates with round bottom wells (Fisher Scientific, Montreal, Canada) were coated with 4 pg per well of antibody MA9 in 50 p1 PBS and allowed to adsorb for 16 ...

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Quantitative dot blot analyses of blood‐group‐related antigens in paired normal and malignant human breast tissues

Ura

Dion

Williams

et al. 1992

Intl Journal of Cancer

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Membranes were prepared from 31 breast-cancer specimens and adjacent mammary tissues, dot-blotted to nitrocellulose paper, and reacted with monoclonal antibodies (MAbs) (A, B, Lewis a, Lewis b, sialylated Lewis a, Lewis x, and Lewis y) and lectins (Ulex europaeus, peanut agglutinin) having various blood-group specificities. The expression of epithelial membrane antigen was assayed with MAb MA5. The ratio of breast-cancer to normal mammary membrane preparations (C/N ratios) of these reagents was measured by densitometric scanning. We observed a decrease in the levels of A, B, Lewis a, Lewis b, sialylated Lewis a, and Lewis y antigens and an increase of Lewis x, T, and MA5-reactive determinants in breast cancers. The incidence of incompatible A, as well as A and B, antigens was demonstrated for 2 patients of blood group B and O respectively. When the receptor content was plotted against the C/N ratio of these various reagents, a significant inverse relationship between the C/N ratio of Lewis x antigen and estrogen (ER) and progesterone receptor (PR) content was observed in breast cancers. The mean C/N ratio of Lewis x antigen was significantly higher in the ER-negative/PR-negative (ER-/PR-; 2.33 +/- 1.17), as compared with the ER-positive/PR-positive (ER+/PR+; 0.97 +/- 0.80). According to these observations, Lewis x antigen expression may be influenced by hormonal stimuli such as estrogen and progesterone.

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Characterization of Cross-Related Antigens of Human Milk Fat Globule Membrane and Breast Tumors Detected by a New Monoclonal Antibody Panel

Cited by 5 publications

References 36 publications

Related Glycoproteins from Normal Secretory and Malignant Breast Cells

Related Glycoproteins from Normal Secretory and Malignant Breast Cells

Double antibody radioimmunoassay for monitoring metastatic breast cancer

Quantitative dot blot analyses of blood‐group‐related antigens in paired normal and malignant human breast tissues

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